N-linked glycosylation of VWF modulates its interaction with ADAMTS13 (original) (raw)

N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity

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A Conformation-Sensitive Monoclonal Antibody against the A2 Domain of von Willebrand Factor Reduces Its Proteolysis by ADAMTS13

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Structure–function and regulation of ADAMTS‐13 protease

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Altered Proteolytic Activities of ADAMTS-4 Expressed by C-terminal Processing

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Thrombospondin1 and ADAMTS13 competitively bind to VWF A2 and A3 domains in vitro

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An autoantibody epitope comprising residues R660, Y661, and Y665 in the ADAMTS13 spacer domain identifies a binding site for the A2 domain of VWF

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Leukocyte proteases cleave von Willebrand factor at or near the ADAMTS13 cleavage site

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ADAMTS4 Cleaves at the Aggrecanase Site (Glu373-Ala374) and Secondarily at the Matrix Metalloproteinase Site (Asn341-Phe342) in the Aggrecan Interglobular Domain

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ADAMTS-4 activity on a proteoglycan vs. a polypeptide is controlled by the ancillary domains

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Endolysosomal N-glycan processing is critical to attain the most active form of the enzyme acid alpha-glucosidase

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VWF73, a region from D1596 to R1668 of von Willebrand factor, provides a minimal substrate for ADAMTS-13

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Glycan structure and site of glycosylation in the ER-resident glycoprotein, uridine 5'-diphosphate-glucose: glycoprotein glucosyltransferases 1 from rat, porcine, bovine, and human

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The distal carboxyterminal domains of murine ADAMTS13 influence proteolysis of platelet-decorated VWF strings in vivo

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Carboxyl Terminus of ADAMTS13 Directly Inhibits Platelet Aggregation and Ultra Large von Willebrand Factor String Formation Under Flow in a Free-Thiol–Dependent Manner

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Modifications of the Glycosaminoglycan-Linkage Region of Proteoglycans: Phosphorylation and Sulfation Determine the Activity of the Human ß1,4-Galactosyltransferase 7 and ß1,3-Glucuronosyltransferase I

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