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Information on EC 3.4.24.87 - ADAMTS13 endopeptidase and Organism(s) Homo sapiens and UniProt Accession Q76LX8

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.87 ADAMTS13 endopeptidase
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This record set is specific for:
Homo sapiens
UNIPROT: Q76LX8 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
The enzyme cleaves the von Willebrand factor at bond Tyr842-/-Met843 within the A2 domain
Synonyms
adamts13, adamts-13, von willebrand factor-cleaving protease, vwf-cp, vwf-cleaving protease, adamts 13, von willebrand factor cleaving protease, vwf cleaving protease, metalloprotease adamts-13, vwf protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
a disintegrin and metalloprotease with thrombospondin motifs 13
-
a disintegrin and metalloproteinase with a thrombospondin motif repeats 13
-
a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13
-
a thrombospondin type 1 motif, member 13
-
ADAMTS13
M12.241
Merops-ID
von Willebrand cleavage protease
-
von Willebrand cleavaging protease
-
von Willebrand factor-cleaving protease
-
von Willebrand factor-cleaving proteinase
-
a disintegrin and metalloprotease with thrombospondin motifs 13
-
-
a disintegrin and metalloprotease with thrombospondin type 1 repeats 13
-
-
a disintegrin and metalloproteinase with a thrombonspondin type 1 motif member 13
-
-
a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13
-
-
a disintegrin-like and metalloprotease with thrombospondin type-1 motifs 13
-
-
a disintegrin-like and metalloproteinase domain with thrombospondin type I motifs 13
-
-
a disintegrin-like and metalloproteinase with thrombospondin type-1 motifs 13
-
-
a disintegrin-like domain and metalloprotease with thrombospondin type I motif
-
-
ADAMTS 13
-
-
ADAMTS VWF cleaving metalloprotease
-
-
ADAMTS-13
ADAMTS13
ADAMTS13 metalloprotease
-
-
metalloprotease ADAMTS-13
-
-
plasma metalloprotease ADAMTS13
-
-
plasma von Willebrand factor cleaving activity
-
-
Upshaw factor
-
-
van Willebrand factor processing activity
-
-
von Willebrand cleavage protease
-
-
von Willebrand factor cleaving protease
-
-
von Willebrand factor specific cleaving protease
-
-
von Willebrand factor-cleaving metalloprotease
-
-
von Willebrand factor-cleaving protease
-
-
von-Willebrand factor cleaving protease
-
-
von-Willebrand factor degrading protease
-
-
von-Willebrand-factor-cleaving protease
-
-
VWF cleaving metalloprotease
-
-
VWF cleaving protease
-
-
vWF protease
-
-
VWF-cleaving metalloprotease
-
-
vWF-cleaving protease
-
-
vWF-degrading protease
-
-
xWF-CP
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme cleaves the von Willebrand factor at bond Tyr842-/-Met843 within the A2 domain
show the reaction diagram
active site sequence HEXXHXXGXXHD
The enzyme cleaves the von Willebrand factor at bond Tyr842-/-Met843 within the A2 domain
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
334869-10-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
FRETS-rVWF71 + H2O
?
show the reaction diagram
substrate based on von Willebrand factor residues Gln1599-Arg1668, with an N-terminal Gly and with mutations N1610C and K1617R. The N-terminus is modified with IRDye QC-1 Nhydroxysuccinimide ester, and Cys1610 is modified with DyLight 633 maleimide
-
-
?
FRETS-von Willebrand factor 73 + H2O
?
show the reaction diagram
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
recombinant human VWF73 peptide + H2O
?
show the reaction diagram
-
-
-
?
von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
show the reaction diagram
-
ADAMTS13 cleaves von Willebrand factor at the Y1605/M1606 peptide bond in the A2 domain. Mutant substrates L1603Q, L1603R, Y1605D, L1603R/Y1605N, Y1605N/M1606T, Y1605R/M1606T are resistant to cleavage. Mutant substrates R1597W, M1606T and I1616N are less efficiently cleaved than wild-type
-
?
von Willebrand factor + H2O
?
show the reaction diagram
VWF115 + H2O
?
show the reaction diagram
von Willebrand factor A2 domain fragment, residues 1554-1668
-
-
?
VWFA2 peptide + H2O
?
show the reaction diagram
substrate based on a 78-amino acid sequence corresponding to the sequence Leu1591-Arg1668 of the von Willebrand factor A2 domain
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
DREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRA + H2O
?
show the reaction diagram
-
i.e. VWF74 peptide, a pseudo-wild-type peptide von Willebrand factor 74, VWF74, encompassing the von Willebrand factor, VWF, A2 domain sequence 1596-1669
-
-
?
fluorescence resonance energy transfer substrate-von Willebrand factor 73 + H2O
?
show the reaction diagram
-
-
-
-
?
FRET-VWF115 peptide + H2O
?
show the reaction diagram
-
von Willebrand factor-derived peptide substrate comprising residues 1554-1668
-
-
?
FRETS-von Willebrand factor 73 + H2O
?
show the reaction diagram
-
-
-
-
?
FRETS-vWF73 + H2O
?
show the reaction diagram
-
a fluorogenic von Willebrand factor-derived peptide substrate
-
-
?
FRETS-VWF73 peptide + H2O
?
show the reaction diagram
-
fluorogenic von Willebrand factor-derived peptide substrate
-
-
?
FRETSVWF73 + H2O
?
show the reaction diagram
-
a von Willebrand factor-derived fluorescein-labeled peptide substrate
-
-
?
FRETSVWF73 peptide + H2O
?
show the reaction diagram
-
a von Willebrand factor-derived fluorescein-labeled peptide substrate
-
-
?
GST-von Willebrand factor 73 + H2O
?
show the reaction diagram
-
contains residues Asp1596-Arg1668 from von Willebrand factor domain A2
-
-
?
GST-VWF73 + H2O
?
show the reaction diagram
-
labeled von Willebrand factor-derived peptide substrate
-
-
?
HRPH-A2-B
?
show the reaction diagram
-
HRPH-A2-B is a derivative of von Willebrand factor 73, consisting of a HRP conjugate of a biotinylated von Willebrand factor 78 sequence
cleavage of Tyr842-Met843 within the A2 domain, i.e. Tyr1605-Met1606 in von Willebrand factor UniProt Id P04275
-
?
large von Willebrand factor multimer + H2O
?
show the reaction diagram
-
-
-
-
?
proteins + H2O
peptides
show the reaction diagram
ultra-large von Willebrand factor + H2O
?
show the reaction diagram
-
-
-
-
?
ultra-large von Willebrand factor multimer + H2O
?
show the reaction diagram
-
-
-
-
?
von Willebrand factor + H2O
2 peptides
show the reaction diagram
von Willebrand factor + H2O
2 peptides of 140 kD and 65 kD
show the reaction diagram
-
cleavage of peptide bond Tyr842-Met843
-
?
von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
show the reaction diagram
von Willebrand factor + H2O
2 peptides of 176 kD and 140 kD
show the reaction diagram
von Willebrand factor + H2O
?
show the reaction diagram
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
show the reaction diagram
von Willebrand factor + H2O
von Willebrand factor fragments
show the reaction diagram
von Willebrand factor 115 (1554-1668) + H2O
?
show the reaction diagram
-
A2 domain fragment
-
-
?
von Willebrand factor 115 + H2O
10000 Da fragment of von Willebrand factor 115 + 7000 Da fragment of von Willebrand factor 115
show the reaction diagram
-
von Willebrand factor is cleaved at the Tyr1605-Met1606 bond in the von Willebrand factor A2 domain
-
-
?
von Willebrand factor 115-A3 (1554-1874) + H2O
?
show the reaction diagram
-
A2 domain fragment
-
-
?
von Willebrand factor 73 + H2O
7722 Da peptide + ?
show the reaction diagram
-
-
-
-
?
von Willebrand factor 73 + H2O
?
show the reaction diagram
-
minimal substrate cleavable by ADAMTS-13
-
-
?
von Willebrand factor 76 (1593-1668) + H2O
?
show the reaction diagram
-
A2 domain fragment
-
-
?
VWF115 + H2O
10 kDa VWF115 fragment + 7 kDa VWF115 fragment
show the reaction diagram
-
VWFA2 domain fragment, spanning von Willebrand factor residues 1554-1668, generation of 2 cleavage products of 10 kDa and 7 kDa
-
-
?
VWF115 + H2O
?
show the reaction diagram
-
a von Willebrand factor-derived peptide substrate, comprising amino acid residues 1554-1668 of von Willebrand factor
-
-
?
VWF115 D1614A mutant + H2O
10 kDa VWF115 fragment + 7 kDa VWF115 fragment
show the reaction diagram
-
Asp1614 VWFA2 domain fragment, spanning von Willebrand factor residues 1554-1668, generation of 2 cleavage products of 10 kDa and 7 kDa
-
-
?
VWF73 peptide + H2O
?
show the reaction diagram
-
von Willebrand factor-derived peptide substrate
-
-
?
VWF73 region of von Willebrand factor + H2O
?
show the reaction diagram
-
with this minimal substrate urea is not required for cleavage, minimal substrate for ADAMTS-13
-
?
VWFA2 peptide + H2O
VWFA2 peptide fragments
show the reaction diagram
-
A2 domain fragment of von Willebrand factor, cleavage of oxidized or nonoxidized VWFA2 peptide by ADAMTS13, cleavage of the Tyr1605-Met(O)1606 peptide bond by ADAMTS13, overview
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
proteins + H2O
peptides
show the reaction diagram
von Willebrand factor + H2O
?
show the reaction diagram
proteins + H2O
peptides
show the reaction diagram
von Willebrand factor + H2O
2 peptides
show the reaction diagram
-
rapid physiological process that occurs on endothelial surfaces, reduced activity results in thrombotic thrombocytopenic pupura
-
?
von Willebrand factor + H2O
2 peptides of 140 kD and 65 kD
show the reaction diagram
-
cleavage of peptide bond Tyr842-Met843
-
?
von Willebrand factor + H2O
2 peptides of 140 kDa and 176 kDa
show the reaction diagram
von Willebrand factor + H2O
2 peptides of 176 kD and 140 kD
show the reaction diagram
-
rapid physiological process that occurs on endothelial surfaces, activity is reduced by 87-100% in patients with thrombotic thrombocytopenic pupura
-
?
von Willebrand factor + H2O
?
show the reaction diagram
von Willebrand factor + H2O
von Willebrand factor 140-kD fragment + von Willebrand factor 176-kD fragment
show the reaction diagram
von Willebrand factor + H2O
von Willebrand factor fragments
show the reaction diagram
von Willebrand factor 115 + H2O
10000 Da fragment of von Willebrand factor 115 + 7000 Da fragment of von Willebrand factor 115
show the reaction diagram
-
von Willebrand factor is cleaved at the Tyr1605-Met1606 bond in the von Willebrand factor A2 domain
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
activates, metalloprotease
Ca2+
metalloprotease, conserved binding site using Glu83, ASp173, Cys281, Asp284
Zn2+
metalloprotease, conserved binding site
Cu2+
-
activates
guanidine
-
activates
Mn2+
-
activates
Ni2+
-
activates
Sr2+
-
activating
Urea
-
activates
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
enzyme catalytic activity in blood plasma is tuned by varying buffer calcium, with lower divalent ion concentrations enhancing cleavage
H2O2
treatment with 25 nM myeloperoxidase plus 50 microM H2O2 reduces ADAMTS13 activity by >85%. Residues Met249, Met331, and Met496 in important functional domains of ADAMTS13 are oxidized to methionine sulfoxide in an HOCl concentration-dependent manner
1,10-phenanthroline
-
activity can be restored by Ca2+
citrate
-
weak
Cl-
-
Chloride ions inhibit von Willebrand factor hydrolysis by ADAMTS-13 of the A1-A2-A3 and A1-A2 domains in the presence of either urea or high shear stress, whereas this effect is either absent or negligible when using A2 and A2-A3 domains
CoCl2
-
an increasing concentration of CoCl2 inhibits ADAMTS13 activity
heparin
-
inhibits ADAMTS13 activity through inhibition of enzyme binding to endothelial cell surfaces, overview
HOCl
-
HOCl can oxidize methionine to methionine sulfoxide and tyrosine to chlorotyrosine, oxidation of VWF A2 peptide, at Met1606 and Tyr1605, markedly impairs ADAMTS13 cleavage. Oxidative modification by myeloperoxidase/H2O2 is similar to that produced by HOCl
Mn2+
-
ADAMTS13 activity is decreased in the presence of 0.9 mM Ni2+
MnSO4
-
an increasing concentration of MnSO4 inhibits ADAMTS13 activity
N-ethylmaleimide
-
slow and weak inhibition
Ni2+
-
ADAMTS13 activity is markedly decreased in the presence of 0.9 mM Ni2+
NiSO4
-
an increasing concentration of NiSO4 inhibits ADAMTS13 activity
peroxynitrite
-
formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13 a prothrombotic mechanism in diseases associated with oxidative stress, overview. Oxidation by peroxynitrite of purified VWF multimers inhibits ADAMTS-13 hydrolysis, but does not alter their electrophoretic pattern nor their ability to induce platelet agglutination by ristocetin. In vitro treatment of ADAMTS-13 with peroxynitrite over a concentration ranging from 0.050 to 0.250 mM causes a complete inhibition of the protease activity of the enzyme
Pro-1645-Lys-1668 fragment of von Willebrand factor 73
-
-
-
Trypsin
-
inhibits ADAMTS13 activity through inhibition of enzyme binding to endothelial cell surfaces, overview
-
VWFA2 domain
-
a C-terminal 32 kDa fragment of VWF, soluble VWFA2 domain effectively inhibits the binding of ADAMTS13 to immobilized VWFA2, and completely inhibits the interaction between ADAMTS13 and immobilized 64 kDa VWFA1A2A3 fragment
-
W688X6-1
-
the monoclonal antibody W688X6-1 shows dose-dependent inhibitory activity toward ADAMTS13-mediated hydrolysis
-
WH2-22-1A
-
the monoclonal antibody WH2-22-1A shows dose-dependent inhibitory activity toward ADAMTS13-mediated hydrolysis
-
Z-Phe-Phe-CHN2
-
best peptidyl diazomethyl ketone inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
plasmin
truncation of the enzyme by plasmin enhances its activity in blood plasma
-
von Willebrand factor
binding to substrate von Willebrand factor D4 allosterically activates ADAMTS13, increasing its catalytic activity. Binding also positions ADAMTS13 on the substrate where it can act rapidly when shear stress exposes the scissile bond in the adjacent A2 domain
-
Ristocetin
-
activates
Rituximab
-
a monoclonal anti-CD 20 antibody, Rituximab leads to a prompt reduction in IgG antibody levels, followed by an increase in ADAMTS 13 activity increases. However, in patients receiving Rituximab electively, normalisation of ADAMTS 13 enzyme activity may be delayed for up to 3 months
-
von Willebrand factor
-
the enzyme is conformationally activated by von Willebrand factor which engages the TSP8-CUB2 domains, inducing the conformational change that disrupts the CUB1-spacer domain interaction and thereby activates the enzyme
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00086 - 0.00154
VWF115
-
0.00662
DREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRA
-
pH 7.5, 25°C, recombinant enzyme
0.00129 - 0.00432
FRET-VWF115 peptide
-
0.0032
FRETS-von Willebrand factor 73
-
apparent value, pH 7.4
-
0.0058
FRETSVWF73 peptide
-
pH 7.5, 37°C, recombinant ADAMTS13
-
0.00025
HRPH-A2-B
-
-
-
0.00065 - 0.00161
von Willebrand factor 115
-
0.09 - 0.59
VWF115
-
0.37 - 0.47
VWF115 D1614A mutant
-
0.0017 - 0.022
VWF73 peptide
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.62 - 0.71
VWF115
-
0.72
DREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRA
-
pH 7.5, 25°C, recombinant enzyme
0.31 - 1.31
FRET-VWF115 peptide
-
4.43
FRETSVWF73 peptide
-
pH 7.5, 37°C, recombinant ADAMTS13
-
0.67
HRPH-A2-B
-
-
-
0.14 - 0.52
von Willebrand factor 115
-
0.0019 - 0.0062
VWF115
-
0.008 - 0.00875
VWF115 D1614A mutant
-
0.76 - 2.05
VWF73 peptide
-
additional information
additional information
-
kcat: 0.83 per min for FRETS-VWF73, a fluorescent synthetic peptide, corresponding to residues Asp1596-Arg1668 of von Willebrand factor domain A2 and containing the Tyr1605-Met1606 bond cleaved by ADAMTS13
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
410 - 830
VWF115
-
71.76 - 1016
FRET-VWF115 peptide
-
763.8
FRETSVWF73 peptide
-
pH 7.5, 37°C, recombinant ADAMTS13
-
821
von Willebrand factor 115
-
wild type enzyme, in 20 mM Tris-HCl (pH 7.8), 150 mM NaCl, 5 mM CaCl2, at 37°C
-
15 - 324
VWF115
-
50 - 57
VWF115 D1614A mutant
-
74 - 733
VWF73 peptide
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
Pro-1645-Lys-1668 fragment of von Willebrand factor 73
-
-
-
0.000028
VWFA2 domain
-
pH 7.8, 37°C
-
additional information
additional information
-
C-terminal fragments competitive inhibition binding, kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000072
VWFA2 domain
Homo sapiens
-
pH 7.8, 37°C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
6
-
peptide substrates
7.5
-
assay at
7.5 - 8
-
multimeric substrate
8 - 9
-
-
8.15
-
assay at
9 - 10
-
in presence of Ca2+
additional information
-
no activity at neutral pH at low salt concentration
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
22
-
room temperature, assay at
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1 - 5.5
-
purified blood plasma ADAMTS13, isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
in cerebral corpora amylacea, that occur in aging brains and in patients with neurodegenerative conditions
Manually annotated by BRENDA team
synthesizes and secreted ADAMTS13
Manually annotated by BRENDA team
in astrocytes of aging brains and patients with neurodegenerative conditions. Corporae amylaceae include glycosylated material, ubiquitin, and an assortment of proteins derived from neuronal cytoplasm. Many of these proteins are not specifically localized to neurons or astrocytes, some components of corpora amylacea, such as complement proteins, are most abundantly expressed outside the central nervous system. Corporae amylaceae can result from a conglomeration of interacting proteins from degenerating neurons and from extravasated blood elements released after transient breakdown of the blood-brain barrier
Manually annotated by BRENDA team
enzyme expression
Manually annotated by BRENDA team
enzyme expression
Manually annotated by BRENDA team
enzyme expression
Manually annotated by BRENDA team
thrombospondin1 and ADAMTS13 form complexes together in cells and in direct protein binding assays
Manually annotated by BRENDA team
enzyme expression
Manually annotated by BRENDA team
enzyme expression
Manually annotated by BRENDA team
-
a renal carcinoma cell line
Manually annotated by BRENDA team
-
primary renal cortical cell cultures, real-time PCR and immunohistochemic analysis, overview
Manually annotated by BRENDA team
-
ADAMTS13 and von Willebrand factor contents, overview
Manually annotated by BRENDA team
-
ADAMTS13 and von Willebrand factor contents, overview
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
secretes the enzyme
Manually annotated by BRENDA team
-
in both proximal and distal in healthy persons and in patients with renal disorders, e.g. tubulopathy
Manually annotated by BRENDA team
-
at the surface of endothelial cells
Manually annotated by BRENDA team
-
only in urine from patients with renal disorder tubulopathy
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
homogeneous distribution of wild-type ADAMTS13 in cis-Golgi and endoplasmic reticulum compartments. Reduction of ADAMTS13(Val88Met) in both compartments. ADAMTS13(Gly1239Val) fails to reach the cis-Golgi compartment and remains in the endoplasmic reticulum
Manually annotated by BRENDA team
-
homogeneous distribution of wild-type ADAMTS13 in cis-Golgi and endoplasmic reticulum compartments. Reduction of ADAMTS13(Val88Met) in both compartments. ADAMTS13(Gly1239Val) fails to reach the cis-Golgi compartment and remains in the endoplasmic reticulum
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
malfunction
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATS13_HUMAN
1427
1
153604
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
x * 45000, recombinant His-tagged ADAMTS13 ancillary domains, ADAMTS13-DTCS, SDS-PAGE
150000
150000 - 190000
-
gel filtration
170000
180000
-
x * 180000, SDS-PAGE
190000
300000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
made as a zymogen, requires proteolytic activation, possibly intracellularly by furin, cleavage of residues 1-74
glycoprotein
proteolytic modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in electron microscopy, wild-type ADAMTS13 adopts a closed conformation, gain-of-function mutant R568K/F592Y/R660K/Y661F/Y665F shows a more open conformation
recombinant His-tagged ADAMTS13 ancillary domains, residues 287-685, sitting-drop vapour-diffusion method, mixing of 100 nl protein solution, containing about 20 mg/ml protein, with an equal amount of reservoir solution, containing 26% w/v PEG 1500, 100 mM MES, pH 6.0, equilibration against 0.1 ml of reservoir solution, at 20°C, for 24 h, crystals are soaked in a solution containing 20% glycerol, 26% PEG 1500, 100 mM MES, pH 6.0, for cryoprotection, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution, labeling with heavy-atom derivatives
purified recombinant detagged ADAMTS13-DTCS, residues 287-685, an non-catalytic von Willebrand factor-exosite-containing ADAMTS13 fragment, sitting drop vapor diffusion method, mixing of 500 nl of protein solution and 500 nl reservoir solution containing 26% w/v PEG1500, 100 mM MES, pH 6.0, supplemented with 200 nl of 40% w/w pentaerythritol ethoxylate, equilibration for several days at 20°C. Os-derivative crystals by soaking native crystals in reservoir solution supplemented with 1 mM OsCl3 and 20% glycerol for several hours, X-ray diffraction structure determination and analysis at 2.6 A and 2.8 A resolution resulting in two crystal structures
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D187H
mutation identified in a patient with pregnancy-onset thrombotic thrombocytopenic purpura. Mutation is located in the high affinity Ca2+-binding site in the metalloprotease domain of ADAMTS13. The homozygous mutation down-regulates ADAMTS13 activity in vitro. Impaired proteolytic activity is linked to unstable Ca2+ binding. In addition, the D187H mutation affects protein secretion in vitro
delQ1624-R1641
mutation minimally affects the rate of cleavage
N146Q
decreased secretion and von Willebrand factor cleaving activity
N552Q
decreased secretion
N828Q
decreased secretion and von Willebrand factor cleaving activity
R568K/F592Y/R660K/Y661F/Y665F
gain-of-function ADAMTS13 spacer domain variant, about 2.5fold more active than wild-type ADAMTS13, but cannot be further activated by anti-CUB monoclonal antibody or von Willebrand factor D4CK and is unable to bind or to be inhibited by the CUB1-2 domains
W390A
the mutant has impaired binding affinity to its substrate von Willebrand factor. The mutation retards the enzyme's secretion, leading to its deposition in endoplasmic reticulum. Compared with the wild type enzyme, the mutant also has a decreased cleavage activity for multimeric von Willebrand factor under both static and shear stress conditions
568K/F592Y/R660K/Y661F/Y665F
-
the mutant shows enhanced proteolytic activity compared to the wild type enzyme
A1033T
-
naturally occuring mutation of ADAMTS13
A250V
-
naturally occuring mutation of ADAMTS13
A596V
-
naturally occuring mutation of ADAMTS13
A606P
-
naturally occuring mutation of ADAMTS13
A732V
-
naturally occuring mutation of ADAMTS13
A900V
C1024G
-
naturally occuring mutation of ADAMTS13
C1213Y
-
naturally occuring mutation of ADAMTS13
C311Y
-
naturally occuring mutation of ADAMTS13
C347S
-
naturally occuring mutation of ADAMTS13
C508Y
C758R
-
naturally occuring mutation of ADAMTS13
C908S
-
naturally occuring mutation of ADAMTS13
C908Y
-
naturally occuring mutation of ADAMTS13
C951G
-
naturally occuring mutation of ADAMTS13
C977W
-
deletion of 6 nucleotides GTGCCC at position 2930-2935, i.e. c.2930_2935del GTGCCC, in exon 23, leading to the replacement of Cys977 residue by a Trp
D187A
D235H
-
naturally occuring mutation of ADAMTS13
D252N
-
the ADAMTS13 VR2 single-point mutant is secreted as the wild type enzyme
D330A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D340A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
D343A
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
D500E
-
point mutation in the RGD cysteine-rich domain, unaltered activity compared to the wild-type enzyme
E184A
E184A/L185A/D187A/R190A
-
the proteolytic function of the mutant is severely affected
E184A/L185A/D187A/R190A/Q191A/V192N/R193A
-
the mutant has abolished activity against von Willebrand factor 115
E212A
-
site-directed mutagenesis of a Ca2+ binding site residue, the kinetic dissociation constant of ADAMTS13 for Ca2+ is dramatically reduced compared to the wild-type enzyme, Vmax of the mutant is also reduced by 75% compared to the wild-type
E627X
-
naturally occuring mutation of ADAMTS13
E634K
-
naturally occuring mutation of ADAMTS13
E663A
E664A
E740K
-
naturally occuring mutation of ADAMTS13
G1239V
G525D
-
naturally occuring mutation of ADAMTS13
G662A
G982R
-
naturally occuring mutation of ADAMTS13
H234Q
-
naturally occuring mutation of ADAMTS13
H96D
-
naturally occuring mutation of ADAMTS13
I1217T
-
naturally occuring mutation of ADAMTS13
I178T
-
naturally occuring mutation of ADAMTS13
I673F
-
naturally occuring mutation of ADAMTS13
I79M
-
naturally occuring mutation of ADAMTS13
L185A
-
the mutant exhibits wild type activity
L218A
-
the ADAMTS13 VR2 single-point mutant is secreted poorly
L232Q
-
naturally occuring mutation of ADAMTS13
L350G
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
L351G
-
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
P353L
-
naturally occuring mutation of ADAMTS13
P457L
-
naturally occuring mutation of ADAMTS13
P475S
P618A
P618A/A732V
-
mutation induces secretion deficiency
P671L
-
naturally occuring mutation of ADAMTS13
Q1302X
-
naturally occuring mutation of ADAMTS13
Q191A
-
the mutant exhibits wild type activity
Q197A
-
the mutant exhibits wild type activity
Q333A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
Q448E
Q449X
-
naturally occuring mutation of ADAMTS13
Q44X
-
naturally occuring mutation of ADAMTS13
Q456H
-
naturally occuring mutation of ADAMTS13
Q929X
-
naturally occuring mutation of ADAMTS13
R102C
-
naturally occuring mutation of ADAMTS13
R1034X
-
naturally occuring mutation of ADAMTS13
R1060W
-
naturally occuring mutation of ADAMTS13
R1096H
-
naturally occuring mutation of ADAMTS13
R1123C
-
naturally occuring mutation of ADAMTS13
R1206X
-
naturally occuring mutation of ADAMTS13
R1219W
-
naturally occuring mutation of ADAMTS13
R1336
-
mutation induces secretion deficiency
R1336W
-
naturally occuring mutation of ADAMTS13
R190A
-
the mutant shows 2fold reduced catalytic efficiency against von Willebrand factor 115 compared to the wild type enzyme
R193A
-
the mutant shows 4fold reduced catalytic efficiency against von Willebrand factor 115 compared to the wild type enzyme
R193W
-
naturally occuring mutation of ADAMTS13
R257A
-
the ADAMTS13 VR2 single-point mutant is secreted as the wild type enzyme
R268P
R349A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, the mutant enzyme shows increased activity with the mutant D1614A von Willebrand factor115 substrate compared to the wild-type enzyme
R349C
-
naturally occuring mutation of ADAMTS13
R398H
-
naturally occuring mutation of ADAMTS13
R484K
-
naturally occuring mutation of ADAMTS13
R507Q
-
naturally occuring mutation of ADAMTS13
R528G
-
naturally occuring mutation of ADAMTS13
R625H
-
naturally occuring mutation of ADAMTS13
R659A
R660A
R660A/Y661A
-
site-directed mutagenesis
R660A/Y661A/Y665A
-
site-directed mutagenesis, the ADAMTS13 variant, i.e. ADAMTS13-RYY, shows a 12fold reduced catalytic efficiency arising from over 25fold reduced substrate binding
R660A/Y665A
-
site-directed mutagenesis
R692C
-
naturally occuring mutation of ADAMTS13
R910X
-
naturally occuring mutation of ADAMTS13
S119A
-
site-directed mutagensis, mutant S119A has properties similar to natural mutant S119F
S119F
S119F/Q448E
-
naturally occuring mutation in the ADAMTS13 metalloprotease domain. The mutant is expressed normally, but shows markedly impaired secretion
S203P
-
naturally occuring mutation of ADAMTS13
S251A
-
the ADAMTS13 VR2 single-point mutant is secreted poorly
S263C
-
naturally occuring mutation of ADAMTS13
S903L
-
naturally occuring mutation of ADAMTS13
T1226I
-
naturally occuring mutation of ADAMTS13
T196A
-
the mutant exhibits wild type activity
T196I
-
naturally occuring mutation of ADAMTS13
T260A
-
the ADAMTS13 VR2 single-point mutant is secreted as the wild type enzyme
T339R
-
naturally occuring mutation of ADAMTS13
V192N
-
the mutant exhibits wild type activity
V352G
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V604I
-
naturally occuring mutation of ADAMTS13
V832M
-
naturally occuring mutation of ADAMTS13
W1016X
-
naturally occuring mutation of ADAMTS13
W1245X
-
naturally occuring mutation of ADAMTS13
W390C
-
naturally occuring mutation of ADAMTS13
W390X
-
naturally occuring mutation of ADAMTS13
Y304C
-
naturally occuring mutation of ADAMTS13
Y658A
-
site-directed mutagenesis
Y661A
Y661A/Y665A
-
site-directed mutagenesis
Y665A
-
site-directed mutagenesis
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1 - 8.8
-
the activity of purified pADAMTS13 is stable and relatively constant at pH ranges between pH 6.1 and 8.8 for 18 h storage at 4°C. However, ADAMTS13 activity is almost totally lost below pH 3.1
719761
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
stable for several days during purification at room temperature
25 - 37
-
the enzyme is stable at room temperature for up to 24 h irrespective of the presence of citrate (0.38% (w/v)). However, at 37°C, citrate causes a time-dependent activity decrease
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADAMTS-13 is highly stable in plasma that is stored frozen at -80°C
-
no enzyme activity decrease is seen in heparinized plasma, but the addition of citrate causes enzyme instability at 37°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged ADAMTS13 ancillary domains, ADAMTS13-DTCS, consisting of residues 287-685, from CHO Lec cells by nickel affinity and cation exchange chromatography
A10-agarose column chromatography, HiTrap DEAE column chromatography, and Superdex 200 gel filtration
-
about 10000fold
-
from commercial factor VIII/vWF concentrate
-
HiLoad Superdex 200 gel filtration
-
Ni-NTA agarose column chromatography
-
Ni-NTA column chromatography
-
recombinant ADAMTS-13 from HEK293 cells by Zn2+-agarose affinity and anion exchange chromatography to homogeneity
-
recombinant His-tagged ADAMTS13 by nickel affinity chromatography
-
recombinant His-tagged ADAMTS13 from HEK-293 cells by anion exchange chromatography, Ni affinity chromatography, and gel filtration
-
recombinant structure-based mutants of ADAMTS13-MDTCS residues 75-685 fragment with a C-terminal tobacco etch virus proteinase cleavage site followed by tandem His-tag sequences from CHO Lec 3.2.8.1 cells by nickel affinity chromatography and gel filtration
-
recombinant tagged deletion mutants
-
recombinant wild-type ADAMTS13 with a C-terminal Myc/His tag from HEK293 cells, and recombinant His-tagged truncated DAMTS13 mutants MP-Dis and MP by nickel affinity chromatography and gel filtration
-
recombinant wild-type and mutant ADAMTS13 from HEK-293 cells by nickel affinity chromatography
-
recombinant wild-type and mutant ADAMTS13s with a C-terminal Myc/His tag expressed from HEK-293 cells by nickel affinity chromatography
-
Sephadex 26/10 gel filtration
-
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis
expression in HEK-293 cell
expression of FLAG-tagged ADAMTS13 in HEK-293 cells, co-expression with thrombospondin1
stable expression of His-tagged ADAMTS13 ancillary domains, ADAMTS13-DTCS, consisting of residues 287-685, in CHO Lec cells
transient expression in HEK293 cells
ADAMTS13 DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, genotyping and expression analysis in HEK-293 cells, overview
-
ADAMTS13 genotyping, overview
-
construction of ADAMTS13 epitope library
-
DNA and amino acid sequence determination and analysis, genotyping
-
DNA sequence determination and analysis, transient expression of wild-type and mutants as FLAG-tagged enzymes in HeLa cells
-
DNA sequence determination of natural genetic variants, heterozygous polymorphism at Tyr/Cys1584 and other, overview
-
expressed in CHO cells
-
expressed in HEK-293 cells
-
expressed in HeLa cells
-
expressed in T-REx 293 cells
-
expression of a series of partial deletions in the A2 domain flanked with N- and C-terminal tags in Escherichia coli
-
expression of ADAMTS-13 in HEK293 cells
-
expression of ADAMTS13 in HEK-293 cells
-
expression of His-tagged ADAMTS13
-
expression of structure-based mutants of ADAMTS13-MDTCS residues 75-685 fragment with a C-terminal tobacco etch virus proteinase cleavage site followed by tandem His-tag sequences in CHO Lec 3.2.8.1 cells. Transient expression of His-tagged mutant ADAMTS13-MDTCS domains using a cytomegalovirus promoter-driven expression vector in HeLa cells
-
expression of wild-type ADAMTS13 with a C-terminal Myc/His tag in HEK293 cells, transient expression of His-tagged truncated DAMTS13 mutants MP-Dis and MP and point mutants in HEK-293T cells
-
expression of wild-type and mutant ADAMTS13 in HEK-293 cells
-
expression of wild-type and mutant ADAMTS13s with a C-terminal Myc/His tag expressed in HEK-293 cells
-
expression of wild-type and mutant enzymes in HEK 293 and COS-7 cells
-
gene ADAMTS13, location of chromosome 9q34
-
gene ADMTS13 and mutant variant truncated after the spacer domain, MDTCS, expression in transgenic mice
-
stable expression in HEK-293 cells
-
stable expression of His-tagged ADAMTS13 in HEK-293 cells
-
transient expression in HeLa cells, in HepG2 cells, in RFL6 cells, and in COS-1 cells, highest expression level is obtained in HeLa cells
-
transient expression of C-terminally tagged enzyme in COS-7 cells or expression in a Sf9 cells/baculovirus expression system, tagged with His6 or V5 epitopes
-
transient expression of wild-type and mutants in HeLa cells as FLAG-tagged proteins
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
plasma enzyme activity in aneurysmal subarachnoid haemorrhage patients is significantly lower than that in healthy subjects
enzyme activity is significantly higher in men with acute human immunodeficiency virus infection than in uninfected controls and in both acute and chronic untreated HIV infection relative to chronic treated infection
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of a 77-amino acid flow cytometry substrate to measure ADAMTS13 activity. Substrate is suitable for microsphere-cytometer based assays in the milieu of human blood plasma. It contains the partial A2-domain of von Willebrand factor (VWF amino acids 1594-1670) that is mutated to include a single primary amine at the N-terminus and free cysteines at the C-terminus. Substrate is bound to streptavidin-bearing microspheres with varyable polyethylene glycol spacer lengths. Recombinant ADAMTS13 activity can be quantified using substrates with all varyable polyethylene glycol repeat-lengths, but only a construct with the longer 77 PEG-unit can quantify proteolysis in blood plasma. Plasma ADAMTS13 down to 5% of normal levels can be detected within 30 min. Enzyme catalytic activity is tuned by varying buffer calcium, with lower divalent ion concentrations enhancing cleavage
medicine
diagnostics
drug development
-
inhibitory anti-ADAMTS 13 antibodies, measurement and clinical application, overview
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chung, D.W.; Fujikawa, K.
Processing of von Willebrand Factor by ADAMTS-13
Biochemistry
41
11065-11070
2002
Homo sapiens
Manually annotated by BRENDA team
Plaimauer, B.; Zimmermann, K.; Volkel, D.; Antoine, G.; Kerschbaumer, R.; Jenab, P.; Furlan, M.; Gerritsen, H.; Lammle, B.; Schwarz, H.P.; Scheiflinger, F.
Cloning, expression, and functional characterization of the von Willebrand factor-cleaving protease (ADAMTS13)
Blood
100
3626-3632
2002
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Dong, J.F.; Moake, J.L.; Nolasco, L.; Bernardo, A.; Arceneaux, W.; Shrimpton, C.N.; Schade, A.J.; McIntire, L.V.; Fujikawa, K.; Lopez, J.A.
ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions
Blood
100
4033-4039
2002
Homo sapiens
Manually annotated by BRENDA team
Soejima, K.; Matsumoto, M.; Kokame, K.; Yagi, H.; Ishizashi, H.; Maeda, H.; Nozaki, C.; Miyata, T.; Fujimura, Y.; Nakagaki, T.
ADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage
Blood
102
3232-3237
2003
Homo sapiens
Manually annotated by BRENDA team
Kokame, K.; Matsumoto, M.; Fujimura, Y.; Miyata, T.
VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13
Blood
103
607-612
2003
Homo sapiens
Manually annotated by BRENDA team
Bowen, D.J.; Collins, P.W.
An amino acid polymorphism in von Willebrand factor correlates with increased susceptibility to proteolysis by ADAMTS13
Blood
103
941-947
2003
Homo sapiens
Manually annotated by BRENDA team
Furlan, M.; Robles, R.; Lamie, B.
Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis
Blood
87
4223-4234
1996
Homo sapiens
Manually annotated by BRENDA team
Fujikawa, K.; Suzuki, H.; McMullen, B.; Chung, D.
Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family
Blood
98
1662-1666
2001
Homo sapiens
Manually annotated by BRENDA team
Arai, S.; Allan, C.; Streiff, M.; Hutchins, G.M.; Vogelsang, G.B.; Tsai, H.M.
Von Willebrand factor-cleaving protease activity and proteolysis of von Willebrand factor in bone marrow transplant-associated thrombotic microangiopathy
Hematol. J.
2
292-299
2001
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.; Chung, D.; Takayama, T.K.; Majerus, E.M.; Sadler, J.E.; Fujikawa, K.
Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura
J. Biol. Chem.
276
41059-41063
2001
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Zheng, X.; Nishio, K.; Majerus, E.M.; Sadler, J.E.
Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13
J. Biol. Chem.
278
30136-30141
2003
Homo sapiens
Manually annotated by BRENDA team
Majerus, E.M.; Zheng, X.; Tuley, E.A.; Sadler, J.E.
Cleavage of the ADAMTS13 propeptide is not required for protease activity
J. Biol. Chem.
278
46643-46648
2003
Homo sapiens
Manually annotated by BRENDA team
Kokame, K.; Matsumoto, M.; Soejima, K.; Yagi, H.; Ishizashi, H.; Funato, M.; Tamai, H.; Konno, M.; Kamide, K.; Kawano, Y.; Miyata, T.; Fujimura, Y.
Mutations and common polymorphisms in ADAMTS13 gene responsible for von Willebrand factor-cleaving protease activity
Proc. Natl. Acad. Sci. USA
99
11902-11907
2002
Homo sapiens
Manually annotated by BRENDA team
Sugimoto, T.; Saigo, K.; Shin, T.; Kaneda, Y.; Manabe, N.; Narita, H.; Wakuya, J.; Imoto, S.; Murayama, T.; Matsumoto, M.; Fujimura, Y.; Nishimura, R.; Koizumi, T.; Kumagai, S.
von Willebrand factor-cleaving protease activity remains at the intermediate level in thrombotic thrombocytopenic purpura
Acta Haematol.
113
198-203
2005
Homo sapiens
Manually annotated by BRENDA team
Schnog, J.J.; Hovinga, J.A.; Krieg, S.; Akin, S.; Laemmle, B.; Brandjes, D.P.; Mac Gillavry, M.R.; Muskiet, F.D.; Duits, A.J.; Duits, A.J.
ADAMTS13 activity in sickle cell disease
Am. J. Hematol.
81
492-498
2006
Homo sapiens
Manually annotated by BRENDA team
Plaimauer, B.; Fuhrmann, J.; Mohr, G.; Wernhart, W.; Bruno, K.; Ferrari, S.; Konetschny, C.; Antoine, G.; Rieger, M.; Scheiflinger, F.
Modulation of ADAMTS13 secretion and specific activity by a combination of common amino acid polymorphisms and a missense mutation
Blood
107
118-125
2006
Homo sapiens
Manually annotated by BRENDA team
Perutelli, P.; Amato, S.; Molinari, A.C.
Cleavage of von Willebrand factor by ADAMTS-13 in vitro: effect of temperature and barium ions on the proteolysis kinetics
Blood Coagul. Fibrinolysis
16
607-611
2005
Homo sapiens
Manually annotated by BRENDA team
Miyata, T.; Kokame, K.; Banno, F.
Measurement of ADAMTS13 activity and inhibitors
Curr. Opin. Hematol.
12
384-389
2005
Homo sapiens
Manually annotated by BRENDA team
Peyvandi, F.; Lavoretano, S.; Palla, R.; Valsecchi, C.; Merati, G.; De Cristofaro, R.; Rossi, E.; Mannuccio Mannucci, P.
Mechanisms of the interaction between two ADAMTS13 gene mutations leading to severe deficiency of enzymatic activity
Hum. Mutat.
27
330-336
2006
Homo sapiens
Manually annotated by BRENDA team
Zhou, W.; Dong, L.; Ginsburg, D.; Bouhassira, E.E.; Tsai, H.M.
Enzymatically active ADAMTS13 variants are not inhibited by anti-ADAMTS13 autoantibodies: a novel therapeutic strategy?
J. Biol. Chem.
280
39934-39941
2005
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Zanardelli, S.; Crawley, J.T.; Chion, C.K.; Lam, J.K.; Preston, R.J.; Lane, D.A.
ADAMTS13 substrate recognition of von Willebrand factor A2 domain
J. Biol. Chem.
281
1555-1563
2006
Homo sapiens
Manually annotated by BRENDA team
Anderson, P.J.; Kokame, K.; Sadler, J.E.
Zinc and calcium ions cooperatively modulate ADAMTS13 activity
J. Biol. Chem.
281
850-857
2006
Homo sapiens
Manually annotated by BRENDA team
Schmugge, M.; Dunn, M.S.; Amankwah, K.S.; Blanchette, V.S.; Freedman, J.; Rand, M.L.
The activity of the von Willebrand factor cleaving protease ADAMTS-13 in newborn infants
J. Thromb. Haemost.
2
228-233
2004
Homo sapiens
Manually annotated by BRENDA team
Plaimauer, B.; Scheiflinger, F.
Expression and characterization of recombinant human ADAMTS-13
Semin. Hematol.
41
24-33
2004
Homo sapiens
Manually annotated by BRENDA team
Sanchez-Luceros, A.; Farias, C.E.; Amaral, M.M.; Kempfer, A.C.; Votta, R.; Marchese, C.; Salviu, M.J.; Woods, A.I.; Meschengieser, S.S.; Lazzari, M.A.
von Willebrand factor-cleaving protease (ADAMTS13) activity in normal non-pregnant women, pregnant and post-delivery women
Thromb. Haemost.
92
1320-1326
2004
Homo sapiens
Manually annotated by BRENDA team
Reiter, R.A.; Varadi, K.; Turecek, P.L.; Jilma, B.; Knoebl, P.
Changes in ADAMTS13 (von-Willebrand-factor-cleaving protease) activity after induced release of von Willebrand factor during acute systemic inflammation
Thromb. Haemost.
93
554-558
2005
Homo sapiens
Manually annotated by BRENDA team
Perutelli, P.; Amato, S.; Calevo, M.G.; Molinari, A.C.
Von Willerbrand factor cleaving protease (ADAMTS-13) activity is stable in a set of plasma samples after prolonged storage at -80 Deg
Thromb. Res.
116
443-445
2005
Homo sapiens
Manually annotated by BRENDA team
Perutelli, P.; Amato, S.; Molinari, A.C.
ADAMTS-13 activity in von Willebrand disease
Thromb. Res.
117
685-688
2006
Homo sapiens
Manually annotated by BRENDA team
Matsukawa, M.; Kaikita, K.; Soejima, K.; Fuchigami, S.; Nakamura, Y.; Honda, T.; Tsujita, K.; Nagayoshi, Y.; Kojima, S.; Shimomura, H.; Sugiyama, S.; Fujimoto, K.; Yoshimura, M.; Nakagaki, T.; Ogawa, H.
Serial changes in von Willebrand factor-cleaving protease (ADAMTS13) and prognosis after acute myocardial infarction
Am. J. Cardiol.
100
758-763
2007
Homo sapiens
Manually annotated by BRENDA team
Shida, Y.; Nishio, K.; Sugimoto, M.; Mizuno, T.; Hamada, M.; Kato, S.; Matsumoto, M.; Okuchi, K.; Fujimura, Y.; Yoshioka, A.
Functional imaging of shear-dependent activity of ADAMTS13 in regulating mural thrombus growth under whole blood flow conditions
Blood
111
1295-1298
2008
Homo sapiens
Manually annotated by BRENDA team
McKinnon, T.A.; Chion, A.C.; Millington, A.J.; Lane, D.A.; Laffan, M.A.
N-linked glycosylation of VWF modulates its interaction with ADAMTS13
Blood
111
3042-3049
2008
Homo sapiens
Manually annotated by BRENDA team
Starke, R.; Machin, S.; Scully, M.; Purdy, G.; Mackie, I.
The clinical utility of ADAMTS13 activity, antigen and autoantibody assays in thrombotic thrombocytopenic purpura
Br. J. Haematol.
136
649-655
2007
Homo sapiens
Manually annotated by BRENDA team
Jin, M.; Casper, T.C.; Cataland, S.R.; Kennedy, M.S.; Lin, S.; Li, Y.J.; Wu, H.M.
Relationship between ADAMTS13 activity in clinical remission and the risk of TTP relapse
Br. J. Haematol.
141
651-658
2008
Homo sapiens
Manually annotated by BRENDA team
Dong, J.F.
Structural and functional correlation of ADAMTS13
Curr. Opin. Hematol.
14
270-276
2007
Homo sapiens
Manually annotated by BRENDA team
Keeney, S.; Grundy, P.; Collins, P.W.; Bowen, D.J.
C1584 in von Willebrand factor is necessary for enhanced proteolysis by ADAMTS13 in vitro
Haemophilia
13
405-408
2007
Homo sapiens
Manually annotated by BRENDA team
Soejima, K.; Nakamura, H.; Hirashima, M.; Morikawa, W.; Nozaki, C.; Nakagaki, T.
Analysis on the molecular species and concentration of circulating ADAMTS13 in blood
J. Biochem.
139
147-154
2006
Homo sapiens
Manually annotated by BRENDA team
De Cristofaro, R.; Peyvandi, F.; Baronciani, L.; Palla, R.; Lavoretano, S.; Lombardi, R.; Di Stasio, E.; Federici, A.B.; Mannucci, P.M.
Molecular mapping of the chloride-binding site in von Willebrand factor (VWF): energetics and conformational effects on the VWF/ADAMTS-13 interaction
J. Biol. Chem.
281
30400-30411
2006
Homo sapiens
Manually annotated by BRENDA team
Chung, M.C.; Popova, T.G.; Jorgensen, S.C.; Dong, L.; Chandhoke, V.; Bailey, C.L.; Popov, S.G.
Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy
J. Biol. Chem.
283
9531-9542
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Turner, N.; Nolasco, L.; Tao, Z.; Dong, J.F.; Moake, J.
Human endothelial cells synthesize and release ADAMTS-13
J. Thromb. Haemost.
4
1396-1404
2006
Homo sapiens
Manually annotated by BRENDA team
Tao, Z.; Anthony, K.; Peng, Y.; Choi, H.; Nolasco, L.; Rice, L.; Moake, J.L.; Dong, J.F.
Novel ADAMTS-13 mutations in an adult with delayed onset thrombotic thrombocytopenic purpura
J. Thromb. Haemost.
4
1931-1935
2006
Homo sapiens
Manually annotated by BRENDA team
Lam, J.K.; Chion, C.K.; Zanardelli, S.; Lane, D.A.; Crawley, J.T.
Further characterization of ADAMTS-13 inactivation by thrombin
J. Thromb. Haemost.
5
1010-1018
2007
Homo sapiens
Manually annotated by BRENDA team
Wu, J.J.; Fujikawa, K.; McMullen, B.A.; Chung, D.W.
Characterization of a core binding site for ADAMTS-13 in the A2 domain of von Willebrand factor
Proc. Natl. Acad. Sci. USA
103
18470-18474
2006
Homo sapiens
Manually annotated by BRENDA team
Gao, W.; Anderson, P.J.; Majerus, E.M.; Tuley, E.A.; Sadler, J.E.
Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease
Proc. Natl. Acad. Sci. USA
103
19099-19104
2006
Homo sapiens
Manually annotated by BRENDA team
Shenkman, B.; Budde, U.; Angerhaus, D.; Lubetsky, A.; Savion, N.; Seligsohn, U.; Varon, D.
ADAMTS-13 regulates platelet adhesion under flow. A new method for differentiation between inherited and acquired thrombotic thrombocytopenic purpura
Thromb. Haemost.
96
160-166
2006
Homo sapiens
Manually annotated by BRENDA team
Fuchigami, S.; Kaikita, K.; Soejima, K.; Matsukawa, M.; Honda, T.; Tsujita, K.; Nagayoshi, Y.; Kojima, S.; Nakagaki, T.; Sugiyama, S.; Ogawa, H.
Changes in plasma von Willebrand factor-cleaving protease (ADAMTS13) levels in patients with unstable angina
Thromb. Res.
122
618-623
2008
Homo sapiens
Manually annotated by BRENDA team
Gunther, K.; Garizio, D.; Nesara, P.
ADAMTS13 activity and the presence of acquired inhibitors in human immunodeficiency virus-related thrombotic thrombocytopenic purpura
Transfusion
47
1710-1716
2007
Homo sapiens
Manually annotated by BRENDA team
Gao, W.; Anderson, P.J.; Sadler, J.E.
Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity
Blood
112
1713-1719
2008
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Zhou, W.; Tsai, H.M.
N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity
Blood
113
929-935
2009
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Pruss, C.M.; Notley, C.R.; Hegadorn, C.A.; OBrien, L.A.; Lillicrap, D.
ADAMTS13 cleavage efficiency is altered by mutagenic and, to a lesser extent, polymorphic sequence changes in the A1 and A2 domains of von Willebrand factor
Br. J. Haematol.
143
552-558
2008
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Bongers, T.N.; de Bruijne, E.L.; Dippel, D.W.; de Jong, A.J.; Deckers, J.W.; Poldermans, D.; de Maat, M.P.; Leebeek, F.W.
Lower levels of ADAMTS13 are associated with cardiovascular disease in young patients
Atherosclerosis
207
250-254
2009
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Akiyama, M.; Takeda, S.; Kokame, K.; Takagi, J.; Miyata, T.
Production, crystallization and preliminary crystallographic analysis of an exosite-containing fragment of human von Willebrand factor-cleaving proteinase ADAMTS13
Acta Crystallogr. Sect. F
65
739-742
2009
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Pereboom, I.T.; Adelmeijer, J.; van Leeuwen, Y.; Hendriks, H.G.; Porte, R.J.; Lisman, T.
Development of a severe von Willebrand factor/ADAMTS13 dysbalance during orthotopic liver transplantation
Am. J. Transplant.
9
1189-1196
2009
Homo sapiens
Manually annotated by BRENDA team
de Mast, Q.; Groot, E.; Asih, P.B.; Syafruddin, D.; Oosting, M.; Sebastian, S.; Ferwerda, B.; Netea, M.G.; de Groot, P.G.; van der Ven, A.J.; Fijnheer, R.
ADAMTS13 deficiency with elevated levels of ultra-large and active von Willebrand factor in P. falciparum and P. vivax malaria
Am. J. Trop. Med. Hyg.
80
492-498
2009
Homo sapiens
Manually annotated by BRENDA team
Moriki, T.; Maruyama, I.N.; Igari, A.; Ikeda, Y.; Murata, M.
Identification of ADAMTS13 peptide sequences binding to von Willebrand factor
Biochem. Biophys. Res. Commun.
391
783-788
2010
Homo sapiens
Manually annotated by BRENDA team
Scully, M.
Inhibitory anti-ADAMTS 13 antibodies: measurement and clinical application
Blood Rev.
24
11-16
2010
Homo sapiens
Manually annotated by BRENDA team
Gardner, M.; Chion, C.; Groot, R.; Shah, A.; Crawley, J.; Lane, D.
A functional calcium-binding site in the metalloprotease domain of ADAMTS13
Blood
113
1149-1157
2009
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.
A team player: The disintegrin domain of ADAMTS13
Blood
113
5373-5374
2009
Homo sapiens
Manually annotated by BRENDA team
de Groot, R.; Bardhan, A.; Ramroop, N.; Lane, D.A.; Crawley, J.T.
Essential role of the disintegrin-like domain in ADAMTS13 function
Blood
113
5609-5616
2009
Homo sapiens
Manually annotated by BRENDA team
Raife, T.J.; Cao, W.; Atkinson, B.S.; Bedell, B.; Montgomery, R.R.; Lentz, S.R.; Johnson, G.F.; Zheng, X.L.
Leukocyte proteases cleave von Willebrand factor at or near the ADAMTS13 cleavage site
Blood
114
1666-1674
2009
Homo sapiens
Manually annotated by BRENDA team
Zanardelli, S.; Chion, A.C.; Groot, E.; Lenting, P.J.; McKinnon, T.A.; Laffan, M.A.; Tseng, M.; Lane, D.A.
A novel binding site for ADAMTS13 constitutively exposed on the surface of globular VWF
Blood
114
2819-2828
2009
Homo sapiens
Manually annotated by BRENDA team
Zhao, B.Q.; Chauhan, A.K.; Canault, M.; Patten, I.S.; Yang, J.J.; Dockal, M.; Scheiflinger, F.; Wagner, D.D.
von Willebrand factor-cleaving protease ADAMTS13 reduces ischemic brain injury in experimental stroke
Blood
114
3329-3334
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Feys, H.B.; Pareyn, I.; Vancraenenbroeck, R.; De Maeyer, M.; Deckmyn, H.; Van Geet, C.; Vanhoorelbeke, K.
Mutation of the H-bond acceptor S119 in the ADAMTS13 metalloprotease domain reduces secretion and substrate turnover in a patient with congenital thrombotic thrombocytopenic purpura
Blood
114
4749-4752
2009
Homo sapiens
Manually annotated by BRENDA team
Turner, N.A.; Nolasco, L.; Ruggeri, Z.M.; Moake, J.L.
Endothelial cell ADAMTS-13 and VWF: production, release, and VWF string cleavage
Blood
114
5102-5111
2009
Homo sapiens
Manually annotated by BRENDA team
Zheng, X.
ADAMTS13 testing: Why bother?
Blood
115
1475-1476
2010
Homo sapiens
Manually annotated by BRENDA team
Pos, W.; Crawley, J.T.; Fijnheer, R.; Voorberg, J.; Lane, D.A.; Luken, B.M.
An autoantibody epitope comprising residues R660, Y661, and Y665 in the ADAMTS13 spacer domain identifies a binding site for the A2 domain of VWF
Blood
115
1640-1649
2010
Homo sapiens
Manually annotated by BRENDA team
Jin, S.Y.; Skipwith, C.G.; Zheng, X.L.
Amino acid residues Arg(659), Arg(660), and Tyr(661) in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor
Blood
115
2300-2310
2010
Homo sapiens
Manually annotated by BRENDA team
McGrath, R.T.; McKinnon, T.A.; Byrne, B.; OKennedy, R.; Terraube, V.; McRae, E.; Preston, R.J.; Laffan, M.A.; ODonnell, J.S.
Expression of terminal alpha2-6-linked sialic acid on von Willebrand factor specifically enhances proteolysis by ADAMTS13
Blood
115
2666-2673
2010
Homo sapiens
Manually annotated by BRENDA team
Wu, T.; Lin, J.; Cruz, M.A.; Dong, J.F.; Zhu, C.
Force-induced cleavage of single VWFA1A2A3 tridomains by ADAMTS-13
Blood
115
370-378
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, J.; Fu, X.; Wang, Y.; Ling, M.; McMullen, B.; Kulman, J.; Chung, D.W.; Lopez, J.A.
Oxidative modification of von Willebrand factor by neutrophil oxidants inhibits its cleavage by ADAMTS13
Blood
115
706-712
2010
Homo sapiens
Manually annotated by BRENDA team
Claus, R.A.; Bockmeyer, C.L.; Sossdorf, M.; Loesche, W.
The balance between von-Willebrand factor and its cleaving protease ADAMTS13: biomarker in systemic inflammation and development of organ failure?
Curr. Mol. Med.
10
236-248
2010
Homo sapiens
Manually annotated by BRENDA team
Lancellotti, S.; De Filippis, V.; Pozzi, N.; Peyvandi, F.; Palla, R.; Rocca, B.; Rutella, S.; Pitocco, D.; Mannucci, P.M.; De Cristofaro, R.
Formation of methionine sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13: a new prothrombotic mechanism in diseases associated with oxidative stress
Free Radic. Biol. Med.
48
446-456
2010
Homo sapiens
Manually annotated by BRENDA team
Trionfini, P.; Tomasoni, S.; Galbusera, M.; Motto, D.; Longaretti, L.; Corna, D.; Remuzzi, G.; Benigni, A.
Adenoviral-mediated gene transfer restores plasma ADAMTS13 antigen and activity in ADAMTS13 knockout mice
Gene Ther.
16
1373-1379
2009
Homo sapiens
Manually annotated by BRENDA team
Palla, R.; Lavoretano, S.; Lombardi, R.; Garagiola, I.; Karimi, M.; Afrasiabi, A.; Ramzi, M.; De Cristofaro, R.; Peyvandi, F.
The first deletion mutation in the TSP1-6 repeat domain of ADAMTS13 in a family with inherited thrombotic thrombocytopenic purpura
Haematologica
94
289-293
2009
Homo sapiens
Manually annotated by BRENDA team
Lotta, L.A.; Garagiola, I.; Palla, R.; Cairo, A.; Peyvandi, F.
ADAMTS13 mutations and polymorphisms in congenital thrombotic thrombocytopenic purpura
Hum. Mutat.
31
11-19
2010
Homo sapiens
Manually annotated by BRENDA team
Kato, R.; Shinohara, A.; Sato, J.
ADAMTS13 deficiency, an important cause of thrombocytopenia during pregnancy
Int. J. Obstet. Anesth.
18
73-77
2009
Homo sapiens
Manually annotated by BRENDA team
Kosugi, N.; Tsurutani, Y.; Isonishi, A.; Hori, Y.; Matsumoto, M.; Fujimura, Y.
Influenza A infection triggers thrombotic thrombocytopenic purpura by producing the anti-ADAMTS13 IgG inhibitor
Intern. Med.
49
689-693
2010
Homo sapiens
Manually annotated by BRENDA team
Vomund, A.N.; Majerus, E.M.
ADAMTS13 bound to endothelial cells exhibits enhanced cleavage of von Willebrand factor
J. Biol. Chem.
284
30925-30932
2009
Homo sapiens
Manually annotated by BRENDA team
Dwyre, D.M.; Dursteler, B.; Nashelsky, M.; Friedman, K.D.; Raife, T.J.
Value of ADAMTS13 activity and inhibitor in the postmortem diagnosis of thrombotic thrombocytopenic purpura
J. Clin. Apher.
24
106-110
2009
Homo sapiens
Manually annotated by BRENDA team
Park, Y.A.; Hay, S.N.; King, K.E.; Matevosyan, K.; Poisson, J.; Powers, A.; Sarode, R.; Shaz, B.; Brecher, M.E.
Is it quinine TTP/HUS or quinine TMA? ADAMTS13 levels and implications for therapy
J. Clin. Apher.
24
115-119
2009
Homo sapiens
Manually annotated by BRENDA team
Park, Y.A.; Hay, S.N.; Brecher, M.E.
ADAMTS13 activity levels in patients with human immunodeficiency virus-associated thrombotic microangiopathy and profound CD4 deficiency
J. Clin. Apher.
24
32-36
2009
Homo sapiens
Manually annotated by BRENDA team
Varadi, K.; Rottensteiner, H.; Vejda, S.; Weber, A.; Muchitsch, E.M.; Turecek, P.L.; Ehrlich, H.J.; Scheiflinger, F.; Schwarz, H.P.
Species-dependent variability of ADAMTS13-mediated proteolysis of human recombinant von Willebrand factor
J. Thromb. Haemost.
7
1134-1142
2009
Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Macaca fascicularis, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Hughes, C.; McEwan, J.R.; Longair, I.; Hughes, S.; Cohen, H.; Machin, S.; Scully, M.
Cardiac involvement in acute thrombotic thrombocytopenic purpura: association with troponin T and IgG antibodies to ADAMTS 13
J. Thromb. Haemost.
7
529-536
2009
Homo sapiens
Manually annotated by BRENDA team
Niiya, M.; Endo, M.; Shang, D.; Zoltick, P.; Muvarak, N.; Cao, W.; Jin, S.; Skipwith, C.; Motto, D.; Flake, A.; Zheng, X.
Correction of ADAMTS13 deficiency by in utero gene transfer of lentiviral vector encoding ADAMTS13 genes
Mol. Ther.
17
34-41
2009
Homo sapiens
Manually annotated by BRENDA team
Meng, H.; Zhang, X.; Blaivas, M.; Wang, M.M.
Localization of blood proteins thrombospondin1 and ADAMTS13 to cerebral corpora amylacea
Neuropathology
29
664-671
2009
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Manea, M.; Tati, R.; Karlsson, J.; Békássy, Z.; Karpman, D.
Biologically active ADAMTS13 is expressed in renal tubular epithelial cells
Pediatr. Nephrol.
25
87-96
2010
Homo sapiens
Manually annotated by BRENDA team
Sauna, Z.E.; Okunji, C.; Hunt, R.C.; Gupta, T.; Allen, C.E.; Plum, E.; Blaisdell, A.; Grigoryan, V.; Geetha, S.; Fathke, R.; Soejima, K.; Kimchi-Sarfaty, C.
Characterization of conformation-sensitive antibodies to ADAMTS13, the von Willebrand cleavage protease
PLoS ONE
4
e6506
2009
Homo sapiens
Manually annotated by BRENDA team
Larkin, D.; de Laat, B.; Jenkins, P.V.; Bunn, J.; Craig, A.G.; Terraube, V.; Preston, R.J.; Donkor, C.; Grau, G.E.; van Mourik, J.A.; ODonnell, J.S.
Severe Plasmodium falciparum malaria is associated with circulating ultra-large von Willebrand multimers and ADAMTS13 inhibition
PLoS Pathog.
5
e1000349
2009
Homo sapiens
Manually annotated by BRENDA team
Akiyama, M.; Takeda, S.; Kokame, K.; Takagi, J.; Miyata, T.
Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor
Proc. Natl. Acad. Sci. USA
106
19274-19279
2009
Homo sapiens
Manually annotated by BRENDA team
Bresin, E.; Gastoldi, S.; Daina, E.; Belotti, D.; Pogliani, E.; Perseghin, P.; Scalzulli, P.R.; Paolini, R.; Marceno, R.; Remuzzi, G.; Galbusera, M.
Rituximab as pre-emptive treatment in patients with thrombotic thrombocytopenic purpura and evidence of anti-ADAMTS13 autoantibodies
Thromb. Haemost.
101
233-238
2009
Homo sapiens
Manually annotated by BRENDA team
Uemura, T.; Kaikita, K.; Yamabe, H.; Soejima, K.; Matsukawa, M.; Fuchigami, S.; Tanaka, Y.; Morihisa, K.; Enomoto, K.; Sumida, H.; Sugiyama, S.; Ogawa, H.
Changes in plasma von Willebrand factor and ADAMTS13 levels associated with left atrial remodeling in atrial fibrillation
Thromb. Res.
124
28-32
2009
Homo sapiens
Manually annotated by BRENDA team
Kobayashi, T.; Wada, H.; Usui, M.; Sakurai, H.; Matsumoto, T.; Nobori, T.; Katayama, N.; Uemoto, S.; Ishizashi, H.; Matsumoto, M.; Fujimura, Y.; Isaji, S.
Decreased ADAMTS13 levels in patients after living donor liver transplantation
Thromb. Res.
124
541-545
2009
Homo sapiens
Manually annotated by BRENDA team
Hyun, J.; Kim, H.K.; Kim, J.E.; Lim, M.G.; Jung, J.S.; Park, S.; Cho, H.I.
Correlation between plasma activity of ADAMTS-13 and coagulopathy, and prognosis in disseminated intravascular coagulation
Thromb. Res.
124
75-79
2009
Homo sapiens
Manually annotated by BRENDA team
Schettert, I.T.; Pereira, A.C.; Lopes, N.H.; Hueb, W.A.; Krieger, J.E.
Association between ADAMTS13 polymorphisms and risk of cardiovascular events in chronic coronary disease
Thromb. Res.
125
61-66
2010
Homo sapiens
Manually annotated by BRENDA team
Taniguchi, S.; Hashiguchi, T.; Ono, T.; Takenouchi, K.; Nakayama, K.; Kawano, T.; Kato, K.; Matsushita, R.; Nagatomo, M.; Nakamura, S.; Nakashima, T.; Maruyama, I.
Association between reduced ADAMTS13 and diabetic nephropathy
Thromb. Res.
125
e310-e316
2010
Homo sapiens
Manually annotated by BRENDA team
George, J.
ADAMTS13: What it does, how it works, and why its important
Transfusion
49
196-198
2009
Homo sapiens
Manually annotated by BRENDA team
Davis, A.K.; Makar, R.S.; Stowell, C.P.; Kuter, D.J.; Dzik, W.H.
ADAMTS13 binds to CD36: a potential mechanism for platelet and endothelial localization of ADAMTS13
Transfusion
49
206-213
2009
Homo sapiens
Manually annotated by BRENDA team
Rossi, F.C.; Angerami, R.N.; de Paula, E.V.; Orsi, F.L.; Shang, D.; del Guercio, V.M.; Resende, M.R.; Annichino-Bizzacchi, J.M.; da Silva, L.J.; Zheng, X.L.; Castro, V.
A novel association of acquired ADAMTS13 inhibitor and acute dengue virus infection
Transfusion
50
208-212
2010
Homo sapiens
Manually annotated by BRENDA team
de Groot, R.; Lane, D.A.; Crawley, J.T.
The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity
Blood
116
3064-3072
2010
Homo sapiens
Manually annotated by BRENDA team
Zhou, M.; Dong, X.; Baldauf, C.; Chen, H.; Zhou, Y.; Springer, T.A.; Luo, X.; Zhong, C.; Graeter, F.; Ding, J.
A novel calcium-binding site of von Willebrand factor A2 domain regulates its cleavage by ADAMTS13
Blood
117
4623-4631
2011
Homo sapiens
Manually annotated by BRENDA team
Crawley, J.T.; de Groot, R.; Xiang, Y.; Luken, B.M.; Lane, D.A.
Unraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor
Blood
118
3212-3221
2011
Homo sapiens
Manually annotated by BRENDA team
Hiura, H.; Matsui, T.; Matsumoto, M.; Hori, Y.; Isonishi, A.; Kato, S.; Iwamoto, T.; Mori, T.; Fujimura, Y.
Proteolytic fragmentation and sugar chains of plasma ADAMTS13 purified by a conformation-dependent monoclonal antibody
J. Biochem.
148
403-411
2010
Homo sapiens
Manually annotated by BRENDA team
Skipwith, C.G.; Cao, W.; Zheng, X.L.
Factor VIII and platelets synergistically accelerate cleavage of von Willebrand factor by ADAMTS13 under fluid shear stress
J. Biol. Chem.
285
28596-28603
2010
Homo sapiens
Manually annotated by BRENDA team
Lenting, P.; Rastegarlari, G.
ADAMTS-13: Double trouble for von Willebrand factor
J. Thromb. Haemost.
8
2775-2777
2010
Homo sapiens
Manually annotated by BRENDA team
Yeh, H.C.; Zhou, Z.; Choi, H.; Tekeoglu, S.; May, W.; Wang, C.; Turner, N.; Scheiflinger, F.; Moake, J.L.; Dong, J.F.
Disulfide bond reduction of von Willebrand factor by ADAMTS-13
J. Thromb. Haemost.
8
2778-2788
2010
Homo sapiens
Manually annotated by BRENDA team
Veyradier, A.; Coppo, P.
ADAMTS13, von Willebrand factor specific cleaving protease
Med. Sci. (Paris)
27
1097-1105
2011
Homo sapiens
Manually annotated by BRENDA team
Zhang, J.; Ma, Z.; Dong, N.; Liu, F.; Su, J.; Zhao, Y.; Shen, F.; Wang, A.; Ruan, C.
A conformation-sensitive monoclonal antibody against the A2 domain of von Willebrand factor reduces its proteolysis by ADAMTS13
PLoS ONE
6
e22157
2011
Homo sapiens
Manually annotated by BRENDA team
Bao, J.; Xiao, J.; Mao, Y.; Zheng, X.L.
Carboxyl terminus of ADAMTS13 directly inhibits platelet aggregation and ultra large von Willebrand factor string formation under flow in a free-thiol-dependent manner
Arterioscler. Thromb. Vasc. Biol.
34
397-407
2014
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Hershko, K.; Simhadri, V.L.; Blaisdell, A.; Hunt, R.C.; Newell, J.; Tseng, S.C.; Hershko, A.Y.; Choi, J.W.; Sauna, Z.E.; Wu, A.; Bram, R.J.; Komar, A.A.; Kimchi-Sarfaty, C.
Cyclosporin A impairs the secretion and activity of ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 repeat)
J. Biol. Chem.
287
44361-44371
2012
Mus musculus (Q769J6), Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Chen, J.; Ling, M.; Lopez, J.A.; Chung, D.W.; Fu, X.
Hypochlorous acid generated by neutrophils inactivates ADAMTS13: an oxidative mechanism for regulating ADAMTS13 proteolytic activity during inflammation
J. Biol. Chem.
290
1422-1431
2015
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
De Cock, E.; Hermans, C.; De Raeymaecker, J.; De Ceunynck, K.; De Maeyer, B.; Vandeputte, N.; Vandenbulcke, A.; Deckmyn, H.; Rottensteiner, H.; De Maeyer, M.; De Meyer, S.F.; Vanhoorelbeke, K.
The novel ADAMTS13-p.D187H mutation impairs ADAMTS13 activity and secretion and contributes to thrombotic thrombocytopenic purpura in mice
J. Thromb. Haemost.
13
283-292
2015
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Desch, K.C.; Kretz, C.; Yee, A.; Gildersleeve, R.; Metzger, K.; Agrawal, N.; Cheng, J.; Ginsburg, D.
Probing ADAMTS13 substrate specificity using phage display
PLoS ONE
10
e0122931
2015
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Gogia, S.; Lo, C.Y.; Neelamegham, S.
Detection of plasma protease activity using microsphere-cytometry assays with E. coli derived substrates: VWF proteolysis by ADAMTS13
PLoS ONE
10
e0126556
2015
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
South, K.; Luken, B.M.; Crawley, J.T.; Phillips, R.; Thomas, M.; Collins, R.F.; Deforche, L.; Vanhoorelbeke, K.; Lane, D.A.
Conformational activation of ADAMTS13
Proc. Natl. Acad. Sci. USA
111
18578-18583
2014
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Muia, J.; Zhu, J.; Gupta, G.; Haberichter, S.L.; Friedman, K.D.; Feys, H.B.; Deforche, L.; Vanhoorelbeke, K.; Westfield, L.A.; Roth, R.; Tolia, N.H.; Heuser, J.E.; Sadler, J.E.
Allosteric activation of ADAMTS13 by von Willebrand factor
Proc. Natl. Acad. Sci. USA
111
18584-18589
2014
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Ling, J.; Ma, Z.; Liu, L.; Yin, J.; Su, J.; Shen, F.; Xie, L.; Hu, S.
Identification of a crucial tryptophan residue in ADAMTS13 required for its secretion and enzymatic activity
Clin. Exp. Pharmacol. Physiol.
45
1181-1186
2018
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Garland, K.S.; Reitsma, S.E.; Shirai, T.; Zilberman-Rudenko, J.; Tucker, E.I.; Gailani, D.; Gruber, A.; McCarty, O.J.T.; Puy, C.
Removal of the C-terminal domains of ADAMTS13 by activated coagulation factor XI induces platelet adhesion on endothelial cells under flow conditions
Front. Med.
4
232
2017
Homo sapiens (Q76LX8)
Manually annotated by BRENDA team
Graham, S.M.; Chen, J.; Le, J.; Ling, M.; Chung, D.W.; Liles, W.C.; Lopez, J.A.
Von Willebrand factor adhesive activity and ADAMTS13 protease activity in HIV-1-infected men
Int. J. Med. Sci.
16
276-284
2019
Homo sapiens
Manually annotated by BRENDA team
South, K.; Freitas, M.O.; Lane, D.A.
A model for the conformational activation of the structurally quiescent metalloprotease ADAMTS13 by von Willebrand factor
J. Biol. Chem.
292
5760-5769
2017
Homo sapiens
Manually annotated by BRENDA team
Rottensteiner, H.; Kaufmann, S.; Rathgeb, A.; Kink, B.; Plaimauer, B.; Matthiessen, P.; Hann, S.; Scheiflinger, F.
Temperature-dependent irreversible conformational change of recombinant ADAMTS13 upon metal ion chelation
J. Thromb. Haemost.
17
995-1002
2019
Homo sapiens
Manually annotated by BRENDA team
Guo, R.; Xie, Y.; Yang, J.; Lu, H.; Ye, P.; Jin, L.; Lin, W.
Increasing plasma ADAMTS13 activity is associated with HBeAg seroconversion in chronic hepatitis B patients during 5 years of entecavir treatment
Sci. Rep.
9
5916
2019
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Kumar, M.; Cao, W.; McDaniel, J.K.; Pham, H.P.; Raju, D.; Nawalinski, K.; Frangos, S.; Kung, D.; Zager, E.; Kasner, S.E.; Levine, J.M.; Zheng, X.L.
Plasma ADAMTS13 activity and von Willebrand factor antigen and activity in patients with subarachnoid haemorrhage
Thromb. Haemost.
117
691-699
2017
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Clark, C.C.; Mebius, M.M.; de Maat, S.; Tielens, A.G.M.; de Groot, P.G.; Urbanus, R.T.; Fijnheer, R.; Hazenberg, B.P.C.; van Hellemond, J.J.; Maas, C.
Truncation of ADAMTS13 by plasmin enhances its activity in plasma
Thromb. Haemost.
118
471-479
2018
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Hassenpflug, W.A.; Obser, T.; Bode, J.; Oyen, F.; Budde, U.; Schneppenheim, S.; Schneppenheim, R.; Brehm, M.A.
Genetic and Functional Characterization of ADAMTS13 variants in a patient cohort with Upshaw-Schulman syndrome investigated in Germany
Thromb. Haemost.
118
709-722
2018
Homo sapiens
Manually annotated by BRENDA team
Connell, N.T.; Cheves, T.; Sweeney, J.D.
Effect of ADAMTS13 activity turnaround time on plasma utilization for suspected thrombotic thrombocytopenic purpura
Transfusion
56
354-359
2016
Homo sapiens (Q76LX8), Homo sapiens
Manually annotated by BRENDA team
Nixon, C.; Guertin, C.; Sweeney, J.
Falsely low ADAMTS13 activity caused by levofloxacin
Transfusion
59
2752-2753
2019
Homo sapiens
Manually annotated by BRENDA team