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Conformational activation of ADAMTS13

Proceedings of the National Academy of Sciences of the United States of America, 2014
Kieron South   +2 more
exaly  

Improvement of recombinant ADAMTS13 production through a more optimal signal peptide or an N‐terminal fusion protein

open access: yesJournal of Thrombosis and Haemostasis, 2022
Recombinant human ADAMTS13 (rADAMTS13) is a key protein in fundamental research for investigating its mode of action and the pathophysiology of thrombotic thrombocytopenic purpura (TTP). However, the expression of rADAMTS13 is quite low in mammalian cells, which makes the production of the protein time-consuming and labor-intensive.We aimed at ...
Kadri Kangro   +2 more
exaly   +4 more sources

Decreased protein C activity, lower ADAMTS13 antigen and free protein S levels accompanied by unchanged thrombin generation potential in hospitalized COVID-19 patients

open access: yesThrombosis Research, 2023
COVID-19 is associated with an increased thromboembolic risk. However, the mechanisms triggering clot formation in those patients remain unknown.In 118 adult Caucasian severe but non-critically ill COVID-19 patients (median age 58 years; 73 % men) and 46 controls, we analyzed in vitro plasma thrombin generation profile (calibrated automated thrombogram
Tomasz Stachura, Krzysztof Sładek
exaly   +4 more sources

Local Elongation of Endothelial Cell-anchored von Willebrand Factor Strings Precedes ADAMTS13 Protein-mediated Proteolysis [PDF]

open access: yesJournal of Biological Chemistry, 2011
Platelet-decorated von Willebrand factor (VWF) strings anchored to the endothelial surface are rapidly cleaved by ADAMTS13. Individual VWF string characteristics such as number, location, and auxiliary features of the ADAMTS13 cleavage sites were explored here using imaging and computing software.
Susana Rocha   +2 more
exaly   +4 more sources

Generation and validation of small ADAMTS13 fragments for epitope mapping of anti‐ADAMTS13 autoantibodies in immune‐mediated thrombotic thrombocytopenic purpura

open access: yesResearch and Practice in Thrombosis and Haemostasis, 2020
Background In immune‐mediated thrombotic thrombocytopenic purpura (iTTP), patients develop an immune response against the multidomain enzyme ADAMTS13.
Kadri Kangro   +8 more
doaj   +2 more sources

Plasma von Willebrand Factor and ADAMTS13 Interact With APOE‐ε4 in Predicting Longitudinal Brain Atrophy and Cognitive Decline Over a 9‐Year Follow‐Up [PDF]

open access: yesJournal of the American Heart Association: Cardiovascular and Cerebrovascular Disease
Background Von Willebrand factor (VWF) and ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin type 1 motif, 13) are linked to dementia risk, and limited evidence suggests apolipoprotein E (APOE)‐ε4 alters VWF release.
Hailey A. Adegboye   +22 more
doaj   +2 more sources

Rat models of thrombotic thrombocytopenic purpura reveal crucial role of placental ADAMTS13 in perinatal survival [PDF]

open access: yesBlood Advances
: Thrombotic thrombocytopenic purpura (TTP), a life-threatening thrombotic microangiopathy, is caused by severe deficiency of plasma ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 repeats, 13) activity.
Quan Zhang   +6 more
doaj   +2 more sources

An IAP retrotransposon in the mouse ADAMTS13 gene creates ADAMTS13 variant proteins that are less effective in cleaving von Willebrand factor multimers

open access: yesBlood, 2007
AbstractSevere deficiency of ADAMTS13, a von Willebrand factor (VWF)–cleaving metalloprotease, causes thrombotic thrombocytopenic purpura. When analyzed with VWF multimers, but not with an abbreviated VWF peptide (VWF73) as the substrate, the plasma ADAMTS13 activity levels of mouse strains segregated into a high and a low group that differed by ...
Eric E Bouhassira   +2 more
exaly   +4 more sources

Optimization of plasma-based BioID identifies plasminogen as a ligand of ADAMTS13

open access: yesScientific Reports
ADAMTS13, a disintegrin and metalloprotease with a thrombospondin type 1 motif, member 13, regulates the length of Von Willebrand factor (VWF) multimers and their platelet-binding activity. ADAMTS13 is constitutively secreted as an active protease and is
Hasam Madarati   +10 more
doaj   +2 more sources

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