Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura (Q24291691)

thrombotic thrombocytopenic purpura

GOA release 2020-03-11

thrombocytopenia

1 reference

based on heuristic

inferred from title

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5

J E Sadler

J E

Sadler

1 reference

30 October 2023

X Zheng

1

X

Zheng

1 reference

30 October 2023

D Chung

2

D

Chung

1 reference

30 October 2023

T K Takayama

3

T K

Takayama

1 reference

30 October 2023

E M Majerus

4

E M

Majerus

1 reference

30 October 2023

K Fujikawa

6

K

Fujikawa

1 reference

Journal of Biological Chemistry

30 October 2023

language of work or name

English

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publication date

2 November 2001

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published in

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volume

276

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issue

44

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page(s)

41059-63

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cites work

THROMBOTIC THROMBOCYTOPENIC PURPURA

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Unusually large plasma factor VIII:von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura

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von Willebrand factor-cleaving protease in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome

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Antibodies to von Willebrand factor-cleaving protease in acute thrombotic thrombocytopenic purpura

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Partial amino acid sequence of purified von Willebrand factor-cleaving protease

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Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family

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ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases. General features and genomic distribution of the ADAM-TS family

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The new kids on the block: ADAMTSs, potentially multifunctional metalloproteinases of the ADAM family

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ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats

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The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

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C-mannosylation and O-fucosylation of the thrombospondin type 1 module

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Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis

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Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites

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The thrombospondin motif of aggrecanase-1 (ADAMTS-4) is critical for aggrecan substrate recognition and cleavage

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Versican V1 proteolysis in human aorta in vivo occurs at the Glu441-Ala442 bond, a site that is cleaved by recombinant ADAMTS-1 and ADAMTS-4

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Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family

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ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan

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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family

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Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation

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ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix

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Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins

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Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats

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ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region

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Interaction of recombinant procollagen and properdin modules of thrombospondin-1 with heparin and fibrinogen/fibrin

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Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling

21 January 2018

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Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.C100515200

0 references

Fatcat ID

release_onhlbe7ahnfs3oprohhyvjqlne

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