3.4.24.69: bontoxilysin
This is an abbreviated version!
For detailed information about bontoxilysin, go to the full flat file.
Word Map on EC 3.4.24.69
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3.4.24.69
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pain
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nerve
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spastic
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dystonias
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bonts
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facial
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palsy
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bladder
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overact
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limb
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botulism
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paralysis
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neuromuscular
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spasm
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placebo
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double-blinded
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headache
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detrusor
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migraine
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incontinence
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cosmetic
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relief
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rehabilitation
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placebo-controlled
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neurogenic
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sphincter
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satisfaction
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aesthetic
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dysphagia
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snap-25
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ptosis
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involuntary
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anticholinergic
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eyelid
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strabismus
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intravesical
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wrinkle
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urodynamic
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electromyography
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flexor
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masseter
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voice
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rectus
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fissure
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filler
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adductor
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antitoxin
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physiotherapy
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pneumatic
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baclofen
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molecular biology
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medicine
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drug development
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analysis
- 3.4.24.69
- pain
- nerve
- spastic
- dystonias
-
bonts
-
facial
- palsy
- bladder
-
overact
- limb
- botulism
- paralysis
- neuromuscular
- spasm
-
placebo
-
double-blinded
- headache
- detrusor
- migraine
- incontinence
-
cosmetic
-
relief
-
rehabilitation
-
placebo-controlled
-
neurogenic
-
sphincter
-
satisfaction
-
aesthetic
- dysphagia
- snap-25
- ptosis
-
involuntary
-
anticholinergic
- eyelid
- strabismus
-
intravesical
-
wrinkle
-
urodynamic
-
electromyography
- flexor
- masseter
- voice
-
rectus
- fissure
-
filler
- adductor
- antitoxin
-
physiotherapy
-
pneumatic
- baclofen
- molecular biology
- medicine
- drug development
- analysis
Reaction
Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevin (also known as neuronal vesicle-associated membrane protein, VAMP), synaptosome-associated protein of 25 kDa (SNAP25) or syntaxin. No detected action on small molecule substrates =
Synonyms
abobotulinumtoxinA, antigen E, Balc424, BoNT, BoNT A, BoNT B, BoNT E, BoNT F, BoNT F/A, BoNT LC, BoNT LC/A, BoNT serotype A, BoNT serotype E, BoNT serotype F, BoNT-A, BoNT-C, BoNT-D, BoNT-E, BoNT-F, BoNT/A, BoNT/A LC, BoNT/A Lc endopeptidase, BoNT/A-LC, BoNT/A1, BoNT/A2, BoNT/A3, BoNT/A4, BoNT/A5, BoNT/A6, BoNT/A8, BoNT/B, BoNT/B light chain protease, BoNT/B-LC, BoNT/B1, BoNT/B6, BoNT/C, BoNT/C1, BoNT/C1-LC, BoNT/C3, BoNT/CD, BoNT/D, BoNT/E, BoNT/F, BoNT/F proteolytic F toxin, BoNT/F-LC, BoNT/F1, BoNT/F5, BoNT/F6, BoNT/F7, BoNT/F9, BoNT/FA, BoNT/G, BoNT/HA, BoNT/T, BoNT/X, BoNTA, BoNTA endopeptidase, BoNTB, BoNTC, BoNTE, BoNTF, Bontoxilysin C1, botox A, botulinum A neurotoxin light chain, Botulinum neurotoxin, botulinum neurotoxin a, botulinum neurotoxin A light chain, botulinum neurotoxin A protease, botulinum neurotoxin A subtype 1, botulinum neurotoxin A subtype 2, botulinum neurotoxin A subtype 6, botulinum neurotoxin A3, botulinum neurotoxin A4, botulinum neurotoxin A8 subtype, botulinum neurotoxin B, botulinum neurotoxin B protease, botulinum neurotoxin C, botulinum neurotoxin D light chain, botulinum neurotoxin E, botulinum neurotoxin endopeptidase, botulinum neurotoxin F, botulinum neurotoxin serotype A, botulinum neurotoxin serotype A endopeptidase, botulinum neurotoxin serotype A light chain, botulinum neurotoxin serotype A protease, botulinum neurotoxin serotype B, botulinum neurotoxin serotype BA, botulinum neurotoxin serotype C1, botulinum neurotoxin serotype C1 light chain protease, botulinum neurotoxin serotype D, botulinum neurotoxin serotype E, botulinum neurotoxin serotype F, botulinum neurotoxin serotype FA, botulinum neurotoxin serotype G, botulinum neurotoxin serotype H, botulinum neurotoxin subtype A, botulinum neurotoxin subtype A3, botulinum neurotoxin subtype A4, botulinum neurotoxin subtype B6, botulinum neurotoxin subtype F5, botulinum neurotoxin type A, botulinum neurotoxin type A light chain, botulinum neurotoxin type B, botulinum neurotoxin type C, botulinum neurotoxin type D, botulinum neurotoxin type E, botulinum neurotoxin type F, botulinum neurotoxin type F light chain, botulinum neurotoxin type G, botulinum neurotoxin type HA, botulinum neurotoxin X, Botulinum neurotoxin-A, botulinum toxin, botulinum toxin C3, botulinum toxin serotype E, botulinum toxin serotype F, botulinum toxin type A, botulinum toxin type B, botulinum toxin type F, Botulinumtoxin A, BoTxA, C2 toxin, CDC69016, Clostridium botulinum A2 neurotoxin, Clostridium botulinum C2 toxin, Clostridium botulinum neurotoxin, Clostridium botulinum neurotoxin A1, Clostridium botulinum neurotoxin F, Clostridium botulinum neurotoxin serotype A, Clostridium botulinum neurotoxin serotype A light chain, Clostridium botulinum neurotoxin type E, Clostridium botulinum serotype D neurotoxin, CNT endopeptidase, D-4947 L-TC, daxibotulinumtoxinA, HCB, HCE, incobotulinumtoxinA, LC/A, LC/D, LC/F5, LC/HA, LC/X, LCA, LcB, lcc1, LCD, LCE, LCF, LHn/D, More, mosaic toxin, neurotoxin A, NT, onabotulinumtoxinA, serotype D botulinum neurotoxin, subtype A4 neurotoxin, TeNT, Tetanus neurotoxin, type A BoNT, type A botulinum neurotoxin, type A botulinum neurotoxin light chain, type A botulinum neurotoxin protease, type F toxin
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Natural Substrates Products on EC 3.4.24.69 - bontoxilysin
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-SNKTIDEANQRATKML-NH2 + H2O
Ac-SNKTIDEANQ + RATKML-NH2
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synaptosomal protein
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?
cytosolic SNARE + H2O
?
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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
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?
membrane-anchored SNARE + H2O
?
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host membrane-anchored SNARE, proteolytically cleaved by BoNT/C
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-
?
SNARE-protein + H2O
?
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soluble NSF-attachment protein receptor
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?
VAMP 2 + H2O
?
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i.e. synaptobrevin-2 or vesicle-associated membrane protein 2
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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?
Neuroexocytosis multi-subunit complex + H2O
?
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involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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?
Neuroexocytosis multi-subunit complex + H2O
?
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involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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?
Neuroexocytosis multi-subunit complex + H2O
?
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involved in limited hydrolysis of proteins of the neuroexocytosis apparatus, blocks release of neurotransmitter acetylcholine at neuromuscular junction
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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-
?
Neuroexocytosis multi-subunit complex + H2O
?
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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
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-
?
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
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-
?
SNAP-25 + H2O
?
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i.e. synaptosomal associated protein of 25 kDa
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-
?
SNAP-25 + H2O
?
serotypes BoNT/A and BoNT/E cleave SNAP-25 at distinct sites, BoNT/E blocks neurotransmission faster and more potently
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-
?
SNAP-25 + H2O
?
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the potent botulinum neurotoxin inhibits neurotransmitter release at cholinergic nerve terminals, causing a descending flaccid paralysis characteristic of the disease botulism
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?
SNAP-25 + H2O
?
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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
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?
SNAP-25 + H2O
?
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i.e. 25-kDa synaptosomal-associated protein, substrate of BoNT/A
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?
SNAP-25 + H2O
?
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i.e. 25-kDa synaptosome-associated protein
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?
SNAP-25 + H2O
?
P10845
i.e. 25-kDa synaptosome-associated protein
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?
SNAP-25 + H2O
?
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i.e. 25-kDa synaptosome-associated protein, a substrate of BoNT/A light chain
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-
?
SNAP-25 + H2O
?
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i.e. 25-kDa synaptosome-associated protein, BoNT/A
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?
SNAP-25 + H2O
?
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i.e. 25-kDa synaptosome-associated protein, is involved in acetylcholine release at the neuromuscular junction
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-
?
SNAP-25 + H2O
?
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i.e. 25-kDa synaptosome-associated protein, substrate of BoNT/A, /E, and /C
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-
?
SNAP-25 + H2O
?
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i.e. synaptosome-associated protein of 25 kDa, a plasma membrane-associated protein, proteolytically cleaved by BoNT types A, C, and E
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-
?
SNAP25 + H2O
?
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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
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?
SNAP25 + H2O
?
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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
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?
SNAP25 + H2O
?
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zinc-endopeptidase activity of the N-terminal light chain of BoNT/A on synaptosome-associated protein-25 kDa of the SNARE complex
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-
?
SNAP25 + H2O
?
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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
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-
?
synaptobrevin + H2O
?
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synaptic vesicle-associated membrane protein, neurotoxin responsible for human and animal botulism
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?
synaptobrevin + H2O
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a vesicle-associated membrane protein, also known as VAMP, the most abundant SV entity, proteolytically cleaved by BoNT types B, D, F, and G
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?
Synaptosome-associated protein + H2O
?
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i.e. SNAP 25, protein of presynaptic membrane
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?
Synaptosome-associated protein + H2O
?
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i.e. SNAP 25, protein of presynaptic membrane
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-
?
Synaptosome-associated protein + H2O
?
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i.e. SNAP 25, protein of presynaptic membrane
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-
?
Synaptosome-associated protein + H2O
?
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i.e. SNAP 25, protein of presynaptic membrane
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-
?
synaptosome-associated protein SNAP-25 + H2O
?
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?
synaptosome-associated protein SNAP-25 + H2O
?
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?
synaptosome-associated protein SNAP-25 + H2O
?
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botulinum neurotoxin type D enables cytosolic delivery of enzymatically active cargo proteins to neurones via unfolded translocation intermediates
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?
synaptosome-associated protein SNAP-25 + H2O
?
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?
VAMP + H2O
?
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i.e. vesicle associated membrane protein or synaptobrevin, BoNT/B, and BoNT/F
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-
?
VAMP + H2O
?
i.e. vesicle-associated membrane protein/synaptobrevin
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-
?
VAMP + H2O
?
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i.e. vesicle-associated membrane protein/synaptobrevin, substrate of BoNT/B, /D, /F, /G, and /C
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-
?
VAMP2 + H2O
?
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i.e. intracellular vesicle associated membrane protein 2
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-
?
VAMP2 + H2O
?
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i.e. synaptobrevin-2 or vesicle-associated membrane protein 2
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-
?
vesicle-associated membrane protein-1 + H2O
?
cleavage at Arg66-Ala67
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-
?
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
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-
?
vesicle-associated membrane protein-2 + H2O
?
cleavage at Gln58-Lys59
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-
?
vesicle-associated membrane protein-2 + H2O
?
Clostridium baratii CNM1212/11
cleavage at Gln58-Lys59
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-
?
vesicle-associated membrane protein-2 + H2O
?
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?
vesicle-associated membrane protein-2 + H2O
?
cleavage at Arg66-Ala67
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?
vesicle-associated membrane protein-2 + H2O
?
cleavage at Gln58-Lys59
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?
vesicle-associated membrane protein-2 + H2O
?
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cleavage at Leu54-Glu55
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-
?
vesicle-associated membrane protein-2 + H2O
?
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cleavage between L54 and E55
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-
?
vesicle-associated membrane protein-2 + H2O
?
Clostridium botulinum BCA10-7060
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cleavage between L54 and E55
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?
vesicle-associated membrane protein-2 + H2O
?
Clostridium botulinum H078-01
cleavage at Gln58-Lys59
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?
vesicle-associated membrane protein-2 + H2O
?
cleavage at Gln58-Lys59
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-
?
vesicle-associated membrane protein-3 + H2O
?
cleavage at Arg66-Ala67
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-
?
vesicle-associated membrane protein-4 + H2O
?
cleavage at Lys87-Ser88
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-
?
vesicle-associated membrane protein-5 + H2O
?
cleavage at Arg40-Ser41
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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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able to cleave selectively an essential component of neurotransmitter exocytosis, causing the syndrome of botulism characterized by flaccid paralysis
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?
additional information
?
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only mammalian proteins, SNAP-25 from Drosophila sp. and Torpedo sp. are no substrates
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?
additional information
?
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undergoes autocatalytic proteolytic processing and fragmentation
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?
additional information
?
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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
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?
additional information
?
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botulinum neurotoxins are a group of proteins produced by different strains of Clostridium botulinum, that are responsible for botulism disease
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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the enzyme causes neuroparalysis by blocking neurotransmitter release at the neuromuscular junctions
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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toxicity in mice of full-length, single-nicked, and double-nicked enzyme forms, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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BoNT serotypes bind to structure of ganglioside GT1b receptors, structure and binding specificities, modelling, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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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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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Clostridium botulinum IBCA10-7060
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no activity with synaptosome-associated protein SNAP-25 and syntaxin
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additional information
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Clostridium botulinum Osaka05
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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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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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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
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