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vesicle-associated membrane protein-2 + H2O
?
-
-
-
?
25 kDa synaptosome-associated protein + H2O
?
-
-
-
-
?
25-kDa synaptosome-associated protein + H2O
?
-
i.e. SNAP-25
-
-
?
5-carboxyfluorescein-TRIDEANQRATK-Dabcyl-6-aminohexanoic acid-CONH2 + H2O
?
-
-
-
-
?
5-carboxyfluorescein-TRIDEANQRATK-Dabcyl-CONH2 + H2O
?
-
-
-
-
?
5-carboxyfluorescein-TRIDEANQRATK-Dabcyl-norleucine-CONH2 + H2O
?
-
-
-
-
?
50-mer synaptobrevin peptide + H2O
?
-
[Pya88]S39-88
-
?
7-hydroxy-4-methylcoumarin-3-acetyl-TRIDEANQRATK-Dabcyl-6-aminohexanoic acid-CONH2 + H2O
?
-
-
-
-
?
7-hydroxy-4-methylcoumarin-3-acetyl-TRIDEANQRATK-Dabcyl-CONH2 + H2O
?
-
-
-
-
?
7-hydroxy-4-methylcoumarin-3-acetyl-TRIDEANQRATK-Dabcyl-norleucine-CONH2 + H2O
?
-
-
-
-
?
Ac-ERDQKLSELDDRADALQAG-(7-methoxy-4-methylcoumaryl)Lys-SQ-diaminopropionic acid(2,4-dinitrophenyl)-ESSAAKLKRKYWWKNLK-NH2 + H2O
?
-
development of a FRET peptide substrate, based on the native substrate binding site of human VAMP2 residues 55-94, and evaluation for enzymatic cleavage by the BoNT/B light chain protease, overview. For the synthesis position 74 is mutated to Lys in order to couple 7-methoxycoumarin-4-acetic acid, MCA, to the amine via an amide bond, in part to aid in the flexibility of the MCA to allow free rotation away from the active site and not affect binding and/or cleavage of the peptide. At position 77 the native Phe is replaced with the unnatural amino acid diaminopropionic acid to facilitate coupling of 2,4-dinitrophenyl to the peptide. Thr79 is mutated to a serine increasing kcat 2fold without affecting Km
-
-
?
Ac-IIGNLRH(Nle)ALD(Nle)GNEIDTQNRQIDRI(Nle)EKADSNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)L-NH2 + H2O
Ac-IIGNLRH(Nle)ALD(Nle)GNEIDTQNRQIDRI(Nle)EKADSNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)L-NH2
-
i.e. peptide PL51, a SNAP-25-NH2in which all methionines were replaced by nonoxidizable Nle
-
-
?
Ac-IIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)L-NH2 + H2O
Ac-IIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)L-NH2
-
i.e. peptide PL50, a SNAP-25-NH2 acetylated at positions 156 to 203 [(pNO2-Phe)197, (1-pyrenylalanine)200, Nle202]
-
-
?
Ac-KSDSNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)LGSG-NH2 + H2O
Ac-KSDSNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)LGSG-NH2
-
-
-
-
?
Ac-RGSNKPKIDAGNQRATRXLGGR-NH2 + H2O
Ac-RGSNKPKIDAGNQR + ATRXLGGR-NH2
-
-
-
?
Ac-SNKTIDEANQRATKML-NH2 + H2O
Ac-SNKTIDEANQ + RATKML-NH2
-
synaptosomal protein
-
?
Ac-SNKTRIDCANQRATKML-NH2 + H2O
Ac-SNKTRIDCANQ + RATKML-NH2
-
-
-
?
Ac-SNKTRIDEAN(1-pyrenylalanine)RA(pNO2-Phe)K(Nle)L-NH2 + H2O
Ac-SNKTRIDEAN(1-pyrenylalanine) + RA(pNO2-Phe)K(Nle)L-NH2
-
-
-
-
?
Ac-SNKTRIDEAN(pNO2-Phe)RA(1-pyrenylalanine)K(Nle)L-NH2 + H2O
Ac-SNKTRIDEAN(pNO2-Phe) + RA(1-pyrenylalanine)K(Nle)L-NH2
-
-
-
-
?
Ac-SNKTRIDEANQRATK(Nle)L-NH2 + H2O
Ac-SNKTRIDEANQ + RATK(Nle)L-NH2
-
-
-
-
?
Ac-SNKTRIDEANQRATKML-NH2 + H2O
Ac-SNKTRIDEANQ + RATKML-NH2
-
-
-
?
Ac-SNKTRIDEANQRCTKML-NH2 + H2O
Ac-SNKTRIDEANQ + RCTKML-NH2
-
-
-
?
Ac-SNKTRIDECNQRATKML + H2O
?
-
-
-
-
?
Ac-SNKTRIDECNQRATKML-NH2 + H2O
Ac-SNKTRIDECNQ + RATKML-NH2
-
-
-
?
biotin-KGSNRTRIDQGNQRATRXLGGK-biotin + H2O
?
-
the catalytic activity resides on the light chains of the toxin molecule
-
-
?
LQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDD + H2O
LQQTQAQVDEVVDI + MRVNVDKVLERDQK + LSELDD
-
the vesicle-associated membrane protein, VAMP, sequence-derived peptide is a substrate of BoNT serotype D light chain
-
-
?
LSELDDRADALQAGASQFETSAAKLKRKYWWKNLK + H2O
LSELDDRADALQAGASQ + FETSAAKLKRKYWWKNLK
-
the vesicle-associated membrane protein, VAMP, sequence-derived peptide is a substrate of BoNT serotype B light chain
-
-
?
membrane-anchored SNARE + H2O
?
-
host membrane-anchored SNARE, proteolytically cleaved by BoNT/C
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
neuronal proteinSNAP-25 + H2O
?
-
-
-
?
Nutide + H2O
?
-
i.e. FITC(bA)T(dR)IDQANQRAT(K/DABCYL)(Nle)-amide
-
-
?
Proteins of neuroexocytosis apparatus + H2O
?
-
-
-
-
?
Recombinant glutathione S-methyltransferase VAMP-2 fusion protein + H2O
Hydrolyzed recombinant glutathione S-methyltransferase VAMP-2 fusion protein
-
-
2 proteolytic fragments, MW 36000 and MW 6000
?
Sb-Snc2p fusion protein + H2O
?
-
a recombinant chimeric SNARE protein where a portion of neuronal synaptobrevin, Sb, is fused to Snc2p, a Sb ortholog required for protein secretion from yeast cells
-
-
?
SNAP-23 + H2O
?
-
a nonneuronal SNARE protein, that mediates vesicle-plasma membrane fusion processes, including secretion of airway mucus, antibody, insulin, gastric acids, and ions. SNAP23 is cleaved by an engineered BoNT/E light chain, LC/E K224D. Molecular modeling of the enzyme-substrate complex using the crystal structure of LC/E, Protein Data Bank ID 3d3x, overview
-
-
?
SNAP-25 peptide (141-206) + H2O
?
-
the minimal size of SNAP-25 known to retain full activity as a BoNT/A substrate is the C-terminal 66-mer peptide, residues 141-206, with both exosites
-
-
?
SNAP-25-derived peptide + H2O
?
-
i.e. HA-tagged SNAP25(141-206) or HA-tagged mutant SNAP25(141-206)-R198A, substrate of light chains of BoNT/A1, BoNT/A2, BoNT/A3, and BoNT/A4
-
-
?
SNAP25(187-203) + H2O
?
-
i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, substrate fragmnent containing residues 87-203
-
-
?
SNAPEtide + H2O
?
substrate for subtype BoNT/E
-
-
?
SNAPtide 520 + H2O
?
-
-
-
-
?
SNAPtide 521 + H2O
?
-
-
-
-
?
SNARE-protein + H2O
?
-
soluble NSF-attachment protein receptor
-
?
SNKTRIDEAAQRATKML + H2O
SNKTRIDEAAQ + RATKML
-
synthetic peptide substrate
-
?
SNKTRIDEANBRATKML + H2O
SNKTRIDEANB + RATKML
-
synthetic peptide substrate
-
?
SNKTRIDEANNRATKML + H2O
SNKTRIDEANN + RATKML
-
synthetic peptide substrate
-
?
SNKTRIDEANQRABKML + H2O
SNKTRIDEANQ + RABKML
-
synthetic peptide substrate
-
?
SNKTRIDEANQRASKML + H2O
SNKTRIDEANQ + RASKML
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATAML + H2O
SNKTRIDEANQ + RATAML
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATK + H2O
SNKTRIDEANQ + RATK
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKAL + H2O
SNKTRIDEANQ + RATKAL
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKM + H2O
SNKTRIDEANQ + RATKM
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKML + H2O
SNKTRIDEANQ + RATKML
SNKTRIDEANQRATKXL + H2O
SNKTRIDEANQ + RATKXL
-
synthetic peptide substrate
-
?
SNKTRIDEANQRBTKML + H2O
SNKTRIDEANQ + RBTKML
-
synthetic peptide substrate
-
?
SNKTRIDEBNQRATKML + H2O
SNKTRIDEBNQ + RATKML
-
synthetic peptide substrate
-
?
SNKTRIDQANQRATKML + H2O
?
-
-
-
-
?
SNKTRINEAAQRATKML + H2O
SNKTRINEAAQ + RATKML
-
synthetic peptide substrate
-
?
SNKTRINEANQRATKML + H2O
?
-
-
-
-
?
SNRTRIDEANK(Dnp)RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML + H2O
SNRTRIDEANK(Dnp) + RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
synaptobrevin-2 + H2O
?
-
cleaves in the same location as that cleaved by BoNT/F proteolytic F toxin of Clostridium botulinum
-
-
?
Synaptosome-associated protein + H2O
?
-
i.e. SNAP 25, protein of presynaptic membrane
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
synaptosome-associated protein SNAP-25 + H2O
?
synaptosome-associated protein SNAP-25 + H2O
hydrolyzed synaptosome-associated protein SNAP-25
-
-
-
-
?
TSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADAL + H2O
TSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ + KLSELDDRADAL
-
-
-
?
VAMP-1 + H2O
?
-
subtype BoNT/D does not cleave human VAMP-1 efficiently
-
-
?
VAMP2 peptide + H2O
?
-
a synthetic peptide substrate representing amino acid residues 60-94 of the intracellular vesicle associated membrane protein 2, i.e. VAMP2, recombinant GST fusion protein and commercial preparation as substrates with equal activity for BONT/B
-
-
?
vesicle-associated membrane protein + H2O
?
-
-
-
-
?
vesicle-associated membrane protein VAMP + H2O
?
-
BoNT F cleaves VAMP between residues Q58 and K59. The minimum substrate is a peptide containing VAMP residues 32-65, which includes only one of the two VAMP structural motifs thought to be required for botulinum substrate recognition. BoNT F exhibits a strict requirement for residues D57 (P2), K59 (P1'), and L60 (P2'), but peptides containing substitutions for R56 (P3), Q58 (P1), and S61 (P3') are cleaved. Therefore, the P2, P1', and P2'?residues of VAMP are of paramount importance for BoNT F substrate recognition near the scissile bond
-
-
?
vesicle-associated membrane protein VAMP-2 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-1 + H2O
?
vesicle-associated membrane protein-2 + H2O
?
vesicle-associated membrane protein-2 mutant D51A + H2O
?
-
the enzyme cleaves the mutant substrate with about 10fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant E41A + H2O
?
-
the enzyme cleaves the mutant substrate with about 80fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant E55A + H2O
?
-
the enzyme cleaves the mutant substrate with about 750fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant K52A + H2O
?
-
the enzyme cleaves the mutant substrate with about 20fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant N49A + H2O
?
-
the enzyme cleaves the mutant substrate with about 10fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant Q58A + H2O
?
-
the enzyme cleaves the mutant substrate with about 25fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant R31A + H2O
?
-
the enzyme cleaves the mutant substrate with about 20fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant R56A + H2O
?
-
the enzyme cleaves the mutant substrate with about 4000fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-2 mutant V50A + H2O
?
-
the enzyme cleaves the mutant substrate with about 50fold lower efficiency compared to the wild type substrate
-
-
?
vesicle-associated membrane protein-3 + H2O
?
vesicle-associated membrane protein-4 + H2O
?
vesicle-associated membrane protein-5 + H2O
?
additional information
?
-
VAMP + H2O
?
i.e. vesicle-associated membrane protein/synaptobrevin
-
-
?
VAMP + H2O
?
i.e. vesicle-associated membrane protein/synaptobrevin, activity with substrate fragments and mechanism of substrate recognition of BoNT F, overview. Arg133 and Arg171, which form part of two separate exosites, are crucial for substrate binding and catalysis. In exosite 2, BoNT F Arg133 has a dominant role in allowing docking of the V1-SNARE motif, by interacting with the main chain of VAMP Val43, the side chain of VAMP Glu41 and with a water that interacts with other main chain residues of VAMP. The VAMP E41A mutant is 470% cleavage resistant, as compared to the native VAMP
-
-
?
cytosolic SNARE + H2O
?
-
host cytosolic SNARE, i.e. soluble NSF attachment protein receptor, a central helical protein-conducting channel, which chaperones the protease across host endosomes, modelling, overview. Sequence-specific claveage by the endoprotease activity of the BoNT light chains
-
-
?
cytosolic SNARE + H2O
?
-
host cytosolic SNARE, i.e. soluble NSF attachment protein receptor, a central helical protein-conducting channel, which chaperones the protease across host endosomes, modelling, overview. Sequence-specific claveage by the endosprotease activity of the BoNT light chains. Enzyme-substrate complex, overview
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
P10845
-
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
-
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
-
neurotoxin binds specifically to nerve cells, botulin neurotoxin-receptors are located on the motor neuron plasmalemma at neuromuscular junctions, neurotoxin binds via protein and lipid interaction, after binding it is internalized inside vesicles of unknown nature
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
-
involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction
-
-
?
Neuroexocytosis multi-subunit complex + H2O
?
-
causing flaccid paralysis, in contrast to spastic paralysis caused by EC 3.4.24.68, three functionally distinct domains: domain L blocks neuroexocytosis, domain HN governs cell penetration, domain HC responsible for neurospecific binding
-
-
?
SNAP-25 + H2O
?
-
-
-
?
SNAP-25 + H2O
?
-
-
-
-
?
SNAP-25 + H2O
?
-
-
-
-
?
SNAP-25 + H2O
?
P10845
-
-
-
?
SNAP-25 + H2O
?
A5HZZ9
-
-
-
?
SNAP-25 + H2O
?
-
synaptosomal associated protein
-
?
SNAP-25 + H2O
?
-
synaptosomal-associated protein
-
?
SNAP-25 + H2O
?
-
synaptosome associated protein
-
?
SNAP-25 + H2O
?
-
mammalian synaptosome associated protein
-
?
SNAP-25 + H2O
?
P10845
BoNT/A-LC is a Zn(II)-dependent metalloprotease that blocks the release of acetylcholine at the neuromuscular junction by cleaving SNAP-25, one of the SNARE proteins required for exocytosis
-
-
?
SNAP-25 + H2O
?
-
i.e. synaptosomal associated protein of 25 kDa
-
-
?
SNAP-25 + H2O
?
P10845
i.e. synaptosomal associated protein of 25 kDa
-
-
?
SNAP-25 + H2O
?
serotypes BoNT/A and BoNT/E cleave SNAP-25 at distinct sites, BoNT/E blocks neurotransmission faster and more potently
-
-
?
SNAP-25 + H2O
?
-
the potent botulinum neurotoxin inhibits neurotransmitter release at cholinergic nerve terminals, causing a descending flaccid paralysis characteristic of the disease botulism
-
-
?
SNAP-25 + H2O
?
-
i.e. synaptosomal associated protein of 25 kDa, all botulinus neurotoxin serotypes cleave the substrate at a unique peptide bond, BoNT/A cleaves SNAP-25 between residues Gln197 and Arg198. Phe194, Ile161, and Asp370 form the S1' subsite responsible for binding the P1' arginine side chain of SNAP-25, overview
-
-
?
SNAP-25 + H2O
?
-
i.e. synaptosomal associated protein of 25 kDa, human substrate, substrate peptide fragment products, overview
-
-
?
SNAP-25 + H2O
?
-
serotype BoNT/C1-LC exhibits dual specificity toward both syntaxin and SNAP-25, in contrast to other serotypes, due to a distinct pocket S1' near the active site likely achieves the correct register for the cleavage site by only allowing Ala as the P1' residue for both SNAP-25 and syntaxin, activity of the serotype C enzyme BoNT/C1-LC with diverse SNAp-25 substrate mutants, overview
-
-
?
SNAP-25 + H2O
?
substrate is a recombinant GFP-SNAP-25-(134206)-His6 fusion protein
-
-
?
SNAP-25 + H2O
?
-
a neuronal SNARE protein
-
-
?
SNAP-25 + H2O
?
-
i.e. 25 kDa synaptosome-associated protein
-
-
?
SNAP-25 + H2O
?
-
i.e. 25 kDa synaptosome-associated protein, BoNT/A requires two extended exosites for optimal substrate binding and recognition of its intracellular target SNAP-25
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosomal-associated protein
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosomal-associated protein, substrate of BoNT/A
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein
-
-
?
SNAP-25 + H2O
?
P10845
i.e. 25-kDa synaptosome-associated protein
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, a substrate of BoNT/A light chain
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, BoNT/A
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, is involved in acetylcholine release at the neuromuscular junction
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, substrate of BoNT/A, /E, and /C
-
-
?
SNAP-25 + H2O
?
-
i.e. synaptosome-associated protein of 25 kDa, a plasma membrane-associated protein, proteolytically cleaved by BoNT types A, C, and E
-
-
?
SNAP-25 + H2O
?
-
a neuronal SNARE protein, cleaved by an engineered BoNT/E light chain, LC/E K224D
-
-
?
SNAP-25 + H2O
?
-
i.e. 25 kDa synaptosomal-associated protein, substrate of BoNT serotypes A and E
-
-
?
SNAP-25 + H2O
?
-
i.e. 25 kDa synaptosome-associated protein, substrate of BoNT/A, /E, and /C
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, design and construction of a lab-on-a-chip for the in vitro detection of BoNT-A activity using an assay that measures cleavage of the fluorescence-labeled peptide substrate specific for BoNT-A by the toxin light chain, detection by Foerster resonance energy transfer, FRET, fluorescence, method development and evaluation, overview. The peptide substrate is labeled with internally labeled with the FRET pair fluorescein-thiocarbamoyl, FITC, and 4-(dimethyla-minoazo)benzene-4-carboxylic acid, DABCYL, or with FITC only for positive control
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, development of a BoNT/A-specific assay method, overview. Usage of BoNT/A cleavage-sensitive antibodies that only interact with full-length SNAP-25, the molecular target of the BoNT/A serotype. These antibodies exhibit high specificity for full-length SNAP-25, allowing the BoNT/A-mediated proteolysis of this protein to be measured in diverse assay formats, e.g. ELISA and immunofluorescent assay methods, detailed overview
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, substrate of light chains of BoNT/A1, BoNT/A2, BoNT/A3, and BoNT/A4
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, the Michaelis complex involves an extensive network of binding interactions ranging from the active site to the opposite surface of the BoNT/A. In the complex, the N-terminal residues of SNAP-25 147-167 form an alpha-helix, imbedded in the rear surface of BoNT/A while the C-terminal residues 201-204 form a distorted beta-strand, and the spanning residues are mostly extended
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein, truncated version of SNAP-25
-
-
?
SNAP-25 + H2O
?
-
i.e. 25-kDa synaptosome-associated protein. The BoNT/E-truncated C-terminal peptide of SNAP-25 is CDMGNEIDTQNRQIDR
-
-
?
SNAP-25 + H2O
?
-
17-residue C-terminal peptide corresponding to residue 187-203 of SNAP-25
-
-
?
SNAP-25 + H2O
?
-
cleaved by the light chains of subtypes BoNT/A and BoNT/E
-
-
?
SNAP25 + H2O
?
-
i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, the enzyme cleaves SNARE proteins, i.e. SNAP receptor proteins, to elicit flaccid paralysis by inhibiting neurotransmitter-carrying vesicle fusion to the plasma membrane of peripheral neurons, overview
-
-
?
SNAP25 + H2O
?
-
i.e. synaptosomal-associated protein of 25 kDa
-
-
?
SNAP25 + H2O
?
-
i.e. synaptosome-associated protein of 25 kDa, located at the host synaptic membrane, serotype E toxin cleaving SNAP25 prevents assembly of the synaptic fusion complex and therefore the fusion of the acetylcholine-containing vesicle and the synaptic membrane
-
-
?
SNAP25 + H2O
?
-
zinc-endopeptidase activity of the N-terminal light chain of BoNT/A on synaptosome-associated protein-25 kDa of the SNARE complex
-
-
?
SNAP25 + H2O
?
-
i.e. soluble N-ethylmaleimide-sensitive factor attachment protein 25, recombinant GST-tagged wild-type and mutant D193A, R198A, R198E, and I171A substrates, full-length and truncated substrate, SNAP25 initially binds along the belt region of BoNT/A, which aligns the P5 residue to the S5 pocket at the periphery of the active site, binding site structures, reaction mechanism, molecular modeling of the LC/A active site domain, overview
-
-
?
SNAP25 + H2O
?
-
i.e. synaptosomal-associated protein of 25 kDa, SNAP25 with varying peptide length, substrate specificity of BoNT/C1, e.g. 17mer peptide corresponding to residues 187-203 of SNAP-25 is a substrate for BoNT/C1 (1-430), importance of remote exosites in BoNT/C1 required for activity, assay optimization, overview
-
-
?
SNAP25 + H2O
?
-
i.e. synaptosome-associated protein of 25 kDa, located at the host synaptic membrane
-
-
?
SNAPtide + H2O
?
-
-
-
-
?
SNAPtide + H2O
?
P10845
-
-
-
?
SNAPtide + H2O
?
A5HZZ9
-
-
-
?
SNAPtide + H2O
?
-
i.e. SNAPtide, as recombinant human SNAP25bHA protein expressed in Escherichia coli
-
-
?
SNKTRIDEANQRATKML + H2O
SNKTRIDEANQ + RATKML
-
-
-
-
?
SNKTRIDEANQRATKML + H2O
SNKTRIDEANQ + RATKML
-
synthetic peptide substrate
-
?
SNKTRIDEANQRATKML + H2O
SNKTRIDEANQ + RATKML
-
the SNAP-25 peptide is a BoNT serotype A light chain substrate, a 17-residue synthetic peptide corresponding to residues 187 to 203 of SNAP-25. Serotype C1 cleaves the serotype A substrate at a bond separated by only one residue compared to serotype A
-
-
?
SNRTRIDEANK(Dnp)RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML + H2O
SNRTRIDEANK(Dnp) + RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML
-
a SNAP-25 peptide, residues 187-203, substrate BoNT/A LC FRET-based assay
-
-
?
SNRTRIDEANK(Dnp)RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML + H2O
SNRTRIDEANK(Dnp) + RA(S-(N-[4-methyl-7-dimethylamino-coumarin-3-yl]-carboxamidomethyl)-L-cysteine)RML
P10845
a synthetic fluorogenic peptide substrate of BoTxA/LC, representing amino acid residues 187-203 of SNAP25, a cleavage site of the enzyme
-
-
?
synaptobrevin + H2O
?
-
-
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
-
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
P10845
-
-
-
?
synaptobrevin + H2O
?
-
-
-
?
synaptobrevin + H2O
?
-
VAMP
-
?
synaptobrevin + H2O
?
-
VAMP2
-
?
synaptobrevin + H2O
?
-
i.e. VAMP
-
-
?
synaptobrevin + H2O
?
-
synaptic vesicle-associated membrane protein, neurotoxin responsible for human and animal botulism
-
-
?
synaptobrevin + H2O
?
-
hydrolyzed by BoNT/B, BoNT/D and BoNT/F
-
-
?
synaptobrevin + H2O
?
-
a vesicle-associated membrane protein, also known as VAMP, the most abundant SV entity, proteolytically cleaved by BoNT types B, D, F, and G
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
i.e. VAMP, neuronal vesicle-associated membrane protein, MW 19000, with 2 isoforms in human, chicken, in rat brain: synaptobrevin/VAMP-1 and synaptobrevin/VAMP-2, cleaves at Gln76-Phe77, the same site as botulin neurotoxin B
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
hydrolyzed by serotypes BoNT/B
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
serotype BoNT/B: cleavage at -Asp-Gln-+-Lys-Leu-, serotype BoNT/G: cleavage at Ala83-Ala84 (VAMP-1), Ala81-Ala82 (VAMP-2)
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
serotype BoNT/B: cleavage at Gln76-Phe77
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
serotype BoNT/B: cleavage at Ser-Ala-+-Ala-Lys
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
serotype BoNT/B: cleavage at Gln-Lys-+-Leu-Ser
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
hydrolyzed by serotypes D, F or G
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
in vitro, in synaptosomes and in injected Aplysia neurons
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
no substrate of serotype BoNT/A or E
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
carrying synaptobrevin/VAMP-2
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
both isoforms are cleaved at the same rate
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
carrying Val76 instead of Gln76 is not hydrolyzed by serotype BoNT/B
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
highly specific neurotoxins
-
-
?
Synaptobrevin + H2O
Hydrolyzed synaptobrevin
-
serotype BoNT/B: cleavage at Ser-Gln-+-Phe-Glu (at the same site as the tetanus neurotoxin)
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
highly specific neurotoxins
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
serotype BoNT/A and E
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
i.e. SNAP 25, protein of presynaptic membrane
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
in vitro, in isolated synaptosomes
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
serotype BoNT/A: cleavage at Asn-Gln-+-Arg-Ala
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
serotype BoNT/E: cleavage at Arg180-Ile181
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
no substrate of serotype BoNT/G
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
in vitro and in injected Aplysia neurons
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
serotype BoNT/A: cleavage at Asp-Arg-+-Ile-Met
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
native and recombinant protein
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
MW 25000
-
-
?
Synaptosome-associated protein + H2O
Hydrolyzed synaptosome-associated protein
-
serotype BoNT/A: cleavage at Gln197-Arg198
-
-
?
synaptosome-associated protein SNAP-25 + H2O
?
-
-
-
-
?
synaptosome-associated protein SNAP-25 + H2O
?
-
-
-
?
synaptosome-associated protein SNAP-25 + H2O
?
-
-
-
?
synaptosome-associated protein SNAP-25 + H2O
?
-
botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates
-
-
?
synaptosome-associated protein SNAP-25 + H2O
?
-
hydrolyzed by BoNT/A, BoNT/E and BoNT/CI
-
-
?
synaptosome-associated protein SNAP-25 + H2O
?
-
significant structural changes near the toxin's catalytic pocket upon substrate binding, probably serving to render the protease competent for catalysis
-
-
?
Syntaxin + H2O
?
-
-
-
?
Syntaxin + H2O
?
-
-
-
-
?
Syntaxin + H2O
?
P10845
-
-
-
?
Syntaxin + H2O
?
-
in vitro, in synaptosomes and in injected Aplysia neurons
-
-
?
Syntaxin + H2O
?
-
no substrate of serotype BoNT/G
-
-
?
Syntaxin + H2O
?
-
serotype BoNT/C
-
-
?
Syntaxin + H2O
?
-
serotype BoNT/C1-LC exhibits dual specificity toward both syntaxin and SNAP-25, in contrast to other serotypes, due to a distinct pocket S1' near the active site likely achieves the correct register for the cleavage site by only allowing Ala as the P1' residue for both SNAP-25 and syntaxin
-
-
?
Syntaxin + H2O
?
-
proteolytically cleaved by BoNT/C
-
-
?
Syntaxin + H2O
?
-
substrate of BoNT/C
-
-
?
VAMP + H2O
?
-
-
-
-
?
VAMP + H2O
?
-
i.e. vesicle associated membrane protein
-
-
?
VAMP + H2O
?
-
i.e. neuronal vesicle-associated membrane protein
-
-
?
VAMP + H2O
?
-
i.e. vesicle associated membrane protein or synaptobrevin, BoNT/B, and BoNT/F
-
-
?
VAMP + H2O
?
-
i.e. vesicle-associated membrane protein/synaptobrevin, substrate of BoNT/B, /D, /F, /G, and /C
-
-
?
VAMP + H2O
?
-
i.e. neuronal vesicle-associated membrane protein, substrate of BoNT/B, /D, /F, and /G
-
-
?
VAMP 2 + H2O
?
-
i.e. synaptobrevin-2 or vesicle-associated membrane protein 2
-
-
?
VAMP 2 + H2O
?
-
i.e. synaptobrevin-2 or vesicle-associated membrane protein 2, with BoNT/B light chain
-
-
?
VAMP-2 + H2O
?
-
-
-
?
VAMP-2 + H2O
?
-
initial substrate recognition is mediated through sequential binding of VAMP-2 to the B1, B2 and B3 pockets in LC/F (light chain of BoNT serotype F), which directed VAMP-2 to the active site of LC/F and stabilized the active site substrate recognition, where the P2, P1' and P2' sites of VAMP-2 are specifically recognized by the S2, S1' and S2' pockets of LC/F to promote substrate hydrolysis
-
-
?
VAMP-2 + H2O
?
-
cleaved by the light chains of subtypes BoNT/B, BoNT/T, BoNT/D, and BoNT/F
-
-
?
VAMP2 + H2O
?
-
i.e. intracellular vesicle associated membrane protein 2
-
-
?
VAMP2 + H2O
?
-
i.e. synaptobrevin-2 or vesicle-associated membrane protein 2
-
-
?
VAMP2 + H2O
?
-
human VAMP2 substrate, i.e. vesicle-associated membrane protein 2
-
-
?
VAMP2 + H2O
?
-
i.e. vesicle-associated membrane protein 2 or synaptobrevin-2, with BoNT/B light chain. BoNT/B HT exhibits little ability to cleave its substrate VAMP-2, when its LC and HC subunits are held together by a disulfide bond
-
-
?
VAMPTide + H2O
?
-
-
-
-
?
VAMPTide + H2O
?
-
a VAMP-2-derived peptide substrate, modified with FRET, with BoNT/B light chain
-
-
?
VAMPTide + H2O
?
substrate for subtype BoNT/B
-
-
?
vesicle-associated membrane protein-1 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-1 + H2O
?
cleavage at Arg66-Ala67
-
-
?
vesicle-associated membrane protein-1 + H2O
?
the enzyme suybtype BoNT/X cleaves vesicle-associated membrane protein-1 with a 10times higher efficiency than subtype BoNT/B and tetanus neurotoxin
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
-
-
?
vesicle-associated membrane protein-2 + H2O
?
cleavage at Arg66-Ala67
-
-
?
vesicle-associated membrane protein-2 + H2O
?
cleavage at Gln58-Lys59
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
cleavage at Leu54-Glu55
-
-
?
vesicle-associated membrane protein-2 + H2O
?
-
cleavage between L54 and E55
-
-
?
vesicle-associated membrane protein-3 + H2O
?
-
-
-
-
?
vesicle-associated membrane protein-3 + H2O
?
-
-
-
?
vesicle-associated membrane protein-3 + H2O
?
cleavage at Arg66-Ala67
-
-
?
vesicle-associated membrane protein-4 + H2O
?
-
-
-
?
vesicle-associated membrane protein-4 + H2O
?
cleavage at Lys87-Ser88
-
-
?
vesicle-associated membrane protein-5 + H2O
?
-
-
-
?
vesicle-associated membrane protein-5 + H2O
?
cleavage at Arg40-Ser41
-
-
?
Ykt6 + H2O
?
-
-
-
?
Ykt6 + H2O
?
cleavage at Lys173-Ser174
-
-
?
additional information
?
-
-
catalytic activity requires reduction of the single interchain disulfide bond of the neurotoxin
-
-
?
additional information
?
-
-
catalytic activity requires reduction of the single interchain disulfide bond of the neurotoxin
-
-
?
additional information
?
-
-
no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins
-
-
?
additional information
?
-
-
no hydrolysis of short peptides spanning the respective cleavage sites of the target proteins
-
-
?
additional information
?
-
-
activating protease activity is localized on light or L-chain of neurotoxin
-
-
?
additional information
?
-
-
the clostridial neurotoxins differ from other proteases in the recognition of the tertiary structure of the target rather than the sequence of the peptide bond to be cleaved
-
-
?
additional information
?
-
-
neuroparalytic activity tested by intravenous injection into Balb/c mice
-
-
?
additional information
?
-
-
synaptotagmin, synaptophysin
-
-
?
additional information
?
-
-
buforin I is no substrate
-
?
additional information
?
-
-
able to cleave selectively an essential component of neurotransmitter exocytosis, causing the syndrome of botulism characterized by flaccid paralysis
-
?
additional information
?
-
-
most potent neurotoxin known
-
?
additional information
?
-
-
most potent toxin known
-
?
additional information
?
-
-
only mammalian proteins, SNAP-25 from Drosophila sp. and Torpedo sp. are no substrates
-
?
additional information
?
-
-
undergoes autocatalytic proteolytic processing and fragmentation
-
?
additional information
?
-
-
BoNTs are the most toxic proteins known with mouse LD50 values in the range of 1-5 ng/kg. They are responsible for the pathophysiology of botulism. BoNTs enter peripheral cholinergic nerve terminals, where they cleave one or two of the three core proteins of the neuroexocytosis apparatus and elicit persistent but reversible inhibition of neurotransmitter release
-
-
?
additional information
?
-
-
botulinum neurotoxins are a group of proteins produced by different strains of Clostridium botulinum, that are responsible for botulism disease
-
-
?
additional information
?
-
-
boutulinum neurotoxin is a potent inhibitor of neuroexocytosis. Organization and regulation of the neurotoxin gene. The botulinum neurotoxin and non-toxic protein genes are organized in two polycistronic operons transcribed in opposite orientation
-
-
?
additional information
?
-
-
BoNTs bind with high specificity at neuromuscular junctions and they impair exocytosis of synaptic vesicles containing acetylcholine through specific proteolysis of SNAREs, soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors, which constitute part of the synaptic vesicle fusion machinery, botulinum neurotoxins cause the neuroparalytic syndrome of botulism, BoNTs are biological hazard to humans and a serious potential bioweapon threat with a lethal dose of 1 ng/kg body weight
-
-
?
additional information
?
-
-
clostridial neurotoxins are the causative agents of the neuroparalytic diseases botulism and tetanus blocking neurotransmitter release through specific proteolysis of one of the three soluble N-ethylmaleimide-sensitive-factor attachment protein receptors, SNAP-25, syntaxin, and synaptobrevin, which constitute part of the synaptic vesicle fusion machinery
-
-
?
additional information
?
-
-
intraglandular injection of botulinum toxin leads to a transient denervation of the submandibular gland and this is associated with reduced salivary secretion in Wistar rats, which may be due to glandular denervation induced by the inhibition of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptors involved in acetylcholine release at the neuroglandular junction and also specially inhibition of those involved in exocytosis of the granula of the acinar cells. Cell organelles and secretory granula show a clear atrophy of the acini, which is more prominent in glands injected with the combination of BoNT/A and B, overview
-
-
?
additional information
?
-
-
LC-mediated proteolysis of SNARE proteins and consequent inhibition of synaptic vesicle fusion to the presynaptic membrane of human motor neurons are responsible for flaccid paralysis associated with botulism
-
-
?
additional information
?
-
-
the cytopathic effect of C2I-C2IIa toxin, e.g. on human HeLa or colon cancer Caco-2 cells, or Vero cells, is higher for the single components compared to the complex
-
-
?
additional information
?
-
-
the enzyme causes neuroparalysis by blocking neurotransmitter release at the neuromuscular junctions
-
-
?
additional information
?
-
-
the neurotoxic enzyme causes the neuroparalytic illness botulism in humans acting as an endopeptidase which cleaves proteins that are necessary for acetylcholine exocytosis, botulinum toxin affets the strength-duration time constant in patients, the toxin acts on the Na+/K+ pump activity, overview
-
-
?
additional information
?
-
-
the proteolytically activated 60 kDa C2II binding component is essential for C2I transport into target cells involving especially amino acids Glu399, Asp426, and Phe428, it forms heptameric channels into membranes that are cation-selective and can be blocked by chloroquine and related compounds
-
-
?
additional information
?
-
P10845
the seven antigenically distinct serotypes of Clostridium botulinum neurotoxins cleave specific SNARE complex proteins and block the release of neurotransmitters causing flaccid paralysis and are considered potential bioweapons, botulinum neurotoxin type A is the most potent among the clostridial neurotoxins
-
-
?
additional information
?
-
-
the seven antigenically distinct serotypes of Clostridium botulinum neurotoxins cleave specific SNARE complex proteins and block the release of neurotransmitters causing flaccid paralysis and are considered potential bioweapons, botulinum neurotoxin type A is the most potent among the clostridial neurotoxins
-
-
?
additional information
?
-
the seven serotypes A-G potently block neurotransmission by binding to presynaptic receptors, undergoing endocytosis, transferring to the cytosol, and inactivating proteins essential for vesicle fusion, overview
-
-
?
additional information
?
-
-
toxicity in mice of full-length, single-nicked, and double-nicked enzyme forms, overview
-
-
?
additional information
?
-
-
development of a rapid assay method to distiguish the enzyme serotypes A, B, E, F, and G, substrate requirements of the different serotypes, overview
-
-
?
additional information
?
-
-
Glu224 and Glu262 are structurally essential for activity, structure-function relationship, overview
-
-
?
additional information
?
-
-
identification of active site and surrounding residues involved in substrate recognition and catalysis of BoNT/A, overview
-
-
?
additional information
?
-
-
LC-mediated proteolysis of soluble N-ethylmaleimide-sensitive factor attachment protein receptor, i.e. SNARE, proteins, complex reaction mechanism, overview
-
-
?
additional information
?
-
-
the catalytic component of the clostridial neurotoxins is their light chain, a Zn2+ endopeptidase, active site structure of serotype C1, substrate and cleavage site specificity of serotypes, overview
-
-
?
additional information
?
-
-
the enzyme is a binary toxin, which is composed of two separate proteins, the enzyme component C2I is an ADP-ribosyltransferase which modifies G-actin of eukaryotic cells, while the proteolytically activated binding/translocation component C2IIa forms ring-shaped heptamers, which bind to cell receptors and mediate the transport of C2I into the cytosol of target cells. Receptor-bound C2IIa serves as a docking platform for C2I on the cell surface, following assembly of C2I, the toxin complex is taken up via receptor-mediated endocytosis, and finally, C2IIa facilitates translocation of C2I from acidic endosomes into the cytosol, the preformed C2 toxin complex ADP-ribosylates actin in vitro and induces cell rounding, overview
-
-
?
additional information
?
-
-
the neurotoxin serotypes show distinct substrate specificities, overview
-
-
?
additional information
?
-
-
the the receptor-binding domain of botulinum neurotoxin serotype B binds to the luminal domain of synaptotagmin II, i.e. Syt-II, interaction occurs at both neutral and acidic endosomal pH, residues Glu44 to Lys60 become structured with residues Phe47 to Ile58 forming an alpha-helix, the HCB-Syt-II complex is stabilized by extensive intermolecular interactions involving two pronounced pockets on the HCB surface, structure, overview, high selectivity of BoNT/B among synaptotagmin I and II isoforms
-
-
?
additional information
?
-
BoNT E first binds to GT1b on the presynaptic membrane, like all other BoNTs. In BoNT B, the sialic acid of the sialyllactose that partly mimics GT1b binds in a shallow cavity formed by Trp1261 and His1240,12 and interacts with Tyr1262 and His1240, binding mode, overviewThe GT1b binding site in BoNT E is similar to those in other BoNTs and tetanus neurotoxin
-
-
?
additional information
?
-
-
BoNT E first binds to GT1b on the presynaptic membrane, like all other BoNTs. In BoNT B, the sialic acid of the sialyllactose that partly mimics GT1b binds in a shallow cavity formed by Trp1261 and His1240,12 and interacts with Tyr1262 and His1240, binding mode, overviewThe GT1b binding site in BoNT E is similar to those in other BoNTs and tetanus neurotoxin
-
-
?
additional information
?
-
-
BoNT serotypes bind to structure of ganglioside GT1b receptors, structure and binding specificities, modelling, overview
-
-
?
additional information
?
-
-
BoNT/A and BoNT/B bind a synaptic vesicle protein complex from synaptic vesicles, interactions of BoNT and host neuronal receptors, overview. Binding and entry of BoNTs at the neuromuscular junction, BoNT/A associates with the presynaptic membrane of alpha-motor neurons through interactions with oligosaccharides such as ganglioside GT1b, structure-function, modelling, overview
-
-
?
additional information
?
-
-
BoNT/A binds to peripheral cholinergic nerve terminals, causing their inhibition, rapidly and with high specificity via its receptor binding, heavy chain domain termed HC. BoNT/A interacts specifically with polysialogangliosides and with a luminal loop of the synaptic vesicle protein SV2 via the C-terminal half of HC, while the N-terminal half of it binds to sphingomyelin-enriched membrane microdomains and shows defined interaction with phosphatidylinositol phosphates, that might play a role in the correct positioning of the toxin for the subsequent low pH-driven membrane insertion of translocation domain sHN. Molecular modelling of Hc-N/A membrane binding, overview
-
-
?
additional information
?
-
BoNTs bind motor neurons via ganglioside-protein dual receptors, i.e. two HCR/F binding glycans: ganglioside GD1a and oligosaccharides containing an N-acetyllactosamine core, HCR/F binds synaptic vesicle glycoproteins through the keratan sulfate moiety of SV2, structure-function properties of BoNT/F host receptor interactions, dual receptors for BoNT/F, overview. Deglycosylation of glycoproteins disrupts the interaction with HCR/F, while the binding of HCR/B to its cognate receptor, synaptotagmin I, is unaffected. Mutations within the putative ganglioside binding pocket of HCR/F decrease binding to gangliosides, synaptic vesicle protein complexes, and primary rat hippocampal neurons, overview
-
-
?
additional information
?
-
-
BoNTs exert their neurotoxic effect by a multistep mechanism: binding, internalization, membrane translocation, intracellular traffic, and proteolytic degradation of target. The protein receptors are SV2 for BoNT/A, BoNT/E, and BoNT/F, and synaptotagmin I and II for BoNT/B and BoNT/G. BoNTs enter sensitive host cells via receptor-mediated endocytosis, detailed overview. The protease is chaperoned across host endosomes, DELTApH of early endosomes is finely tuned to elicit drastic conformational changes, leading to the insertion of BoNT into the membrane, while it is auspiciously set to interrupt further processing in the harsh acidic conditions existent inside lysosomes. HC dictates the target cell specificity and, during cell binding and intracellular traffic, serves to chaperone the light chain and HN, which ensures that partial unfolding of the light chain is concomitant with HN channel formation, thereby promoting productive light chain translocation
-
-
?
additional information
?
-
botulinum neurotoxin binds host peripheral neurons at the neuromuscular junction through a dual-receptor mechanism that includes interactions with ganglioside and protein receptors. The receptor identities vary depending on BoNT serotype. BoNT/B and BoNT/G bind the luminal domains of synaptotagmin I and II, homologous synaptic vesicle proteins, structure analysis of BoNT/G binding to Syt andGT1b, overview
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additional information
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design of BoNT A or B H-chain peptides for localizing BoNT/A binding regions to mouse brain synaptosomes
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additional information
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P10845
ganglioside GT1b is considered as BoNT/A receptor at nerve cells and can bind to the C-terminal end of the heavy chain
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additional information
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ganglioside GT1b is considered as BoNT/A receptor at nerve cells and can bind to the C-terminal end of the heavy chain
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additional information
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sialic acid-dependent binding is required for the transcytosis of serotype D botulinum neurotoxin and toxin complex L-TC in rat intestinal epithelial cell line IEC-6, mechanism, overview. HA-33 molecules play an important role in the effective binding of D-4947 L-TC to Caco-2 cells
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additional information
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the BoNT light chain domain is the Zn-dependent metalloprotease, that cleaves specific proteins that prevent acetylcholine release. BoNT shows endoproteolytic activity on one of the three SNARE proteins, i.e. soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins. The BoNT serotypes all show distinct cleavage sites on the SNARE substrates
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additional information
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the catalytic light chains of BoNTs, BoNT-LC, recognize extended regions of their substrates for cleavage
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additional information
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the heavy chain mediates the binding of the toxin with ganglioside and glycoprotein receptors at the neuronal surface, followed by toxin entry by means of receptor-mediated endocytosis. It mediates the translocation of the light chain into the neuronal cytosol, where it functions as a Zn2+-dependent endoprotease
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additional information
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the toxin light chain, LC, is a zinc-dependent endopeptidase that cleaves soluble N-ethylmaleimide-sensitive fusion proteins, SNARE, located at nerve endings
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additional information
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active site structure, Tyr351 is close to both nucleophilic water and catalytic zinc, overview
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additional information
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active site structure, Tyr351 is close to both nucleophilic water and catalytic zinc, overview
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additional information
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assay method measuring noradrenaline release in human neuronal SHSY-5Y cells
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additional information
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assay method measuring noradrenaline release in human neuronal SHSY-5Y cells
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additional information
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BoNT/E light chain mutant K224D does not cleave the SNARE proteins SNAP29 or SNAP47
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additional information
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development and evaluation of in vitro cell-based assays and in vivo assays for drug discovery and development, especially with regard to the potential for medium- to high-throughput automation and its use in identifying physiologically relevant inhibitors, development of FRET substrates, overview
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additional information
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development of a fluorescence sandwich immunoassay for BoNT activity determination, using serotype BoNT/A, demonstration of its application in both 96-well plate- and bead-based assay formats, both involving a solid substrate, overview
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additional information
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development of an improved ultra-performance liquid chromatography product detection method, overview
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additional information
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development of Endopep-MS, a mass spectrometry-based endopeptidase method for detecting and differentiating BoNT/A-G serotypes in buffer and BoNT/A, /B, /E, and /F in clinical samples
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additional information
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development of internally quenched fluorescent substrates containing the fluorophore/repressor pair pyrenylalanine/4-nitrophenylalanine for a sensitive assay method. (pNO2-Phe) and (1-pyrenylalanine) are, respectively, introduced at positions 197 and 200 of the cleavable fragment, amino acids 187 to 203, of SNAP-25, with norleucine at position 202 [Nle202], which is acetylated at its N terminus and amidated at its C-terminus. Sensitivity is increased when the peptide sequence of the previous substrate is lengthened to account for exosite binding to BoNT/A, substrate specificity and assay optimization, overview
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additional information
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enzyme-substrate complex, detailed overview. BoNT/C is unique among the BoNTs, in that it cleaves both SNAP-25 and syntaxin, another plasma membrane-anchored SNARE
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additional information
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F1-40 is a mouse-derived, IgG1 monoclonal antibody that binds the light chain of BoNT serotype A and is used in a sensitive immunoassay for toxin detection, determination of binding epitopes, overview
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additional information
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feasibility of using the CFP-YFP pair with full-length SNAP-25 as a FRET-based substrate for BoNT/A in a cell-based assay or with the 66-mer peptide as a FRET substrate in an in vitro assay, optimization of FRET efficiency by use of fluorescent protein variants, CsY, CsYY or YsCsY, overview
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additional information
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functional assay of the toxin protease activity using a fluorogenic substrate. Development of a bead-based sandwich immunoassay for botulinum neurotoxin serotype A, BoNT/A, using a recombinant 50 kDa fragment of the BoNT/A heavy chain as a structurally valid simulant. Different anti-BoNT/A antibodies are attached to three different fluorescent, dye encoded flow cytometry beads for multiplexing. The assay is conducted in two formats: a manual microcentrifuge tube format and an automated fluidic system format. Flow cytometry detection is used for both formats, method evaluation, overview
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additional information
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recombinant BoNT/E fragment HC1163-1256 binds synaptotagmin and gangliosides, the expressed and purified HC1163-1256 protein retains a functionally active conformation
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additional information
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regions on BoNT/B that bind to blocking antibodies, synaptotagmin, or gangliosides, recognition pattern, overview
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additional information
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standard assay used to determine potency of clinical samples is the in vivo mouse bioassay, MBA, another possibilty is the primary rat spinal cord cells using RSC assay, that also permits sensitive and quantitative detection of BoNT/A, with usage of Sprague Dawley E15 rat pup spinal cords, Direct comparison of MBA and RSC assays, overview
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additional information
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substrate specificities of the BoNT light chain subtypes, overview. The LC subtypes perform autolytic cleavage. Each LC/A subtype possesses the di-tyrosine autocleavage site, which indicate that residues in addition to the cleavage site are necessary for autocleavage. Control LC, LC/A1 DYM, contains mutations to cleavage site residues, Y250A and Y251A, which abrogates autocatalysis in LC/A1
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additional information
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synaptosome capture assay for the different serotype BoNTs, synaptosome from rat brains, overview
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additional information
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usage of a single molecule assay of BoNT serotypes A and E light chain translocation through the heavy chain channel in neurons, and of BoNT intoxication assays, namely the mouse protection and the primary rat spinal cord cell assays
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additional information
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enzyme binding to the receptor synaptotagmin II is functionally related to the enzyme's toxic action
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additional information
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no activity with synaptosome-associated protein SNAP-25 and syntaxin
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additional information
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no activity with Arg-Ile-Met-Glu
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additional information
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no activity with human SNAP-23
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additional information
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no activity with vesicle-associated membrane protein-7, vesicle-associated membrane protein-8, syntaxin 1, SNAP-25 and Sec22b
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additional information
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subtype BoNT/A6 enters cells more efficiently than other enzyme subtypes
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additional information
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the reduction of the disulfide bond is necessary for the optimum activity of the enzyme
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VAMP 22-58/Gln58D-cysteine
a substrate-based inhibitor, that binds to BoNT F in the canonical direction but is positioned specifically via three major exosites away from the active site
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VAMP 27-58/Gln58D-cysteine
a substrate-based inhibitor, that binds to BoNT F in the canonical direction but is positioned specifically via three major exosites away from the active site. The cysteine sulfur of the inhibitors interacts with the zinc and exists as sulfinic acid
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(2E)-2-(1H-benzimidazol-2-yl)-3-(3-iodo-4-methoxyphenyl)prop-2-enenitrile
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(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
(2E)-3-(2-amino-4-chlorophenyl)-N-hydroxyprop-2-enamide
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(2E)-3-(2-bromo-4-chlorophenyl)-N-hydroxyprop-2-enamide
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(2E)-3-(4-chloro-2-fluorophenyl)-N-hydroxyprop-2-enamide
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(2E)-3-(4-chloro-2-hydroxyphenyl)-N-hydroxyprop-2-enamide
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(2E)-3-(4-chloro-2-methoxyphenyl)-N-hydroxyprop-2-enamide
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(2E)-3-(4-chloro-2-methylphenyl)-N-hydroxyprop-2-enamide
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(2E)-3-(4-chloro-2-nitrophenyl)-N-hydroxyprop-2-enamide
-
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(2E)-3-(4-chlorophenyl)-N-hydroxyprop-2-enamide
-
a trans-cinnamic hydroxamate
(2E)-3-[4-chloro-2-(iminomethyl)phenyl]-N-hydroxyprop-2-enamide
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(2E)-3-[4-chloro-2-(methylsulfanyl)phenyl]-N-hydroxyprop-2-enamide
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(2E)-3-[4-chloro-2-(methylsulfonyl)phenyl]-N-hydroxyprop-2-enamide
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(2E)-3-[4-chloro-2-(trifluoromethyl)phenyl]-N-hydroxyprop-2-enamide
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(2E)-4-[(7-nitro-9H-fluoren-2-yl)amino]-4-oxobut-2-enoic acid
-
19.5% inhibition at 0.02 mM
(3alpha,5beta,7alpha,12alpha,17alpha)-24-([2-[(7-chloroquinolin-4-yl)amino]ethyl]amino)cholane-3,7,12-triyl triacetate
P10845
90% inhibition at 0.02 mM
(3R)-3-(2,4-dichlorophenyl)-N,5-dihydroxypentanamide
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(3R)-3-(4-chlorophenyl)-N,5-dihydroxypentanamide
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(3S)-3-(2,4-dichlorophenyl)-N,5-dihydroxypentanamide
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(3S)-3-(4-chlorophenyl)-N,5-dihydroxypentanamide
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([[5-[[1-(4-ammoniobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-(3-hydroxyphenyl)thiophen-3-yl]acetyl]amino)oxidanide
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synthesis and binding structure, overview, multiple molecular dynamics simulations of the endopeptidase in complex with inhibitor 2 using the dummy atom approach, overview
1-(2,4-dichlorobenzyl)-1H-pyrrole-2,5-dione
-
inhibitor is providing relatively potent BoNT protection in a cellular assay. It inhibits the biological activity of BoNT/A1 in neuronal cells. This inhibitor is about 7 to 10times more potent than 2-(2,4-dichlorobenzylidene)cyclopent-4-ene-1,3-dione
2'-((9H-fluoren-2-ylamino)carbonyl)-4,4'-bis(hydroxy(oxido)amino)[1,1'-biphenyl]-2-carboxylic acid
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82% inhibition at 0.02 mM
2'-[(7-fluoro-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
47.6% inhibition at 0.02 mM
2'-[(7-methoxy-9H-fluoren-2-yl)carbamoyl]biphenyl-2-carboxylic acid
-
20.9% inhibition at 0.02 mM
2'-[(9-hydroxy-9H-fluoren-2-yl)carbamoyl]biphenyl-2-carboxylic acid
-
20% inhibition at 0.02 mM
2'-[(9-oxo-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
20.2% inhibition at 0.02 mM
2'-[(9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
37.2% inhibition at 0.02 mM
2(9H-fluorene-2-carbonyl)benzoic acid
-
80.1% inhibition at 0.02 mM
2,2'-(1,4-dioxobutane-1,4-diyl)dibenzoic acid
-
21.2% inhibition at 0.02 mM
2,4-dichlorocinnamic acid hydroxamate
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2,4-dichlorocinnamic hydroxamate
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binding site and complex structure, overview
2,5-dichlorocyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2,5-dimethoxy-3-(4-methylphenyl)naphthalene-1,4-dione
A5HZZ9
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2-(1,2-dihydroacenaphthylene-5-carbonyl)benzoic acid
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11.5% inhibition at 0.02 mM
2-(1H-benzo[d]imidazol-2-yl)-3-(5-(furan-2-yl)thiophen-2-yl)acrylonitrile
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2-(1H-benzo[d]imidazol-2-yl)-3-(biphenyl-4-yl)acrylonitrile
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2-(2,3-dihydro-1H-indene-5-carbonyl)benzoic acid
-
16.3% inhibition at 0.02 mM
2-(2,4-dichlorobenzylidene)cyclopent-4-ene-1,3-dione
-
inhibits the biological activity of BoNT/A1 in neuronal cells. This inhibitor is about 7 to 10times less potent than 1-(2,4-dichlorobenzyl)-1H-pyrrole-2,5-dione
2-(2,4-dihydroxybenzoyl)benzoic acid
-
14.7% inhibition at 0.02 mM
2-(2-oxo-2,3-dihydro-1,3-benzoxazole-5-carbonyl)benzoic acid
-
35% inhibition at 0.02 mM
2-(3,5-dichloro-2-hydroxybenzoyl)benzoic acid
-
19.2% inhibition at 0.02 mM
2-(3,6-dioxocyclohexa-1,4-dien-1-yl)acetic acid
A5HZZ9
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2-(3-methyl-5,6,7,8-tetrahydronaphthalene-2-carbonyl)benzoic acid
-
24.8% inhibition at 0.02 mM
2-(4-(2,4-dichlorophenoxy)phenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)-1H-indole
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2-(4-(2-chloro-4-cyanophenoxy)phenyl)-1H-indole-6-carbonitrile
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2-(4-(2-chloro-4-cyanophenoxy)phenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)indole
-
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2-(4-(4-(6-(1,4,5,6-tetrahydropyrimidin-2-yl)benzo[b]thiophen-2-yl)phenoxy)phenyl)-1,4,5,6-tetrahydropyrimidine
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2-(4-(4-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)phenoxy)phenyl)-4,5-dihydro-1H-imidazole
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2-(4-(4-(6-(5-hydroxy-1,4,5,6-tetrahydropyrimidin-2-yl)-1H-indol-2-yl)phenoxy)phenyl)-1,4,5,6-tetrahydropyrimidin-5-ol
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2-(4-(4-carbamoylphenoxy)phenyl)-1H-indole-6-carboxamide
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2-(4-(4-cyanophenoxy)phenyl)-1H-indole-6-carboximidamide
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2-(4-(4-cyanophenoxy)phenyl)indole-6-carbonitrile
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2-(4-(6-(1,4,5,6-tetrahydropyrimidin-2-yl)benzo[b]thiophen-2-yl)phenyl)-1,4,5,6-tetrahydropyrimidine
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2-(4-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)-phenyl)-4,5-dihydro-1H-imidazole
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2-(4-carboxybenzoyl)benzoic acid
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13.7% inhibition at 0.02 mM
2-(4-fluorophenyl)-1H-indole-6-carbonitrile
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2-(4-fluorophenyl)-1H-indole-6-carboxamide
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2-(4-fluorophenyl)-1H-indole-6-carboximidamide
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2-(4-iodophenyl)cyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-(4-methoxyphenyl)-1H-indole-6-carboxamide
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2-(4-methoxyphenyl)-1H-indole-6-carboximidamide
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2-(4-methoxyphenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)-1H-indole
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2-(4-methylphenyl)naphthalene-1,4-dione
A5HZZ9
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2-(5-(4-cyanophenoxy)pyridin-2-yl)-1H-indole-6-carbonitrile
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2-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarboxamide
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2-(5-{[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl}-2-phenylthiophen-3-yl)-N-hydroxyacetamide
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i.e. 2-(5-[[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-phenylthiophen-3-yl)-N-hydroxyacetamide
2-(9H-fluorene-2-carbonyl)benzoic acid
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2-(pyridin-2-ylamino)cyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-([1,1'-biphenyl]-4-carbonyl)benzoic acid
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37.8% inhibition at 0.02 mM
2-amino-N-(4-phenoxyphenyl)acetamide
A5HZZ9
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2-amino-N-[3-(benzyloxy)phenyl]acetamide
A5HZZ9
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2-benzoylbenzoic acid
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15.9% inhibition at 0.02 mM
2-bromo-4-chlorocinnamic acid hydroxamate
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2-chlorocyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-mercapto-3-phenylpropionyl-R
-
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2-mercapto-3-phenylpropionyl-RA
-
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2-mercapto-3-phenylpropionyl-RAAKML
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2-mercapto-3-phenylpropionyl-RAT
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2-mercapto-3-phenylpropionyl-RATAML
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2-mercapto-3-phenylpropionyl-RATK
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2-mercapto-3-phenylpropionyl-RATKAL
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2-mercapto-3-phenylpropionyl-RATKM
-
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2-mercapto-3-phenylpropionyl-RATKML
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2-mercapto-3-phenylpropionyl-RATKMLGSG
-
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2-mercapto-3-phenylpropionyl-RVTKML
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2-methoxy-3-(4-methylphenyl)cyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-methoxycyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-methyl-4-chlorocinnamic acid hydroxamate
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2-methyl-7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
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2-methyl-7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
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2-methyl-7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
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2-methylcyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-methylnaphthalene-1,4-dione
A5HZZ9
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2-phenylcyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-trifluoromethyl-4-chlorocinnamic acid hydroxamate
-
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2-[(3-bromo-9-oxo-9H-fluoren-2-yl)carbamoyl]cyclohexane-1-carboxylic acid
-
19.3% inhibition at 0.02 mM
2-[(4-bromo-9-oxo-9H-fluoren-2-yl)carbamoyl]benzoic acid
-
26.2% inhibition at 0.02 mM
2-[(9-oxo-9H-fluoren-2-yl)carbamoyl]benzoic acid
-
14.8% inhibition at 0.02 mM
2-[(9-oxo-9H-fluoren-2-yl)carbamoyl]cyclohexane-1-carboxylic acid
-
18.3% inhibition at 0.02 mM
2-[(9H-fluoren-2-yl)carbamoyl]cyclohexane-1-carboxylic acid
-
12% inhibition at 0.02 mM
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2-[1-cyano-2-(3-bromo-5-methoxy-4-hydroxyphenyl)vinyl]benzimidazole
-
-
2-[1-cyano-2-(3-chloro-5-methoxy-4-hydroxyphenyl)vinyl]benzimidazole
-
-
2-[4-(methylamino)-3-nitrobenzoyl]benzoic acid
-
14.1% inhibition at 0.02 mM
2-[5-{[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl}-2-(3-hydroxyphenyl)thiophen-3-yl]-N-hydroxyacetamide
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i.e. 2-[5-[[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-(3-hydroxyphenyl)thiophen-3-yl]-N-hydroxyacetamide, 79% inhibition of BoNTA at 0.02 mM
2-[5-{[1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indol-6-yl]carbonyl}-2-(3-aminophenyl)thiophen-3-yl]-N-hydroxyacetamide
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i.e. 2-(5-(1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indole-6-carbonyl)-2-(3-aminophenyl)thiophen-3-yl)-N-hydroxyacetamide, 47% inhibition of BoNTA at 0.02 mM. The hydroxamate coordinates the zinc ion embedded in the active site and forms a hydrogen bond to Glu224. The cation shows pi-interaction of the thiophene-substituted phenyl group with Arg363. Occurence of pi-pi interactions of the thiophene-substituted phenyl group with Phe194 and Tyr366, of interaction of the ketone oxygen atom with Asp370 that is bridged by at least one water molecule, and of cation-pi and pi-pi interactions of the indole-substituted phenyl group with Lys66 and Gln162, respectively
2-[5-{[1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indol-6-yl]carbonyl}-2-(4-hydroxyphenyl)thiophen-3-yl]-N-hydroxyacetamide
-
i.e. 2-(5-(1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indole-6-carbonyl)-2-(4-hydroxyphenyl)thiophen-3-yl)-N-hydroxyacetamide, 82% inhibition of BoNTA at 0.02 mM. The hydroxamate coordinates the zinc ion embedded in the active site and forms a hydrogen bond to Glu224. The cation shows pi-interaction of the thiophene-substituted phenyl group with Arg363. Occurence of pi-pi interactions of the thiophene-substituted phenyl group with Phe194 and Tyr366, of interaction of the ketone oxygen atom with Asp370 that is bridged by at least one water molecule, and of cation-pi and pi-pi interactions of the indole-substituted phenyl group with Lys66 and Gln162, respectively
2-[[17-oxoestra-1,3,5(10)-trien-3-yl]oxy]cyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
24-mer C-terminal peptide of LcE1
-
the activity of the light chain of botulinum toxin A is significantly reduced to 32% by the peptide with sequence TGRGLVKKIIRFCKNIVSVKGIRK
-
3'-O-ethyl-dynasore
A5HZZ9
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3,9-dichloro-6-(5,7-dichloro-9H-fluoren-2-yl)-5H-dibenzo[c,e]azepine-5,7(6H)-dione
-
68.9% inhibition at 0.02 mM
3,9-dichloro-6-(9H-fluoren-2-yl)-5H-dibenzo[c,e]azepine-5,7(6H)-dione
-
48% inhibition at 0.02 mM
3-(2,20-bithiophen-5-yl)-2-(1H-benzo-imidazol-2-yl)acrylonitrile
-
-
3-(2,4-dichlorophenyl)-5-(4-fluorophenethoxy)-N-hydroxypentanamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-(4-fluoro-2-methoxyphenyl)-N5-hydroxypentanediamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-(4-fluorophenethyl)-N5-hydroxypentanediamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-hydroxy-N5-(4-methoxyphenethyl)pentanediamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-hydroxy-N5-(o-tolyl)pentanediamide
A5HZZ9
-
3-(3,6-dioxocyclohexa-1,4-dien-1-yl)propanoic acid
A5HZZ9
-
3-(4-(1H-imidazol-1-yl)phenyl)-2-(1H-benzoimidazol-2-yl)acrylonitrile
-
-
3-(4-chloro-2-methylphenyl)-N-hydroxypropanamide
-
-
3-fluoro-2-(naphthalene-2-carbonyl)benzoic acid
-
43.9% inhibition at 0.02 mM
3-hydroxy-N'-[(E)-(2-hydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
-
3-hydroxy-N'-[(E)-(3,4,5-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
competitive inhibition
3-hydroxy-N'-[(E)-(3-hydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
-
3-hydroxy-N-phenylanthracene-2-carboxamide
-
70.1% inhibition at 0.02 mM
32-mer C-terminal peptide of LcA
-
the activity of the light chain of botulinum toxin A is significantly reduced to 15% by the peptide with sequence KNFTGLFEFYKLLCVRGIITSKTKSLDKGYNK
-
4,4'-dichloro-2'-((9H -fluoren-2-ylamino)carbonyl)[1,1'-biphenyl]-2-carboxylic acid
-
88.3% inhibition at 0.02 mM
4,4'-dichloro-2'-[(5,7-dichloro-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
79.11% inhibition at 0.02 mM
4-(2-amino-3-sulfanylpropyl)benzamide
-
-
4-(2-amino-3-sulfanylpropyl)benzenesulfonamide
-
-
4-(2-amino-3-sulfanylpropyl)benzenesulfonic acid
-
-
4-amino-7-chloroquinoline
-
12% inhibition at 0.05 mM
4-chloro-(3-fluorophenyl)methyl benzenesulfonamide
-
i.e. MSU84, competitive inhibitor of botulinum neurotoxin type A light chain
4-chloro-N-[(4-fluorophenyl)methyl] pyridin-3-amine
-
i.e. MSU58, competitive inhibitor of botulinum neurotoxin type A light chain
4-chlorocinnamic hydroxamate
4-[((2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2R)-2-phenylethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl)]benzoic acid
-
-
4-[((2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(4-hydroxyphenyl)ethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl)]benzoic acid
-
-
4-[((2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl)]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(3H-imidazol-4-yl)ethylcarbamoyl]-(2S)-2-biphenyl-4-ylethylcarbamoyl)-3(S)sulfanylpropyl]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-methylbutylcarbamoyl)-(2S)-2-biphenyl-4-ylethylcarbamoyl]-3(S)-sulfanylpropyl]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2R)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1-methyl-1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-naphthalen-1-yl-ethylcarbamoyl]-3(S)sulfanylpropyl] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl]-3(S)sulfanylpropyl)] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(2S)-2-benzol[beta]thiophen-3-yl-1-benzylcarbamoylethylcarbamoyl-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3-(S)-sulfanylpropyl] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(2S)-2-benzo[b]thiophen-3-yl-1-benzylcarbamoylethylcarbamoyl-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)-sulfanylpropyl]benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2R)-2-phenylethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(3H-imidazol-4-yl)ethylcarbamoyl]-(2S)-2-biphenyl-4-yl-ethylcarbamoyl}-3(S)sulfanylpropyl)}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(4-hydroxyphenyl)ethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2R)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1-methyl-1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-naphthalen-1-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl]-3(S)-sulfanylpropyl)}benzoic acid
-
-
5,8-dihydroxynaphthalene-1,4-dione
A5HZZ9
-
5,8-dioxo-5,8-dihydronaphthalen-1-yl acetate
A5HZZ9
-
5,8-dioxo-5,8-dihydronaphthalen-1-yl cyclopentanecarboxylate
A5HZZ9
-
5-((3-bromoadamantan-1-yl)methoxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
A5HZZ9
-
5-(allyloxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
A5HZZ9
-
5-(benzyloxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
A5HZZ9
-
5-(benzyloxy)naphthalene-1,4-dione
A5HZZ9
-
5-chloro-7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-hydroxynaphthalene-1,4-dione
A5HZZ9
-
5-methoxynaphthalene-1,4-dione
A5HZZ9
-
5-methyl-2-(propan-2-yl)naphthalene-1,4-dione
A5HZZ9
-
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy)phenyl)-1H-benzo[d]imidazole
-
-
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy)phenyl)-1H-indole
-
-
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-{5-[4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy]pyridin-2-yl}-1H-indole
-
-
6-(3,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(3,4,5,6-tetrahydropyrimidin-2-yl)phenyl)-1H-indole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4,5-dihydro-1H-imidazol-2-yl)phenyl)-1H-indole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)phenyl)-1H-benzo[d]imidazole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)phenyl)-1H-indole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-fluorophenyl)-1H-indole
-
-
6-(4,5-dihydroimidazol-2-yl)-2-(5-(4-(4,5-dihydroimidazol-2-yl)phenoxy)pyridine-2-yl)indole
-
-
6-(9H-fluoren-2-yl)-3,9-dinitro-5H-dibenzo[c,e]azepine-5,7(6H)-dione
-
24.7% inhibition at 0.02 mM
6-bromo-N-hydroxynaphthalene-2-carboxamide
-
-
6-chloro-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)-phenyl)-1H-indole
-
-
6-chloro-N-hydroxy-1-benzothiophene-2-carboxamide
-
-
6-chloro-N-hydroxy-1-methyl-1H-indole-2-carboxamide
-
-
6-chloro-N-hydroxy-1H-indene-2-carboxamide
-
-
6-chloro-N-hydroxynaphthalene-2-carboxamide
-
-
6-hydroxynaphthalene-1,4-dione
A5HZZ9
-
6-[(2,5-dimethoxyphenyl)amino]-N-(4-phenoxybenzyl)picolinamide
A5HZZ9
-
6-[(3,6-dioxocyclohexa-1,4-dien-1-yl)amino]-N-(4-phenoxybenzyl)picolinamide
A5HZZ9
-
7-((4-nitroanilino)(phenyl)methyl)-8-quinolinol
-
NSC 1010
7-N-phenylcarbamoylamino-4-chloro-3-propyloxyisocoumarin
-
ICD 1578
7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
9H-fluorene
-
17.3% inhibition at 0.02 mM
Ac-SNKTRIDEACQRATKML-NH2
-
-
Ac-SNKTRIDEAN(D)CRATKML-NH2
-
-
Ac-SNKTRIDEAN(D)QCRATKML-NH2
-
-
Ac-SNKTRIDEANCRATKML-NH2
-
-
Ac-SNKTRIDEANQCATKML-NH2
-
-
Ala-Ser-Gln-Phe-Glu-Thr-Ser
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica, serotype BoNT/B, not A or E
aminopterin
P10845
11% inhibition at 0.01 mM
ammonium chloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
amodiaquine
-
antimalarial drug, 30% inhibition
antibody F1-40
-
F1-40 binds a peptide fragment of the BoNT/A light chain, designated L1-3, which spans from T125 to L200, with recognition motif QPDRS. No binding to BoNT/A mutant Q138G/P139G/D140G. Wild-type residues Q138, P139 and D140 form a loop on the external surface of BoNT/A, exposed to solvent
-
AQVDEVVDIMRVNVDKVLERDQ
-
residues 37-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
bafilomycin A1
-
inhibits all BoNT serotypes. The ATPase inhibitor also functions as antagonist of the acidification process
bis-aminoquinoline
P10845
60% inhibition at 0.02 mM
bisquinoline Q2-15
-
60% inhibition
bisquinoline Q2-61
-
50% inhibition
buforin I
-
natural peptide, isolated from the stomach of the Asian toad Bufo bufo gargarizans
-
CB 7969312
-
the quinolinol-based analogue effectively neutralizes BoNT/A toxicity, ex vivo protection at 500 nM
CB7967495
-
inhibitor of botulinum neurotoxin serotypes B, C, E, and F
CB7969312
-
inhibitor of botulinum neurotoxin serotypes B, C, E, and F
chicoric acid iso-propyl ester
A5HZZ9
competitive partial inhibition
Chloroquinone
P10845
7% inhibition at 0.02 mM
cinnamic acid hydroxamate
-
-
CpA
-
i.e. [5-(4-chlorobenzoyl)-2-phenylthiophen-3-yl]acetic acid, 15% inhibition of BoNTA at 0.1 mM
CRATKML
-
competitive peptide inhibitor
cyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
D-chicoric acid
-
mechanism of inhibition, overview. The inhibitor binds to an exosite, displays noncompetitive partial inhibition, and is synergistic with a competitive inhibitor I2 when used in combination
desmosine
P10845
25% inhibition at 0.01 mM
Dyngo-4a
A5HZZ9
endocytic inhibitor of BoNT/A neurotoxicity through dynamin inhibition, competitive inhibition. Complete inhibition of the BoNT/A light chain at 0.02 mM
expoxomicin
-
increases ubiquitination of BoNT/B light chain in neuronal cells. Ubiquitination in vitro and in cells decreases the biological activity of BoNT/B light chain
ganglioside GT1b glycoconjugate
-
the synthetic glycoconjugates based on GT1b prevents SNAP25 cleavage in spinal cord cells of rat embryos
GGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 17-58 of vesicle-associated membrane protein VAMP
Gln-Phe-Glu-Thr
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica, serotype BoNT/B, not A or E
GRKKRRQRRRPPQC
-
90% inhibition
LQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 32-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
mefloquine
P10845
28% inhibition at 0.02 mM
methyl 3alpha-(N-[(7-chloroquinolin-4-yl)amino]ethyl)amino,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
-
-
methyl 3alpha-(N-[(7-chloroquinolin-4-yl)amino]ethyl)oxy,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
-
9% inhibition at 0.05 mM
methyl 3alpha-amino-7alpha,12alpha-diacetoxycholan-24-oate
-
13% inhibition at 0.05 mM
methyl 3beta-(N-[(7-chloroquinolin-4-yl)amino]ethyl)amino,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
-
-
methyl 6-[(3,6-dioxocyclohexa-1,4-dien-1-yl)amino]picolinate
A5HZZ9
-
methylamine hydrochloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
monensin
P10845
38% inhibition at 0.01 mM
N'-(2-(dimethylamino)ethyl)-2-(4-(4-(N'-2-(dimethylaminoethyl)carbamimidoyl)phenoxy)phenyl)-1H-indole-6-carboximidamide
-
-
N'-[(E)-(2,4,5-trihydroxyphenyl)methylidene]benzohydrazide
A5HZZ9
-
N'-[(E)-(2,4,5-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
-
N,N-bis(7-aminoheptyl)-1-benzyl-4-[3-(hydroxyamino)-3-oxopropyl]-5-(3-hydroxy-3,3-diphenylpropyl)-1H-pyrrole-2-carboxamide
-
a tetrasubstituted pyrrole inhibitor
N-(2,6-dimethylphenyl)-2-(pyridine-4-carbonyl)hydrazine-1-carbothioamide
-
28% inhibition at 0.02 mM
N-(2-chlorophenyl)-2-(pyridine-4-carbonyl)hydrazine-1-carbothioamide
-
19% inhibition at 0.02 mM
N-(3-amino-9H-fluoren-2-yl)acetamide
-
13.7% inhibition at 0.02 mM
N-(3alpha,7alpha,12alpha-triacetoxy-5beta-cholan-24-yl)-N'-(7'-chloroquinolin-4'-yl)-ethane-1,2-diamine
-
-
N-(4-bromobenzyl)-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
69% inhibition at 0.02 mM
N-(4-bromobenzyl)-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
68% inhibition at 0.02 mM
N-(4-phenoxybenzyl)picolinamide
A5HZZ9
-
N-(4-tert-butylbenzyl)-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
47% inhibition at 0.02 mM
N-(4-tert-butylbenzyl)-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
50.28% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-fluorobenzyl)ethane-1,2-diamine
P10845
68% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-fluorobenzyl)propane-1,3-diamine
P10845
50.09% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-methoxybenzyl)ethane-1,2-diamine
P10845
18% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-methoxybenzyl)propane-1,3-diamine
P10845
14% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-3-ylmethyl)ethane-1,2-diamine
P10845
25% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-3-ylmethyl)propane-1,3-diamine
P10845
39.89% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-4-ylmethyl)ethane-1,2-diamine
P10845
24% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-4-ylmethyl)propane-1,3-diamine
P10845
42.29% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-adamantylethane-1,2-diamine
P10845
51.4% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-[(4-methoxypyridin-3-yl)methyl]ethane-1,2-diamine
P10845
19% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-[(4-methoxypyridin-3-yl)methyl]propane-1,3-diamine
P10845
43.25% inhibition at 0.02 mM
N-(9-oxo-9H-fluoren-2-yl)benzamide
-
12.7% inhibition at 0.02 mM
N-(methyl 7alpha,12alpha-diacetoxy-5beta-cholan-24-oate,3alpha-yloxy)-ethyl-N'-(7-chloroquinolin-4-yl)-ethane-1,2-diamine
-
62% inhibition at 0.05 mM
N-(pyridin-2-yl)prop-2-enamide
A5HZZ9
-
N-(pyridin-3-yl)prop-2-enamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-1-(2,5-dimethoxybenzyl)-1H-1,2,4-triazole-3-carboxamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-1-[(3,6-dioxocyclohexa-1,4-dien-1-yl)methyl]-1H-1,2,4-triazole-3-carboxamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-1H-1,2,4-triazole-3-carboxamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-2-aminoacetamide
A5HZZ9
-
N-Ac-CRATKML
P10845
an inhibitory peptide, structure of the serotype A toxin light chain with an inhibitory peptide bound at the catalytic Zn(II) ion, the peptide is bound with the Cys Sgamma atom coordinating the metal ion, overview
N-acetyl neuraminic acid
-
both binding and permeation of toxins are potently inhibited by N-acetyl neuraminic acid in the cell culture mediumor by treatment of the cells with neuraminidase, but neither galactose, lactose nor N-acetyl galactosamine inhibit binding or permeation of toxins
N-acetyl-CRATKML-amide
-
-
N-benzyl-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
52% inhibition at 0.02 mM
N-benzyl-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
51.83% inhibition at 0.02 mM
N-hydroxy-2-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
A5HZZ9
-
N-hydroxy-4-pentylbenzamide
-
-
N-hydroxyacetamidoadamantan
-
a synthetic hydroxamate
N-[(4-chloropyridin-3-yl)methyl]-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
23% inhibition at 0.02 mM
N-[(4-chloropyridin-3-yl)methyl]-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
35.87% inhibition at 0.02 mM
N-[3-(benzyloxy)phenyl]-2-[(2,5-dimethoxybenzyl)amino]acetamide
A5HZZ9
-
N-[3-(benzyloxy)phenyl]-2-[[(3,6-dioxocyclohexa-1,4-dien-1-yl)methyl]amino]acetamide
A5HZZ9
-
N1-(2-cyclopropylethyl)-3-(2,4-dichlorophenyl)-N5-hydroxypentanediamide
A5HZZ9
-
N1-(4-bromophenyl)-3-(2,4-dichlorophenyl)-N5-hydroxypentanediamide
A5HZZ9
-
N1-(6-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)-pyridine-3-yl)ethane-1,2-diamine
-
-
N1-(7-chloroquinolin-4-yl)-ethane-1,2-diamine
-
33% inhibition at 0.05 mM
N1-(7-chloroquinolin-4-yl)-propane-1,3-diamine
-
22% inhibition at 0.05 mM
naphthalene-1,4-dione
A5HZZ9
-
NSC 119889
-
56% inhibition
NSC 130796
-
48% inhibition
NSC 240898
-
NSC 240898, a potent BoNT/A LC endopeptidase inhibitor, 75% inhibition at 0.02 mM, no cytotoxicity
NSC 357756
-
57% inhibition
NSC 402959
-
40% inhibition
NSC 625324 (silver sulfadiazine)
-
100% inhibition
NSC 661755 (michellamine B)
-
62% inhibition
NSC 86372
-
51% inhibition
paclitaxel
P10845
95% inhibition at 0.01 mM
phorbol 12-myristate 13-acetate
-
increases ubiquitination of BoNT/B light chain in neuronal cells. Ubiquitination in vitro and in cells decreases the biological activity of BoNT/B light chain
PPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 22-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
PTEN
P10845
a zinc-chelating agent
-
Quinacrine
-
antimalarial drug, 30% inhibition
RRGF
-
0.02 mM, 95% inhibition
S132B-C11
-
a RNA aptamer that inhibits the enzyme's endopeptidase activity in a non-competitive manner. The core sequence is GACAGCGUGCCUAGAAGUCCAAGCUUAAAUAACCACGCUCGACAAGC, structure, overview
-
S132B-C12
-
a RNA aptamer that inhibits the enzyme's endopeptidase activity in a non-competitive manner. The core sequence is ACAACCCGGAACAACGUCUAACAGUGUACCAUAACCCGGCAUUCA, structure, overview
-
S132B-C22
-
a RNA aptamer that inhibits the enzyme's endopeptidase activity in a non-competitive manner. The core sequence is AUUCGGGCCCAGGAACCAACUAUAUAAAUGUCCCGAAUGCUUCGACG, structure, overview
-
single-domain llama antibody Aa1
-
most potent antibody isolated from a single domain VHH, i.e. camelid heavy-chain variable region derived from heavy-chain-only antibody, antibodies, it is resistant to heat denaturation and reducing conditions. The Aa1 paratope coincides with an alpha-helical portion of the SNAP25 substrate. Structure of BoNT/A Lc-Aa1 VHH complex and inhibition mechanism, overview
-
synaptotagmin II luminal domain
-
the luminal domain of syt II, syt II-LD, inhibits the toxicity of BoNT/B by interfering with the toxin-receptor interaction. It contains toxin-binding sites that have a high affinity for BoNT/B heavy chain. Recombinant syt II-LD in vivo provides protection against BoNT/B intoxication in mice models to about 30% survivals at 0.27 mg/ml of sytII-LD, the neutralization effect is improved by using gangliosides to 60% survivals. Syt II-LD specifically binds to BoNT/B compared to other BoNT serotypes, overview
-
THF-toosendanin
-
tetrahydrofuran analogue of toosendanin, selectively arrests the light chain translocation step of intoxication with subnanomolar potency, and increases the unoccluded heavy chain channel propensity to open with micromolar efficacy, inhibitory profile on light chain translocation, overview. The bimodal modulation by toosendanin depends on the dynamic interactions between channel and cargo, highlighting their tight interplay during the progression of LC transit across endosomes
tris-(2-carboxyethyl)-phosphine hydrochloride
-
i.e. TCEP, a non-odorous, oxygen-insensitive, non-toxic sulfhydryl reducing compound, reduces proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells at higher concentrations above 4 mM, protects against BoNT/B inhibition of noradrenaline release, achieving 72% of the release from un-intoxicated controls. TCEP significantly changes the conformation of BoNT/B holotoxin. But TCEP does not fragment un-nicked BoNT/B holotoxin
tris[3-(7-chloroquinolin-4-yl)aminopropyl]amine
-
-
Triticum vulgaris lectin
-
a known competitive antagonist of BoNT, inhibits the activation of neurit outgrowth by BoNT/A
-
TSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 27-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
VVDIMRVNVDKVLERDQ
-
residues 42-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
Zn2+
-
addition of exogenous ZnCl2 to the assay mixture reduces the activity of BoNT/Am activity ratio of wild-type and mutant enzymes in presence or absence of ZnCl2, overview
[[(5-[[1-(4-ammoniobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-phenylthiophen-3-yl)acetyl]amino]oxidanide
-
synthesis and binding structure, overview, multiple molecular dynamics simulations of the endopeptidase in complex with inhibitor 1 using the dummy atom approach, overview
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
-
a synthetic hydroxamate, D-chicoric acid is synergistic with a competitive inhibitor I2 when used in combination
4-chlorocinnamic hydroxamate
-
-
4-chlorocinnamic hydroxamate
-
binding site and complex structure, overview
captopril
-
-
captopril
-
serotype BoNT/B
Chloroquine
-
antimalarial drug, 20% inhibition
Chloroquine
-
the C2II channel can be blocked by chloroquine and related compounds
concanamycin A
-
concanamycin A
-
the ATPase inhibitor also functions as antagonist of the acidification process
EDTA
-
-
L-Arginine hydroxamate
-
-
L-Arginine hydroxamate
-
binding site and complex structure, overview
RRGC
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGC
-
0.02 mM, 95% inhibition, most potent inhibitor. When assayed in the presence of dithiothreitol, the inhibitory effect is drastically reduced
RRGI
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGI
-
0.02 mM, 90% inhibition
RRGL
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGL
-
0.02 mM, 95% inhibition
RRGM
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGM
-
0.02 mM, 90% inhibition
toosendanin
-
i.e. TSDN, selectively arrests the light chain translocation step of intoxication with subnanomolar potency, and increases the unoccluded heavy chain channel propensity to open with micromolar efficacy, inhibitory profile on light chain translocation, overview. The bimodal modulation by toosendanin depends on the dynamic interactions between channel and cargo, highlighting their tight interplay during the progression of LC transit across endosomes. Toosendanin modulates both cargo-dependent and cargo-free activities of the BoNT/E protein-conducting channel
toosendanin
an enzyme translocation inhibitor that hinders subtype BoNT/B oligomerization
additional information
P10845
not inhibited by D-fructose
-
additional information
-
less than 10% inhibition with captopril
-
additional information
-
inhibitor synthesis, overview
-
additional information
-
inhibitory potency and activity-structure relationship of 4-amino-7-chloroquinoline substructure-based compounds, molecular modeling, overview, no inhibition by methyl cholate triacetate
-
additional information
-
analysis of Echinacea components in inhibition of BoNT/A protease, overview
-
additional information
-
BoNT/B LC is processed for removal via the proteasome-dependent degradation pathway after ubiquitination in neuronal cells
-
additional information
-
capsaicin interacts with TRPV1 receptors, transient receptor potential proteins of the vanilloid subfamily, on motor nerve endings to reduce BoNT/A uptake into Neuro 2a cells via a Ca2+-dependent mechanism, but capsaicin fails to protect against the neuroparalytic effects of BoNT/A. Capsaicin protects muscle functions and electromygraphic activity from the incapacitating effects of BoNT/A. Capsazepine pretreatment antagonizes the protective effect of capsaicin on acetylcholine release at high frequencies
-
additional information
-
construction of a non-immune llama single-domain library for display on the surface of Saccharomyces cerevisiae and identification of a single-domain llama antibody that potently inhibits the enzymatic activity of BoNT/A light chain by binding to the non-catalytic alpha-exosite binding region, overview
-
additional information
P10845
construction of type A-specific monoclonal antibodies using antigene heavy chain antibody fragment VH/VHH from a nonimmune camel, primers specific to human VH gene segments, and recombinant expression in phagemid-transformed Escherichia coli. The selected antibodies inhibiting the endopeptidase activity of BoTxA light chain and of botulism in hosts in vivo. Molecular docking and interface binding of BoTxA/LC and antibody VHH17
-
additional information
-
development and synthesis of small molecule inhibitors of BoNTA endopeptidase, that antagonize the extracellular or intracellular toxin, in vivo pharmacokinetics in mice, overview. Extended multiple molecular dynamics simulations of inhibitor-enzyme complex formations, overview
-
additional information
-
development of llama single domain antibodies specific for the seven botulinum neurotoxin serotypes as heptaplex immunoreagents. A single llama is immunized with a cocktail of seven BoNT toxoids to generate a phage display library of single domain antibodies, sdAb, VHH or nanobodies, which are selected on live toxins. Several sdAb act as both captor and tracer for several toxin and toxin complexes suggesting sdAb can be used as architectural probes to indicate BoNT oligomerisation, cross reactivities, overview
-
additional information
-
development of specific potent inhibitors of BoNT/A light chain, structure-activity relationship studies, overview
-
additional information
-
evaluation of relevant and available in vitro cell-based assays and in vivo assays for drug discovery and development, especially with regard to the potential for medium- to high-throughput automation and its use in identifying physiologically relevant inhibitors. BoNT intoxication steps as targets for inhibitors, schematic overview. Because all BoNT serotypes require the acidification step for inducing muscle failure, developing pan inhibitors that target this stage is an attractive approach. The cell entry of the toxin is inhibited by plant and animal lectines, glycoconjugates, and antibodies. The SNARE cleavage is inhibited by small molecule, peptide, and peptidomimetic inhibitors
-
additional information
-
identification of three RNA aptamers from a ssDNA random library through SELEX-process, which bind strongly to the light chain of type A BoNT and inhibit the endopeptidase activity, with IC50 in low nM range. Inhibition kinetic studies reveal low nM KI and non-competitive nature of their inhibition, enzyme docking study, and inhibition kinetics, overview
-
additional information
-
inhibition of enzymatic activity of botulinum neurotoxins/A1, /A2, and /A3 by a panel of monoclonal anti-BoNT/A antibodies
-
additional information
-
inhibitor virtual screening performed by computationally docking compounds of the NCI database into the active site of BoNT/A light chain, inhibition studies in neuroblastoma N2a cell-based and tissue-based mouse phrenic nerve hemidiaphragm assays, overview. Five quinolinol-based analogues effectively neutralize BoNT/A toxicity, with CB 7969312 exhibiting ex vivo protection at 500 nM
-
additional information
-
monoclonal antibodies F1-2 and F1-40 do not inhibit the catalytic activity of BoNT/A, but inhibit the entry of the toxin into host neuronal cells, leading to reduced toxicity to mice, and block intracellular SNAP25 cleavage, overview
-
additional information
-
regions on BoNT/B that bind to blocking antibodies, synaptotagmin, or gangliosides, recognition pattern, overview
-
additional information
-
semisynthetic strategy to identify inhibitors based on toosendanin, a traditional Chinese medicine reported to protect from BoNT intoxication, overview. No inhibition by deacetylted toosendanin and by toosendanin ketone and lactone analogues
-
additional information
-
the toxicity of the enzyme is reduced in absence of gangliosides
-
additional information
-
a tetrapeptide provides an optimum length as the most efficient peptide inhibitor that binds at the active site normally occupied by the substrate. The peptides survive within neurons for at least 40 h and inhibit BoNT/A activity within two primary neuronal cells without showing any apparent cellular toxicity
-
additional information
P10845
not inhibited by artemisin
-
additional information
-
peptide HN729-845(corresponding to the BoNT/A region comprising heavy-chain N-terminal domain residues 729 to 845) is able to inhibit the binding of 125I-labeled serotype BoNT/A to synaptosomes
-
additional information
-
the C-terminal peptides of LcB-1, LcC1-1, LcD-1, and LcF-1 show no inhibitory effect
-
additional information
the receptor-binding domain of botulinum neurotoxin serotype B significantly delays intoxication by botulinum neurotoxin serotype B
-
additional information
-
the recombinant subtype A4 neurotoxin is effectively neutralized by botulism heptavalent antitoxin
-
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0.000001
VAMP 22-58/Gln58D-cysteine
Clostridium botulinum
pH not specified in the publication, temperature not specified in the publication
-
0.0000019
VAMP 27-58/Gln58D-cysteine
Clostridium botulinum
pH not specified in the publication, temperature not specified in the publication
-
0.007
(2E)-2-(1H-benzimidazol-2-yl)-3-(3-iodo-4-methoxyphenyl)prop-2-enenitrile
Clostridium botulinum
-
37°C, pH not specified in the publication
0.0004 - 0.0009
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
0.025
(2E)-3-(2-amino-4-chlorophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.0007
(2E)-3-(2-bromo-4-chlorophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.0044
(2E)-3-(4-chloro-2-fluorophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.013
(2E)-3-(4-chloro-2-hydroxyphenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.009
(2E)-3-(4-chloro-2-methoxyphenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.0008
(2E)-3-(4-chloro-2-methylphenyl)-N-hydroxyprop-2-enamide
0.002
(2E)-3-(4-chloro-2-nitrophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.015
(2E)-3-(4-chlorophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.012
(2E)-3-[4-chloro-2-(iminomethyl)phenyl]-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.0051
(2E)-3-[4-chloro-2-(methylsulfanyl)phenyl]-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.017
(2E)-3-[4-chloro-2-(methylsulfonyl)phenyl]-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.0006
(2E)-3-[4-chloro-2-(trifluoromethyl)phenyl]-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.01
(3alpha,5beta,7alpha,12alpha,17alpha)-24-([2-[(7-chloroquinolin-4-yl)amino]ethyl]amino)cholane-3,7,12-triyl triacetate
Clostridium botulinum
P10845
pH and temperature not specified in the publication
0.001
(3R)-3-(2,4-dichlorophenyl)-N,5-dihydroxypentanamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.008
(3R)-3-(4-chlorophenyl)-N,5-dihydroxypentanamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.021
(3S)-3-(2,4-dichlorophenyl)-N,5-dihydroxypentanamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.036
(3S)-3-(4-chlorophenyl)-N,5-dihydroxypentanamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.0027
2'-((9H-fluoren-2-ylamino)carbonyl)-4,4'-bis(hydroxy(oxido)amino)[1,1'-biphenyl]-2-carboxylic acid
Clostridium botulinum
-
at pH 7.4 and 37°C
0.0009
2,4-dichlorocinnamic acid hydroxamate
Clostridium botulinum
-
-
0.0003
2,4-dichlorocinnamic hydroxamate
Clostridium botulinum
-
-
0.059
2-(1H-benzo[d]imidazol-2-yl)-3-(5-(furan-2-yl)thiophen-2-yl)acrylonitrile
Clostridium botulinum
-
37°C, pH not specified in the publication
0.086
2-(1H-benzo[d]imidazol-2-yl)-3-(biphenyl-4-yl)acrylonitrile
Clostridium botulinum
-
37°C, pH not specified in the publication
0.025
2-(4-(2,4-dichlorophenoxy)phenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-(2-chloro-4-cyanophenoxy)phenyl)-1H-indole-6-carbonitrile
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.03
2-(4-(2-chloro-4-cyanophenoxy)phenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.054
2-(4-(4-(6-(1,4,5,6-tetrahydropyrimidin-2-yl)benzo[b]thiophen-2-yl)phenoxy)phenyl)-1,4,5,6-tetrahydropyrimidine
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.0071
2-(4-(4-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)phenoxy)phenyl)-4,5-dihydro-1H-imidazole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.0073
2-(4-(4-(6-(5-hydroxy-1,4,5,6-tetrahydropyrimidin-2-yl)-1H-indol-2-yl)phenoxy)phenyl)-1,4,5,6-tetrahydropyrimidin-5-ol
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-(4-carbamoylphenoxy)phenyl)-1H-indole-6-carboxamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.025
2-(4-(4-cyanophenoxy)phenyl)-1H-indole-6-carboximidamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-(4-cyanophenoxy)phenyl)indole-6-carbonitrile
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-(6-(1,4,5,6-tetrahydropyrimidin-2-yl)benzo[b]thiophen-2-yl)phenyl)-1,4,5,6-tetrahydropyrimidine
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.043
2-(4-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)-phenyl)-4,5-dihydro-1H-imidazole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-fluorophenyl)-1H-indole-6-carbonitrile
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-fluorophenyl)-1H-indole-6-carboxamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-fluorophenyl)-1H-indole-6-carboximidamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-methoxyphenyl)-1H-indole-6-carboxamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(4-methoxyphenyl)-1H-indole-6-carboximidamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.045
2-(4-methoxyphenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(5-(4-cyanophenoxy)pyridin-2-yl)-1H-indole-6-carbonitrile
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
2-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarboxamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.097
2-(pyridin-2-ylamino)cyclohexa-2,5-diene-1,4-dione
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.12
2-amino-N-(4-phenoxyphenyl)acetamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.417
2-amino-N-[3-(benzyloxy)phenyl]acetamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0007
2-methyl-7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0014
2-methyl-7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0046
2-methyl-7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.094
2-[1-cyano-2-(3-bromo-5-methoxy-4-hydroxyphenyl)vinyl]benzimidazole
Clostridium botulinum
-
37°C, pH not specified in the publication
0.059
2-[1-cyano-2-(3-chloro-5-methoxy-4-hydroxyphenyl)vinyl]benzimidazole
Clostridium botulinum
-
37°C, pH not specified in the publication
0.04
3'-O-ethyl-dynasore
Clostridium botulinum
A5HZZ9
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.0098
3,9-dichloro-6-(5,7-dichloro-9H-fluoren-2-yl)-5H-dibenzo[c,e]azepine-5,7(6H)-dione
Clostridium botulinum
-
at pH 7.4 and 37°C
0.026
3-(2,20-bithiophen-5-yl)-2-(1H-benzo-imidazol-2-yl)acrylonitrile
Clostridium botulinum
-
37°C, pH not specified in the publication
0.00097
3-(2,4-dichlorophenyl)-5-(4-fluorophenethoxy)-N-hydroxypentanamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0011
3-(2,4-dichlorophenyl)-N1-(4-fluoro-2-methoxyphenyl)-N5-hydroxypentanediamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0026
3-(2,4-dichlorophenyl)-N1-(4-fluorophenethyl)-N5-hydroxypentanediamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0067
3-(2,4-dichlorophenyl)-N1-hydroxy-N5-(4-methoxyphenethyl)pentanediamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.002
3-(2,4-dichlorophenyl)-N1-hydroxy-N5-(o-tolyl)pentanediamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.073
3-(4-(1H-imidazol-1-yl)phenyl)-2-(1H-benzoimidazol-2-yl)acrylonitrile
Clostridium botulinum
-
37°C, pH not specified in the publication
0.003
3-(4-chloro-2-methylphenyl)-N-hydroxypropanamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.04
3-hydroxy-N'-[(E)-(2-hydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
Clostridium botulinum
A5HZZ9
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.00194
3-hydroxy-N'-[(E)-(3,4,5-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
Clostridium botulinum
A5HZZ9
pH and temperature not specified in the publication
0.04
3-hydroxy-N'-[(E)-(3-hydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
Clostridium botulinum
A5HZZ9
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.0024
3-hydroxy-N-phenylanthracene-2-carboxamide
Clostridium botulinum
-
at pH 7.4 and 37°C
0.04
3H-dynasore
Clostridium botulinum
A5HZZ9
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.04
3H-dyngo-4a
Clostridium botulinum
A5HZZ9
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.0032
4,4'-dichloro-2'-((9H -fluoren-2-ylamino)carbonyl)[1,1'-biphenyl]-2-carboxylic acid
Clostridium botulinum
-
at pH 7.4 and 37°C
0.003
4,4'-dichloro-2'-[(5,7-dichloro-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
Clostridium botulinum
-
at pH 7.4 and 37°C
0.0058
4-chloro-(3-fluorophenyl)methyl benzenesulfonamide
Clostridium botulinum
-
at pH 7.4 and 25°C
0.0033
4-chloro-N-[(4-fluorophenyl)methyl] pyridin-3-amine
Clostridium botulinum
-
at pH 7.4 and 25°C
0.015
4-chlorocinnamic hydroxamate
Clostridium botulinum
-
-
0.013
5-((3-bromoadamantan-1-yl)methoxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0054
5-(allyloxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0029
5-(benzyloxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0007
5-chloro-7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0006
5-chloro-7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0022
5-chloro-7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0014
5-chloro-7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0007
5-chloro-7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.004
5-chloro-7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0006
5-chloro-7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0023
5-chloro-7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0007
5-chloro-7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0015
5-chloro-7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0035
5-chloro-7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0045
5-chloro-7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.028
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy)phenyl)-1H-benzo[d]imidazole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.021
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy)phenyl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.067
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-{5-[4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy]pyridin-2-yl}-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
6-(3,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(3,4,5,6-tetrahydropyrimidin-2-yl)phenyl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.02
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4,5-dihydro-1H-imidazol-2-yl)phenyl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.0245
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)phenyl)-1H-benzo[d]imidazole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.0125
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)phenyl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.1
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-fluorophenyl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.069
6-(4,5-dihydroimidazol-2-yl)-2-(5-(4-(4,5-dihydroimidazol-2-yl)phenoxy)pyridine-2-yl)indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.071
6-bromo-N-hydroxynaphthalene-2-carboxamide
Clostridium botulinum
-
-
0.1
6-chloro-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)-phenyl)-1H-indole
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.045
6-chloro-N-hydroxy-1-benzothiophene-2-carboxamide
Clostridium botulinum
-
-
0.038
6-chloro-N-hydroxy-1-methyl-1H-indole-2-carboxamide
Clostridium botulinum
-
-
0.041
6-chloro-N-hydroxy-1H-indene-2-carboxamide
Clostridium botulinum
-
-
0.021
6-chloro-N-hydroxynaphthalene-2-carboxamide
Clostridium botulinum
-
-
0.2
6-[(2,5-dimethoxyphenyl)amino]-N-(4-phenoxybenzyl)picolinamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0023
6-[(3,6-dioxocyclohexa-1,4-dien-1-yl)amino]-N-(4-phenoxybenzyl)picolinamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0027
7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0036
7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0123
7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0044
7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0043
7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0127
7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0014
7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0012
7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0007
7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0024
7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.012
7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0019
7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0016
7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0041
7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0008
7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0046
7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0042
7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0017
7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0015
7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0062
7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0027
7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
Clostridium botulinum
-
pH and temperature not specified in the publication
0.0113
bis-aminoquinoline
Clostridium botulinum
P10845
at pH 7.3 and 37°C
0.0293
dynasore
Clostridium botulinum
A5HZZ9
pH and temperature not specified in the publication
0.06
L-Arginine hydroxamate
Clostridium botulinum
-
-
0.007
methyl 3alpha-(N-[(7-chloroquinolin-4-yl)amino]ethyl)amino,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
Clostridium botulinum
-
-
0.017
methyl 3beta-(N-[(7-chloroquinolin-4-yl)amino]ethyl)amino,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
Clostridium botulinum
-
-
0.014
methyl 6-[(3,6-dioxocyclohexa-1,4-dien-1-yl)amino]picolinate
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0025
N'-(2-(dimethylamino)ethyl)-2-(4-(4-(N'-2-(dimethylaminoethyl)carbamimidoyl)phenoxy)phenyl)-1H-indole-6-carboximidamide
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.04
N'-[(E)-(2,4,5-trihydroxyphenyl)methylidene]benzohydrazide
Clostridium botulinum
A5HZZ9
IC50 above 0.04 mM, pH and temperature not specified in the publication
0.00625
N'-[(E)-(2,4,5-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
Clostridium botulinum
A5HZZ9
pH and temperature not specified in the publication
0.01
N-(3alpha,7alpha,12alpha-triacetoxy-5beta-cholan-24-yl)-N'-(7'-chloroquinolin-4'-yl)-ethane-1,2-diamine
Clostridium botulinum
-
-
0.57
N-(4-phenoxybenzyl)picolinamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0189
N-(7-chloroquinolin-4-yl)-N'-adamantylethane-1,2-diamine
Clostridium botulinum
P10845
pH and temperature not specified in the publication
0.1
N-(pyridin-2-yl)prop-2-enamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.048
N-(pyridin-3-yl)prop-2-enamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.04
N-([1,1'-biphenyl]-4-ylmethyl)-1-(2,5-dimethoxybenzyl)-1H-1,2,4-triazole-3-carboxamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0025
N-([1,1'-biphenyl]-4-ylmethyl)-1-[(3,6-dioxocyclohexa-1,4-dien-1-yl)methyl]-1H-1,2,4-triazole-3-carboxamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.21
N-([1,1'-biphenyl]-4-ylmethyl)-1H-1,2,4-triazole-3-carboxamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.16
N-([1,1'-biphenyl]-4-ylmethyl)-2-aminoacetamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.041
N-hydroxy-4-pentylbenzamide
Clostridium botulinum
-
pH not specified in the publication, temperature not specified in the publication
0.025
N-[3-(benzyloxy)phenyl]-2-[(2,5-dimethoxybenzyl)amino]acetamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.018
N-[3-(benzyloxy)phenyl]-2-[[(3,6-dioxocyclohexa-1,4-dien-1-yl)methyl]amino]acetamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0092
N1-(2-cyclopropylethyl)-3-(2,4-dichlorophenyl)-N5-hydroxypentanediamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.0064
N1-(4-bromophenyl)-3-(2,4-dichlorophenyl)-N5-hydroxypentanediamide
Clostridium botulinum
A5HZZ9
at pH 7.4 and 37°C
0.056
N1-(6-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)-pyridine-3-yl)ethane-1,2-diamine
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.011
NSC 240898
Clostridium botulinum
-
pH 7.4, 37°C, BoNT/A light chain
0.0052
paclitaxel
Clostridium botulinum
P10845
at pH 8.2 and 37°C
0.00000047
single-domain llama antibody Aa1
Clostridium botulinum
-
pH not specified in the publication, temperature not specified in the publication
-
0.0032
tris[3-(7-chloroquinolin-4-yl)aminopropyl]amine
Clostridium botulinum
-
-
0.0004
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
pH 7.4, 22.5°C
0.0009
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
pH not specified in the publication, temperature not specified in the publication
0.0008
(2E)-3-(4-chloro-2-methylphenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
-
0.0008
(2E)-3-(4-chloro-2-methylphenyl)-N-hydroxyprop-2-enamide
Clostridium botulinum
-
pH not specified in the publication, temperature not specified in the publication
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E110A
the mutant shows similar activity to wild-type BoNT/F
K29A
the BoNT F K29A mutation does not abrogate VAMP cleavability
R133A
the BoNT/F mutant shows over 95% reduced activity with VAMP substrate compared to the wild-type enzyme
R133K
the BoNT/F mutant shows over 95% reduced activity with VAMP substrate compared to the wild-type enzyme
R171K
the exosite 1 variant BoNT F shows about 98% reduction in activity with VAMP compared to the wild-type enzyme
Y361A
the BoNT/F mutant shows about 18% reduction in activity with VAMP compared to the wild-type enzyme
A308L
-
the mutant shows 8.7% of wild type SNAP-25 cleavage activity
A308V
-
the mutant shows 86.4% of wild type SNAP-25 cleavage activity
C134A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
C461S
the mutant shows similar levels of activity as the wild type enzyme
C467S
the mutant shows similar levels of activity as the wild type enzyme
D130A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
D161A
-
the mutant exhibits a 1000fold reduction of wild type activity
D341A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
D342C
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
D369N
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
D370A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
D370R
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
D426A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
D70A
-
the mutant exhibits a 10fold reduction of wild type activity
D877N
the mutant shows 20% reduced neurotoxicity compared to the wild type
E1172A
-
the binding of radioactively-labeled, in vitro translated HCE E1172A to rat brain synaptosomes is highly decreased to 8.5% of wild-type levels, as well as the binding of Escherichia coli derived HCE mutants to isolated GT1b
E1191C/S1199W
-
the mutations enhance enzyme binding to human synaptotagmin II and human synaptotagmin I
E1191Q/S1199W
-
the mutation enhances binding to the human receptor synaptotagmin 2
E1191V/S1199W
-
the mutations enhance enzyme binding to human synaptotagmin II and human synaptotagmin I
E1195A
-
the HCF mutant E1195A displays a diminished affinity of 31.6% to synaptosomes as well as a reduction of about 85% in binding to isolated GT1b compared to HCF wild-type
E147A/E308A
-
the mutant exhibits a 5fold reduction of wild type activity
E147R
-
the mutant exhibits a 80fold reduction of wild type activity
E148A
-
the mutant shows 8.2% of wild type SNAP-25 cleavage activity
E148K
-
the mutant shows 1.7% of wild type SNAP-25 cleavage activity
E148R
-
the mutant shows 4.0% of wild type SNAP-25 cleavage activity
E158A/T159A/N160A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 7.4fold lower than the wild-type value
E163L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E163Q
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E170A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E200A
-
Km (VAMP-2) similar to wild-type, kcat strongly decreased compared to wild-type
E212A/E335Q
-
no detectable activity with synaptosome-associated protein SNAP-25
E224A
-
the mutation abrogates the catalytic activity of the endopeptidase of BoNT/A
E224A/E262A
-
the recombinant full length botulinum type A with mutation in its two active site residues is a detoxified BoNT/A mutant since it lacks its endopeptidase activity
E224D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E224Q/H227Y
the mutation removes the endopeptidase activity of BoNT/A LH fragment
E224Q/R363A/Y366F
P10845
enzymatically inactive
E231Q/H234Y
the mutation removes the endopeptidase activity of BoNT/B LH fragment
E249A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 20fold lower than the wild-type value
E256A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme in addition of ZnCl2 but not in absence of it, the ratio of activity in absence or presence of exogenous ZnCl2 is altered compared to the wild-type enzyme
E257A
-
site-directed mutagenesis, mutation of an S4' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
E257K
-
site-directed mutagenesis, mutation of an S4' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
E262D
-
site-directed mutagenesis, the mutant shows a three-fold reduced activity compared to the wild-type enzyme
E262Q
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E272A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E280C
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E308R
-
the mutant exhibits a 0.8fold reduction of wild type activity
E315A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
E335A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 37fold lower than the wild-type value
E335Q
-
kcat/KM for synaptosome-associated protein SNAP-25 is 7300fold lower than the wild-type value. Mutation causes the toxin to transform into a persistent apoenzyme decoid of zinc
E346A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E399/D426A/F428A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows almost no channel forming activity
E399A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows unaltered channel forming activity compared to the wild-type enzyme
E399A/D425A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows almost no channel forming activity
E48Q
the mutant shows 64% reduced neurotoxicity compared to the wild type
E48Q/D877N
the mutant shows 8% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
E48Q/E653K
the mutant shows 9% reduced neurotoxicity compared to the wild type
E48Q/E653Q
the mutant shows 38% reduced neurotoxicity compared to the wild type
E48Q/E653Q/D877N
the mutant shows 54% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
E54A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E63A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
E653 K/D877N
the mutant shows 28% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
E653K
the mutant shows 15% reduced neurotoxicity compared to the wild type
E653Q
the mutant shows 31% reduced neurotoxicity compared to the wild type
E653Q/D877N
the mutant shows 32% increased neurotoxicity due to faster cytosolic delivery of the enzymatic domain
F163A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
F194A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
F194A/T220A
-
site-directed mutagenesis, mutation of S1' pocket residues, the mutant shows reduced activity compared to the wild-type enzyme
F428A
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F428D
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F428W
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F428Y
-
site-directed mutagenesis, a C2II component mutant, the mutant shows altered chloroquine binding and almost no channel formation activity compared to the wild-type enzyme
F50A
the mutant shows wild type activity
F50A/I191A
the mutant shows 60fold activity reduction compared to the wild type enzyme
F50D
the mutant shows 4fold activity reduction compared to the wild type enzyme
F50D/I191D
the mutant shows 400fold activity reduction compared to the wild type enzyme
H1241K
mutant shows an increased affinity for GD1a and confers the ability to bind ganglioside GM1a
H132A
the mutant shows wild type activity
H132Q
the mutant shows 100fold activity reduction compared to the wild type enzyme
H223A
-
the mutation abrogates the catalytic activity of the endopeptidase of BoNT/A
H223A/E224A/H227A
-
site-directed mutagenesis of active site residues, catalytically inactive BoNT/A1 mutant
H227A
-
the mutation abrogates the catalytic activity of the endopeptidase of BoNT/A
H269A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
I115A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
I151A
the mutant shows 2fold activity reduction compared to the wild type enzyme
I151D
the mutant shows 1000fold activity reduction compared to the wild type enzyme
I152D
the mutant shows 2fold activity reduction compared to the wild type enzyme
I191A
the mutant shows wild type activity
I191D
the mutant shows 4fold activity reduction compared to the wild type enzyme
I52A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
K165L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
K172A
-
Km (VAMP-2) increased compared to wild-type, kcat moderately decreased compared to wild-type
K218R
-
the mutant exhibits an 8fold reduction of wild type activity
K224D
-
mutation of BoNT/E light chain. The mutant shows extended substrate specificity to cleave SNAP-23, and the natural substrate, SNAP-25, but not SNAP-29 or SNAP-47, introduction into HeLa cells
K23A
-
the mutant shows 111% of wild type SNAP-25 cleavage activity
K23D
-
the mutant shows 72% of wild type SNAP-25 cleavage activity
K337A
-
the mutant shows 55% of wild type SNAP-25 cleavage activity
K337E
-
the mutant shows 28.5% of wild type SNAP-25 cleavage activity
K340A
-
the mutant shows 99.5% of wild type SNAP-25 cleavage activity
K340D
-
the mutant shows 71.5% of wild type SNAP-25 cleavage activity
K340H
-
the mutant shows 64.1% of wild type SNAP-25 cleavage activity
K340R
-
the mutant shows 147.5% of wild type SNAP-25 cleavage activity
K41A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
K58A
-
the mutant exhibits a 250fold reduction of wild type activity
L173A
-
Km (VAMP-2) increased compared to wild-type, kcat moderately decreased compared to wild-type
L175A
-
site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
L175A/R177A
-
site-directed mutagenesis, mutation of S5 pocket residues, the mutant shows reduced activity compared to the wild-type enzyme
L200A
the mutant shows 2fold activity reduction compared to the wild type enzyme
L200D
the mutant shows 8fold activity reduction compared to the wild type enzyme
L256E
-
the mutant shows 13.9% of wild type SNAP-25 cleavage activity
L256E/V258P
-
the mutant shows 49.3% of wild type SNAP-25 cleavage activity
L260F/I264R
-
these mutations do not alter the activity of the enzyme
M106A
-
the mutant shows 73% of wild type SNAP-25 cleavage activity
M344A
-
the mutant shows 73% of wild type SNAP-25 cleavage activity
N26D
-
the mutant shows 90.8% of wild type SNAP-25 cleavage activity
N26K
-
the mutant shows 82.8% of wild type SNAP-25 cleavage activity
P154D
the mutant shows 4fold activity reduction compared to the wild type enzyme
P25A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
Q138G/P139G/D140G
-
site-directed mutagenesis, the mutant is no longer recognized by antibody F1-40
Q161A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
Q34A
-
the mutation reduces the VAMP-2 cleavability by about 3fold compared to the wild type enzyme
Q66A
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
R1111A/H1241K/R1256A
triple mutant binds GD1a 17fold greater than the double-mutant
R1111A/R1256A
triple mutant binds GD1a 17fold greater than the double-mutant
R133A
-
the mutant exhibits a 300fold reduction of wild type activity
R171A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
R177D
-
the mutant shows 77% of wild type SNAP-25 cleavage activity
R230K
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
R23A
the mutant shows wild type activity
R23D/H132A
the mutant shows 25fold activity reduction compared to the wild type enzyme
R240A
-
Km (VAMP-2) similar to wild-type, kcat decreased compared to wild-type
R263A
-
Km (VAMP-2) similar to wild-type, kcat decreased compared to wild-type
R347A
-
kcat/KM for synaptosome-associated protein SNAP-25 is 1060fold lower than the wild-type value
R362L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
R372A
the mutant shows 40fold activity reduction compared to the wild type enzyme
R63A
the mutant shows 10fold activity reduction compared to the wild type enzyme
R63E
the mutant shows 50fold activity reduction compared to the wild type enzyme
S147A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
S224A
-
Km (VAMP-2) similar to wild-type, kcat decreased compared to wild-type
S28E
-
the mutation reduces the VAMP-2 cleavability by about 2fold compared to the wild type enzyme
T132D
-
the mutant shows 42.5% of wild type SNAP-25 cleavage activity
T176A
-
site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
T192A
-
the mutant exhibits a 3fold reduction of wild type activity
T220A
-
site-directed mutagenesis, mutation of an S1' pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
V129A
-
site-directed mutagenesis, mutation of a binding site residue, the mutant shows reduced activity compared to the wild-type enzyme
V137A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
V148/I151A
the mutant shows 15fold activity reduction compared to the wild type enzyme
V148A
the mutant shows wild type activity
V148D
the mutant shows wild type activity
V258A
-
the mutant shows 33.1% of wild type SNAP-25 cleavage activity
W1224L
-
the binding of radioactively-labeled, in vitro translated HCE W1224L to rat brain synaptosomes is highly decreased to 3.7% of wild-type levels, as well as the binding of Escherichia coli derived HCE mutants to isolated GT1b
W1250L
-
the HCF mutant W1250L displays a diminished affinity of 20.5% to synaptosomes as well as a reduction of about 85% in binding to isolated GT1b compared to HCF wild-type
W1266L
-
the mutant HCA W1266L that lacks ganglioside binding, does not interfere with BoNT/A neurotoxicity
W315A
the mutant shows 20fold activity reduction compared to the wild type enzyme
W315D
the mutant shows 40fold activity reduction compared to the wild type enzyme
W319A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
W44A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
W44A/I152A/P154A
the mutant shows 20fold activity reduction compared to the wild type enzyme
W44D
the mutant shows 2fold activity reduction compared to the wild type enzyme
Y113A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
Y133A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
Y168A/L200A
the mutant shows 2fold activity reduction compared to the wild type enzyme
Y168D
the mutant shows 2fold activity reduction compared to the wild type enzyme
Y168D/L200D
the mutant shows 60fold activity reduction compared to the wild type enzyme
Y183A
-
the mutant exhibits a 3.2fold reduction of wild type activity
Y183A/Y239A
-
the mutant exhibits a 1000fold reduction of wild type activity
Y239A
-
the mutant exhibits an 8fold reduction of wild type activity
Y26A/Y50A/T192A
-
the mutant exhibits a 600fold reduction of wild type activity
Y322A
-
Km (VAMP-2) increased compared to wild-type, kcat similar to wild-type
Y350A
-
no detectable activity with synaptosome-associated protein SNAP-25
Y365F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y368A
-
Km (VAMP-2) similar to wild-type, kcat strongly decreased compared to wild-type
Y50A
-
the mutant exhibits a 10fold reduction of wild type activity
E1191M/S1199Y
-
the mutant exhibits about 11fold higher efficacy in blocking neurotransmission than wild type botulinum neurotoxin B in neurons expressing human synaptotagmin II
E1191M/S1199Y
-
the mutation enhances binding to the human receptor synaptotagmin 2
Q162A
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
Q162A
-
the mutant shows 110% of wild type SNAP-25 cleavage activity
R177A
-
site-directed mutagenesis, mutation of an S5 pocket residue, the mutant shows reduced activity compared to the wild-type enzyme
R177A
-
the mutant shows 82% of wild type SNAP-25 cleavage activity
R230L
-
inactive
R230L
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
Y168A
the mutant shows wild type activity
Y168A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
Y26A
-
Km (VAMP-2) increased compared to wild-type, kcat decreased compared to wild-type
Y26A
-
the mutant exhibits a 60fold reduction of wild type activity
Y365N
-
inactive
Y365N
-
site-directed mutagenesis, the mutant shows reduced activity and an altered ratio of activity in absence or presence of exogenous ZnCl2 compared to the wild-type enzyme
additional information
-
an insertion mutant moving Glu224 laterally by one residue is catalytically inactive
additional information
-
construction and growth-selection of chimeric SNARE mutations that inhibit proteolysis, when these mutations are introduced into Sb and examined for cleavage, substrate residues located near and distal to the cleavage site are important, including residues positioned near the Sb transmembrane domain, overview, additional mutations in a nine-residue SNARE motif
additional information
-
construction of a HCB-Syt-II fusion protein by fusion of the HC fragment of BoNT/B, residues 858-1291, with the luminal domain of rat Syt-II, residues 861, connected by a 15-residue linker, PPTPGSAWSHPQFEK, including a Strep-tag, site-directed mutagenesis analysis of the toxin-receptor binding site in BoNT/B and in the luminal domains of Syt-I and Syt-II, overview
additional information
construction of BoNT AE and EA chimeras from serotypes BoNT/A and BoNT/E in DC and SC forms, overview, catalytic and physiological properties of the chimeric forms, overview
additional information
-
an atoxic derivative of BoNT/A (BoNT/A ad) as a full-length 150 kDa molecule consisting of a 50 kDa light chain and a 100 kDa heavy chain joined by a disulfide bond and metalloprotease-inactivating point mutations (E224A/Y366A) in the light chain. Studies in neuronal cultures demonstrates that the mutant is unable to cleave SNAP25, and that it effectively competes with wild-type BoNT/A for binding to endogenous neuronal receptors. In vivo studies indicate accumulation of the mutant (BoNT/A ad) at the neuromuscular junction of the mouse diaphragm. Toxicity of the mutant BoNT/A ad is reduced by 100000fold relative to wild-type BoNT/A
additional information
-
an atoxic derivative of BoNT/A (BoNT/A ad) as a full-length 150 kDa molecule consisting of a 50 kDa light chain and a 100 kDa heavy chain joined by a disulfide bond and metalloprotease-inactivating point mutations (E224A/Y366A) in the light chain. Studies in neuronal cultures demonstrates that the mutant is unable to cleave SNAP25, and that it effectively competes with wild-type BoNT/A for binding to endogenous neuronal receptors. In vivo studies indicate accumulation of the mutant (BoNT/A ad) at the neuromuscular junction of the mouse diaphragm. Toxicity of the mutant BoNT/A ad is reduced by 100000fold relative to wild-type BoNT/A
additional information
-
four variants of type A BoNT (BoNT/A) light chain are prepared and their catalytic parameters with those of BoNT/A whole toxin are compared. The four variants are light chain + translocation domain, a trypsin-nicked light chain + translocation domain, light chain + belt, and a free light chain. Km (SNAP-25) (synaptosomal associated protein of 25 kDa) for these constructs is not very different, but kcat for the free light chain is 6-100fold higher than those of its four variants. None of the four variants of the light chain is prone to autocatalysis
additional information
-
the endopeptidase activities of the three forms (complex, purified BoNT/B holotoxin, and separated light chain) are compared under the same conditions. Results show that enzyme activities of the three forms differ significantly and are dependent on nicking and disulfide reduction conditions. Light chain form has the highest level of activity, and the complex has the lowest. The activity is enhanced by nicking of BoNT/B holotoxin and is enhanced even more by dithiothreitol reduction after nicking
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Formation of a biologically active toxin complex of the binary Clostridium botulinum C2 toxin without cell membrane interaction
Biochemistry
45
13361-13368
2006
Clostridium botulinum
brenda
Jin, R.; Sikorra, S.; Stegmann, C.M.; Pich, A.; Binz, T.; Brunger, A.T.
Structural and biochemical studies of botulinum neurotoxin serotype C1 light chain protease: implications for dual substrate specificity
Biochemistry
46
10685-10693
2007
Clostridium botulinum, Clostridium tetani
brenda
Silvaggi, N.R.; Wilson, D.; Tzipori, S.; Allen, K.N.
Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex
Biochemistry
47
5736-5745
2008
Clostridium botulinum (P10845), Clostridium botulinum
brenda
Kukreja, R.V.; Sharma, S.; Cai, S.; Singh, B.R.
Role of two active site Glu residues in the molecular action of botulinum neurotoxin endopeptidase
Biochim. Biophys. Acta
1774
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2007
Clostridium botulinum
brenda
Capkova, K.; Yoneda, Y.; Dickerson, T.J.; Janda, K.D.
Synthesis and structure-activity relationships of second-generation hydroxamate botulinum neurotoxin A protease inhibitors
Bioorg. Med. Chem. Lett.
17
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2007
Clostridium botulinum
brenda
Teymoortash, A.; Sommer, F.; Mandic, R.; Schulz, S.; Bette, M.; Aumueller, G.; Werner, J.A.
Intraglandular application of botulinum toxin leads to structural and functional changes in rat acinar cells
Br. J. Pharmacol.
152
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2007
Clostridium botulinum
brenda
Silvaggi, N.R.; Boldt, G.E.; Hixon, M.S.; Kennedy, J.P.; Tzipori, S.; Janda, K.D.; Allen, K.N.
Structures of Clostridium botulinum neurotoxin serotype A light chain complexed with small-molecule inhibitors highlight active-site flexibility
Chem. Biol.
14
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2007
Clostridium botulinum
brenda
Yerdelen, D.; Koc, F.; Sarica, Y.
Effects of botulinum toxin on strength-duration properties
Int. J. Neurosci.
117
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2007
Clostridium botulinum
brenda
McAllister, L.A.; Hixon, M.S.; Kennedy, J.P.; Dickerson, T.J.; Janda, K.D.
Superactivation of the botulinum neurotoxin serotype A light chain metalloprotease: a new wrinkle in botulinum neurotoxin
J. Am. Chem. Soc.
128
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2006
Clostridium botulinum
brenda
Chen, S.; Kim, J.J.; Barbieri, J.T.
Mechanism of substrate recognition by botulinum neurotoxin serotype A
J. Biol. Chem.
282
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Clostridium botulinum
brenda
Wang, J.; Meng, J.; Lawrence, G.W.; Zurawski, T.H.; Sasse, A.; Bodeker, M.O.; Gilmore, M.A.; Fernandez-Salas, E.; Francis, J.; Steward, L.E.; Aoki, K.R.; Dolly, J.O.
Novel chimeras of botulinum neurotoxin /A and /E unveil contributions from the binding, translocation and protease domains to their functional characteristics
J. Biol. Chem.
283
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2008
Clostridium botulinum (Q00496)
brenda
Kumaran, D.; Rawat, R.; Ludivico, M.L.; Ahmed, S.A.; Swaminathan, S.
Structure and substrate based inhibitor design for clostridium botulinum neurotoxin serotype A
J. Biol. Chem.
283
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2008
Clostridium botulinum (P10845), Clostridium botulinum
brenda
Neumeyer, T.; Schiffler, B.; Maier, E.; Lang, A.E.; Aktories, K.; Benz, R.
Clostridium botulinum C2 toxin. Identification of the binding site for chloroquine and related compounds and influence of the binding site on properties of the C2II channel
J. Biol. Chem.
283
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2008
Clostridium botulinum
brenda
Sinha, J.; Inan, M.; Fanders, S.; Taoka, S.; Gouthro, M.; Swanson, T.; Barent, R.; Barthuli, A.; Loveless, B.M.; Smith, L.A.; Smith, T.; Henderson, I.; Ross, J.; Meagher, M.M.
Cell bank characterization and fermentation optimization for production of recombinant heavy chain C-terminal fragment of botulinum neurotoxin serotype E (rBoNTE(H(c)): antigen E) by Pichia pastoris
J. Biotechnol.
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Clostridium botulinum, Clostridium botulinum NCTC 11219
brenda
Burnett, J.C.; Opsenica, D.; Sriraghavan, K.; Panchal, R.G.; Ruthel, G.; Hermone, A.R.; Nguyen, T.L.; Kenny, T.A.; Lane, D.J.; McGrath, C.F.; Schmidt, J.J.; Vennerstrom, J.L.; Gussio, R.; Solaja, B.A.; Bavari, S.
A refined pharmacophore identifies potent 4-amino-7-chloroquinoline-based inhibitors of the botulinum neurotoxin serotype A metalloprotease
J. Med. Chem.
50
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2007
Clostridium botulinum
brenda
Jin, R.; Rummel, A.; Binz, T.; Brunger, A.T.
Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
Nature
444
1092-1095
2006
Clostridium botulinum
brenda
Tang, J.; Park, J.G.; Millard, C.B.; Schmidt, J.J.; Pang, Y.P.
Computer-aided lead optimization: improved small-molecule inhibitor of the zinc endopeptidase of botulinum neurotoxin serotype A
PLoS ONE
2
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2007
Clostridium botulinum
brenda
Fang, H.; Luo, W.; Henkel, J.; Barbieri, J.; Green, N.
A yeast assay probes the interaction between botulinum neurotoxin serotype B and its SNARE substrate
Proc. Natl. Acad. Sci. USA
103
6958-6963
2006
Clostridium botulinum
brenda
Rawat, R.; Ashraf Ahmed, S.; Swaminathan, S.
High level expression of the light chain of botulinum neurotoxin serotype C1 and an efficient HPLC assay to monitor its proteolytic activity
Protein Expr. Purif.
60
165-169
2008
Clostridium botulinum
brenda
Suzuki, T.; Kouguchi, H.; Watanabe, T.; Hasegawa, K.; Yoneyama, T.; Niwa, K.; Nishikawa, A.; Lee, J.C.; Oguma, K.; Ohyama, T.
Effect of nicking the C-terminal region of the Clostridium botulinum serotype D neurotoxin heavy chain on its toxicity and molecular properties
Protein J.
26
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2007
Clostridium botulinum
brenda
Ahmed, S.A.; Olson, M.A.; Ludivico, M.L.; Gilsdorf, J.; Smith, L.A.
Identification of residues surrounding the active site of type A botulinum neurotoxin important for substrate recognition and catalytic activity
Protein J.
27
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2008
Clostridium botulinum
brenda
Antonucci, F.; Bozzi, Y.; Caleo, M.
Intrahippocampal infusion of botulinum neurotoxin E (BoNT/E) reduces spontaneous recurrent seizures in a mouse model of mesial temporal lobe epilepsy
Epilepsia
50
963-966
2009
Clostridium botulinum
brenda
Oeconomou, A.; Madersbacher, H.; Kiss, G.; Berger, T.J.; Melekos, M.; Rehder, P.
Is botulinum neurotoxin type A (BoNT-A) a novel therapy for lower urinary tract symptoms due to benign prostatic enlargement? A review of the literature
Eur. Urol.
54
765-775
2008
Clostridium botulinum
brenda
Antonucci, F.; Di Garbo, A.; Novelli, E.; Manno, I.; Sartucci, F.; Bozzi, Y.; Caleo, M.
Botulinum neurotoxin E (BoNT/E) reduces CA1 neuron loss and granule cell dispersion, with no effects on chronic seizures, in a mouse model of temporal lobe epilepsy
Exp. Neurol.
210
388-401
2008
Clostridium botulinum
brenda
Uchida, H.; Matsumoto, M.; Ueda, H.
Profiling of BoNT/C3-reversible gene expression induced by lysophosphatidic acid: ephrinB1 gene up-regulation underlying neuropathic hyperalgesia and allodynia
Neurochem. Int.
54
215-221
2009
Clostridium botulinum, Clostridium botulinum C3
brenda
Nuemket, N.; Tanaka, Y.; Tsukamoto, K.; Tsuji, T.; Nakamura, K.; Kozaki, S.; Yao, M.; Tanaka, I.
Preliminary X-ray crystallographic study of the receptor-binding domain of the D/C mosaic neurotoxin from Clostridium botulinum
Acta Crystallogr. Sect. F
66
608-610
2010
Clostridium botulinum (A5JGM8), Clostridium botulinum
brenda
Tsai, C.Y.; Chiu, W.C.; Liao, Y.H.; Tsai, C.M.
Effects on craniofacial growth and development of unilateral botulinum neurotoxin injection into the masseter muscle
Am. J. Orthod. Dentofacial. Orthop.
135
142.e1-6
2009
Clostridium botulinum
brenda
Rowe, B.; Schmidt, J.J.; Smith, L.A.; Ahmed, S.A.
Rapid product analysis and increased sensitivity for quantitative determinations of botulinum neurotoxin proteolytic activity
Anal. Biochem.
396
188-193
2010
Clostridium botulinum
brenda
Ozanich, R.M.; Bruckner-Lea, C.J.; Warner, M.G.; Miller, K.; Antolick, K.C.; Marks, J.D.; Lou, J.; Grate, J.W.
Rapid multiplexed flow cytometric assay for botulinum neurotoxin detection using an automated fluidic microbead-trapping flow cell for enhanced sensitivity
Anal. Chem.
81
5783-5793
2009
Clostridium botulinum
brenda
Montal, M.
Botulinum neurotoxin: a marvel of protein design
Annu. Rev. Biochem.
79
591-617
2010
Clostridium botulinum
brenda
Roxas-Duncan, V.; Enyedy, I.; Montgomery, V.A.; Eccard, V.S.; Carrington, M.A.; Lai, H.; Gul, N.; Yang, D.C.; Smith, L.A.
Identification and biochemical characterization of small-molecule inhibitors of Clostridium botulinum neurotoxin serotype A
Antimicrob. Agents Chemother.
53
3478-3486
2009
Clostridium botulinum
brenda
Poras, H.; Ouimet, T.; Orng, S.V.; Fournie-Zaluski, M.C.; Popoff, M.R.; Roques, B.P.
Detection and quantification of botulinum neurotoxin type A by a novel rapid in vitro fluorimetric assay
Appl. Environ. Microbiol.
75
4382-4390
2009
Clostridium botulinum
brenda
De Medici, D.; Anniballi, F.; Wyatt, G.M.; Lindstroem, M.; Messelhaeusser, U.; Aldus, C.F.; Delibato, E.; Korkeala, H.; Peck, M.W.; Fenicia, L.
Multiplex PCR for detection of botulinum neurotoxin-producing clostridia in clinical, food, and environmental samples
Appl. Environ. Microbiol.
75
6457-6461
2009
Clostridium botulinum (A2I2R9), Clostridium botulinum (Q58GH1), Clostridium botulinum
brenda
Lin, G.; Tepp, W.H.; Pier, C.L.; Jacobson, M.J.; Johnson, E.A.
Expression of the Clostridium botulinum A2 neurotoxin gene cluster proteins and characterization of the A2 complex
Appl. Environ. Microbiol.
76
40-47
2010
Clostridium botulinum
brenda
Raphael, B.H.; Choudoir, M.J.; Luquez, C.; Fernandez, R.; Maslanka, S.E.
Sequence diversity of genes encoding botulinum neurotoxin type F
Appl. Environ. Microbiol.
76
4805-4812
2010
Clostridium botulinum (C5IWN7), Clostridium botulinum (D2KCK3), Clostridium botulinum (P30996), Clostridium botulinum (Q58GH1), Clostridium botulinum, Clostridium baratii (Q45851), Clostridium baratii
brenda
Muraro, L.; Tosatto, S.; Motterlini, L.; Rossetto, O.; Montecucco, C.
The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane
Biochem. Biophys. Res. Commun.
380
76-80
2009
Clostridium botulinum
brenda
Chang, T.W.; Blank, M.; Janardhanan, P.; Singh, B.R.; Mello, C.; Blind, M.; Cai, S.
In vitro selection of RNA aptamers that inhibit the activity of type A botulinum neurotoxin
Biochem. Biophys. Res. Commun.
396
854-860
2010
Clostridium botulinum
brenda
Henkel, J.S.; Jacobson, M.; Tepp, W.; Pier, C.; Johnson, E.A.; Barbieri, J.T.
Catalytic properties of botulinum neurotoxin subtypes A3 and A4
Biochemistry
48
2522-2528
2009
Clostridium botulinum
brenda
Fu, Z.; Chen, C.; Barbieri, J.T.; Kim, J.J.; Baldwin, M.R.
Glycosylated SV2 and gangliosides as dual receptors for botulinum neurotoxin serotype F
Biochemistry
48
5631-5641
2009
Clostridium botulinum (Q57236)
brenda
Kukreja, R.V.; Sharma, S.K.; Singh, B.R.
Molecular basis of activation of endopeptidase activity of botulinum neurotoxin type E
Biochemistry
49
2510-2519
2010
Clostridium botulinum
brenda
Schmitt, J.; Karalewitz, A.; Benefield, D.A.; Mushrush, D.J.; Pruitt, R.N.; Spiller, B.W.; Barbieri, J.T.; Lacy, D.B.
Structural analysis of botulinum neurotoxin type G receptor binding
Biochemistry
49
5200-5205
2010
Clostridium botulinum (Q60393)
brenda
Moghaddam, M.M.; Mousavi, L.; Shokrgozar, M.A.; Amani, J.; Nazariyan, S.; Azari, S.
Cloning and expression of a region of vesicle associated membrane protein2 (VAMP2) gene and its use as a recombinant peptide substrate for assaying clostridial neurotoxins in contaminated biologicals
Biologicals
38
113-119
2010
Clostridium botulinum
brenda
Mansour, A.A.; Mousavi, S.L.; Rasooli, I.; Nazarian, S.; Amani, J.; Farhadi, N.
Cloning, high level expression and immunogenicity of 1163-1256 residues of C-terminal heavy chain of C. botulinum neurotoxin type E
Biologicals
38
260-264
2010
Clostridium botulinum
brenda
Salzameda, N.T.; Barbieri, J.T.; Janda, K.D.
Synthetic substrate for application in both high and low throughput assays for botulinum neurotoxin B protease inhibitors
Bioorg. Med. Chem. Lett.
19
5848-5850
2009
Clostridium botulinum
brenda
Warner, M.G.; Grate, J.W.; Tyler, A.; Ozanich, R.M.; Miller, K.D.; Lou, J.; Marks, J.D.; Bruckner-Lea, C.J.
Quantum dot immunoassays in renewable surface column and 96-well plate formats for the fluorescence detection of botulinum neurotoxin using high-affinity antibodies
Biosens. Bioelectron.
25
179-184
2009
Clostridium botulinum
brenda
Pannek, J.; Goecking, K.; Bersch, U.
Long-term effects of repeated intradetrusor botulinum neurotoxin A injections on detrusor function in patients with neurogenic bladder dysfunction
BJU Int.
104
1246-1250
2009
Clostridium botulinum
brenda
Hill, K.K.; Xie, G.; Foley, B.T.; Smith, T.J.; Munk, A.C.; Bruce, D.; Smith, L.A.; Brettin, T.S.; Detter, J.C.
Recombination and insertion events involving the botulinum neurotoxin complex genes in Clostridium botulinum types A, B, E and F and Clostridium butyricum type E strains
BMC Biol.
7
66
2009
Clostridium botulinum, Clostridium butyricum
brenda
Scotcher, M.C.; Johnson, E.A.; Stanker, L.H.
Characterization of the epitope region of F1-2 and F1-5, two monoclonal antibodies to botulinum neurotoxin type A
Hybridoma
28
315-325
2009
Clostridium botulinum, Clostridium botulinum ATCC 3502
brenda
Shone, C.; Agostini, H.; Clancy, J.; Gu, M.; Yang, H.H.; Chu, Y.; Johnson, V.; Taal, M.; McGlashan, J.; Brehm, J.; Tong, X.
Bivalent recombinant vaccine for botulinum neurotoxin types A and B based on a polypeptide comprising their effector and translocation domains that is protective against the predominant A and B subtypes
Infect. Immun.
77
2795-2801
2009
Clostridium botulinum (P10844), Clostridium botulinum (P10845)
brenda
Cheng, L.W.; Stanker, L.H.; Henderson, T.D.; Lou, J.; Marks, J.D.
Antibody protection against botulinum neurotoxin intoxication in mice
Infect. Immun.
77
4305-4313
2009
Clostridium botulinum
brenda
Fach, P.; Fenicia, L.; Knutsson, R.; Wielinga, P.R.; Anniballi, F.; Delibato, E.; Auricchio, B.; Woudstra, C.; Agren, J.; Segerman, B.; de Medici, D.; van Rotterdam, B.J.
An innovative molecular detection tool for tracking and tracing Clostridium botulinum types A, B, E, F and other botulinum neurotoxin producing Clostridia based on the GeneDisc cycler
Int. J. Food Microbiol.
145
S145-151
2011
Clostridium baratii, Clostridium botulinum, Clostridium butyricum
brenda
Silhar, P.; Capkova, K.; Salzameda, N.T.; Barbieri, J.T.; Hixon, M.S.; Janda, K.D.
Botulinum neurotoxin A protease: discovery of natural product exosite inhibitors
J. Am. Chem. Soc.
132
2868-2869
2010
Clostridium botulinum
brenda
Evans, E.R.; Skipper, P.J.; Shone, C.C.
An assay for botulinum toxin types A, B and F that requires both functional binding and catalytic activities within the neurotoxin
J. Appl. Microbiol.
107
1384-1391
2009
Clostridium botulinum
brenda
Thanongsaksrikul, J.; Srimanote, P.; Maneewatch, S.; Choowongkomon, K.; Tapchaisri, P.; Makino, S.; Kurazono, H.; Chaicumpa, W.
A V H H that neutralizes the zinc metalloproteinase activity of botulinum neurotoxin type A
J. Biol. Chem.
285
9657-9666
2010
Clostridium botulinum (P10845)
brenda
Nuss, J.E.; Ruthel, G.; Tressler, L.E.; Wanner, L.M.; Torres-Melendez, E.; Hale, M.L.; Bavari, S.
Development of cell-based assays to measure botulinum neurotoxin serotype A activity using cleavage-sensitive antibodies
J. Biomol. Screen.
15
42-51
2010
Clostridium botulinum
brenda
Shi, X.; Garcia, G.E.; Neill, R.J.; Gordon, R.K.
TCEP treatment reduces proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells
J. Cell. Biochem.
107
1021-1030
2009
Clostridium botulinum
brenda
Shi, X.; Curran, J.E.; Liao, Z.; Gordon, R.K.
The biological activity of ubiquitinated BoNT/B light chain in vitro and in human SHSY-5Y neuronal cells
J. Cell. Biochem.
108
660-667
2009
Clostridium botulinum
brenda
Li, B.; Pai, R.; Cardinale, S.C.; Butler, M.M.; Peet, N.P.; Moir, D.T.; Bavari, S.; Bowlin, T.L.
Synthesis and biological evaluation of botulinum neurotoxin A protease inhibitors
J. Med. Chem.
53
2264-2276
2010
Clostridium botulinum
brenda
Kumaran, D.; Eswaramoorthy, S.; Furey, W.; Navaza, J.; Sax, M.; Swaminathan, S.
Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation
J. Mol. Biol.
386
233-245
2009
Clostridium botulinum (Q00496), Clostridium botulinum
brenda
Dong, J.; Thompson, A.A.; Fan, Y.; Lou, J.; Conrad, F.; Ho, M.; Pires-Alves, M.; Wilson, B.A.; Stevens, R.C.; Marks, J.D.
A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic alpha-exosite binding region
J. Mol. Biol.
397
1106-1118
2010
Clostridium botulinum
brenda
Caleo, M.; Antonucci, F.; Restani, L.; Mazzocchio, R.
A reappraisal of the central effects of botulinum neurotoxin type A: by what mechanism?
J. Neurochem.
109
15-24
2009
Clostridium botulinum
brenda
Rummel, A.; Haefner, K.; Mahrhold, S.; Darashchonak, N.; Holt, M.; Jahn, R.; Beermann, S.; Karnath, T.; Bigalke, H.; Binz, T.
Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor
J. Neurochem.
110
1942-1954
2009
Clostridium botulinum
brenda
Coffield, J.A.; Yan, X.
Neuritogenic actions of botulinum neurotoxin A on cultured motor neurons
J. Pharmacol. Exp. Ther.
330
352-358
2009
Clostridium botulinum
brenda
Thyagarajan, B.; Krivitskaya, N.; Potian, J.G.; Hognason, K.; Garcia, C.C.; McArdle, J.J.
Capsaicin protects mouse neuromuscular junctions from the neuroparalytic effects of botulinum neurotoxin A
J. Pharmacol. Exp. Ther.
331
361-371
2009
Clostridium botulinum
brenda
Pellett, S.; Tepp, W.H.; Toth, S.I.; Johnson, E.A.
Comparison of the primary rat spinal cord cell (RSC) assay and the mouse bioassay for botulinum neurotoxin type A potency determination
J. Pharmacol. Toxicol. Methods
61
304-310
2010
Clostridium botulinum
brenda
Sun, S.; Ossandon, M.; Kostov, Y.; Rasooly, A.
Lab-on-a-chip for botulinum neurotoxin a (BoNT-A) activity analysis
Lab Chip
9
3275-3281
2009
Clostridium botulinum
brenda
Shi, J.; Li, T.; Hou, X.; Cai, K.; Bao, S.; Liu, H.; Gao, X.; Xiao, L.; Tu, W.; Wang, Q.; Yin, J.; Wang, H.
Recombinant luminal domain of human synaptotagmin II in combination with gangliosides inhibits the toxicity of botulinum neurotoxins in mice
Microbes Infect.
12
319-323
2010
Clostridium botulinum
brenda
Agarwal, R.; Schmidt, J.J.; Stafford, R.G.; Swaminathan, S.
Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F
Nat. Struct. Mol. Biol.
16
789-794
2009
Clostridium botulinum (P30996), Clostridium botulinum
brenda
Antonucci, F.; Cerri, C.; Vetencourt, J.F.; Caleo, M.
Acute neuroprotection by the synaptic blocker botulinum neurotoxin E in a rat model of focal cerebral ischaemia
Neuroscience
169
395-401
2010
Clostridium botulinum
brenda
Stowe, G.N.; Silhar, P.; Hixon, M.S.; Silvaggi, N.R.; Allen, K.N.; Moe, S.T.; Jacobson, A.R.; Barbieri, J.T.; Janda, K.D.
Chirality holds the key for potent inhibition of the botulinum neurotoxin serotype A protease
Org. Lett.
12
756-759
2010
Clostridium botulinum
brenda
Miller, D.; Richardson, D.; Eisa, M.; Bajwa, R.J.; Jabbari, B.
Botulinum neurotoxin-A for treatment of refractory neck pain: a randomized, double-blind study
Pain Med.
10
1012-1017
2009
Clostridium botulinum
brenda
Carmichael, N.M.; Dostrovsky, J.O.; Charlton, M.P.
Peptide-mediated transdermal delivery of botulinum neurotoxin type A reduces neurogenic inflammation in the skin
Pain
149
316-324
2010
Clostridium botulinum
brenda
Franciosa, G.; Maugliani, A.; Scalfaro, C.; Aureli, P.
Evidence that plasmid-borne botulinum neurotoxin type B genes are widespread among Clostridium botulinum serotype B strains
PLoS ONE
4
e4829
2009
Clostridium botulinum (A2I2U3), Clostridium botulinum (A2I2W1), Clostridium botulinum (Q08077), Clostridium botulinum (Q93G71), Clostridium botulinum
brenda
Scotcher, M.C.; McGarvey, J.A.; Johnson, E.A.; Stanker, L.H.
Epitope characterization and variable region sequence of f1-40, a high-affinity monoclonal antibody to botulinum neurotoxin type a (Hall strain)
PLoS ONE
4
e4924
2009
Clostridium botulinum
brenda
Kalb, S.R.; Lou, J.; Garcia-Rodriguez, C.; Geren, I.N.; Smith, T.J.; Moura, H.; Marks, J.D.; Smith, L.A.; Pirkle, J.L.; Barr, J.R.
Extraction and inhibition of enzymatic activity of botulinum neurotoxins/A1, /A2, and /A3 by a panel of monoclonal anti-BoNT/A antibodies
PLoS ONE
4
e5355
2009
Clostridium botulinum
brenda
Pang, Y.P.; Davis, J.; Wang, S.; Park, J.G.; Nambiar, M.P.; Schmidt, J.J.; Millard, C.B.
Small molecules showing significant protection of mice against botulinum neurotoxin serotype A
PLoS ONE
5
e10129
2010
Clostridium botulinum
brenda
Conway, J.O.; Sherwood, L.J.; Collazo, M.T.; Garza, J.A.; Hayhurst, A.
Llama single domain antibodies specific for the 7 botulinum neurotoxin serotypes as heptaplex immunoreagents
PLoS ONE
5
e8818
2010
Clostridium botulinum
brenda
Fischer, A.; Nakai, Y.; Eubanks, L.M.; Clancy, C.M.; Tepp, W.H.; Pellett, S.; Dickerson, T.J.; Johnson, E.A.; Janda, K.D.; Montal, M.
Bimodal modulation of the botulinum neurotoxin protein-conducting channel
Proc. Natl. Acad. Sci. USA
106
1330-1335
2009
Clostridium botulinum
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Chen, S.; Barbieri, J.T.
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Clostridium botulinum, Clostridium botulinum Okra
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Clostridium botulinum (A5HZZ9)
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Clostridium botulinum, Clostridium botulinum Okra
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Clostridium botulinum (P10845)
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Clostridium botulinum, Clostridium botulinum (D2KHS9)
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Clostridium botulinum
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Clostridium botulinum, Clostridium botulinum 1873
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Clostridium botulinum
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Clostridium botulinum, Clostridium botulinum IBCA10-7060
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Clostridium botulinum
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Clostridium botulinum
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Clostridium botulinum, Clostridium botulinum CDC41370
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Clostridium botulinum, Clostridium botulinum Chemnitz
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Clostridium botulinum
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Clostridium botulinum (P0DPK1)
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Clostridium botulinum
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144
34-41
2018
Clostridium botulinum
brenda
Hackett, G.; Moore, K.; Burgin, D.; Hornby, F.; Gray, B.; Elliott, M.; Mir, I.; Beard, M.
Purification and characterization of recombinant botulinum neurotoxin serotype FA, also known as serotype H
Toxins
10
E195
2018
Clostridium botulinum, Clostridium botulinum IBCA 10-7060
brenda
Sikorra, S.; Skiba, M.; Dorner, M.B.; Weisemann, J.; Weil, M.; Valdezate, S.; Davletov, B.; Rummel, A.; Dorner, B.G.; Binz, T.
Botulinum neurotoxin F subtypes cleaving the VAMP-2 Q58-K59 peptide bond exhibit unique catalytic properties and substrate specificities
Toxins
10
E311
2018
Clostridium botulinum (A0A1P8YWK9), Clostridium botulinum (A7GBG3), Clostridium botulinum (D2KHS4), Clostridium baratii (A0A1P8YWP1), Clostridium baratii CNM1212/11 (A0A1P8YWP1), Clostridium botulinum NCTC 10281 (A7GBG3), Clostridium botulinum H078-01 (A0A1P8YWK9), Clostridium botulinum H078-01 (D2KHS4)
brenda
Joussain, C.; Le Coz, O.; Pichugin, A.; Marconi, P.; Lim, F.; Sicurella, M.; Salonia, A.; Montorsi, F.; Wandosell, F.; Foster, K.; Giuliano, F.; Epstein, A.L.; Aranda Munoz, A.
Botulinum neurotoxin light chains expressed by defective herpes simplex virus type-1 vectors cleave SNARE proteins and inhibit CGRP release in rat sensory neurons
Toxins
11
E123
2019
Clostridium botulinum (P0DPI1), Clostridium botulinum (P19321), Clostridium botulinum (P30996), Clostridium botulinum (Q00496), Clostridium phage c-st (P18640), Clostridium botulinum ATCC 3502 (P0DPI1)
brenda