About: Amino acid sequence of human von Willebrand factor

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rdf:type	Item
description	artículu científicu espublizáu en 1986 (ast) vědecký článek publikovaný v roce 1986 (cs) 1986 թուականի Յունիսին հրատարակուած գիտական յօդուած (hyw) наукова стаття, опублікована в червні 1986 (uk) 1986 թվականի հունիսին հրատարակված գիտական հոդված (hy) article scientifique publié en 1986 (fr) scientific journal article (en) wetenschappelijk artikel (gepubliceerd op 1986/06/03) (nl) vedecký článok (publikovaný 1986/06/03) (sk) im Juni 1986 veröffentlicher wissenschaftlicher Artikel (de) مقالة علمية (نشرت في 3-6-1986) (ar)
publication date	wds:Q28630812-FE8A3587-BEB3-4ECC-9D3F-B2CCE5E0DF75
publication date	1986-06-03 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28630812-791DE9ED-2993-4BA4-B272-047267E4279E
language of work or name	English
author name string	wds:Q28630812-13DB7918-1854-4861-8BD6-464A40783D3A wds:Q28630812-1F876055-A778-4CAF-9A81-4EDA34ADFA90 wds:Q28630812-4B728AD6-ADCF-4921-9598-12885935932C wds:Q28630812-6A1FC12D-5783-40FB-819A-138AEE48909C wds:Q28630812-767EA2F4-37FF-40D9-8613-832E3A933411 wds:Q28630812-7F0ECE79-D4CC-4024-9FE1-27A5EA4B5212 wds:Q28630812-A698DBA5-08BA-4F1A-AA0E-D1591378BF7B wds:Q28630812-AF85B0EF-BF1F-43D4-9E43-BB1D405C3562 wds:Q28630812-E574712F-4A6C-4208-9276-7DD390F4E408 wds:Q28630812-F08E7A12-7BF2-4E22-A02F-D4C94A6CE964
OpenCitations bibliographic resource ID	wds:Q28630812-6E468652-171E-4795-AE2B-733DEB8E25CA
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3754456
author name string	S. Kumar K. Fujikawa K. Takio K. Titani J. E. Sadler K. A. Walsh K. Ashida L. H. Ericsson M. W. Chopek R. D. Wade
OpenCitations bibliographic resource ID	3754456
rdfs:label	Amino acid sequence of human von Willebrand factor (en) Amino acid sequence of human von Willebrand factor (nl) Amino acid sequence of human von Willebrand factor (ast)
skos:prefLabel	Amino acid sequence of human von Willebrand factor (en) Amino acid sequence of human von Willebrand factor (nl) Amino acid sequence of human von Willebrand factor (ast)
name	Amino acid sequence of human von Willebrand factor (en) Amino acid sequence of human von Willebrand factor (nl) Amino acid sequence of human von Willebrand factor (ast)
title	wds:Q28630812-7CF468F8-CD19-40AA-8923-4EE51106592D
title	Amino acid sequence of human von Willebrand factor (en)
page(s)	wds:Q28630812-98E17AB4-3961-4A49-BBEA-281E3D69A756
page(s)	3171–3184
instance of	wds:Q28630812-549180F8-AC60-4EFB-8D43-175B733C00AF
instance of	scholarly article
PubMed ID	wds:Q28630812-345FA2AD-D74E-4F03-AF2A-A943BF46ED85
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3524673
PubMed ID	3524673
published in	wds:Q28630812-1FEB3525-262B-4EEF-B4D8-8606A36EADEA
published in	Biochemistry
issue	wds:Q28630812-7EC6C7BF-7B6D-4358-89F2-6B0E5E5F887D
volume	wds:Q28630812-AA931ED9-C17A-4C9D-9BDF-905C7E9F57E5
issue	11
volume	25
DOI	wds:Q28630812-2C02119B-2106-42B7-80C6-548E52A5F5E1
DOI	http://dx.doi.org/10.1021/BI00359A015
DOI	10.1021/BI00359A015
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28630812
is cites work of	Characterization of the unique mechanism mediating the shear-dependent binding of soluble von Willebrand factor to platelets Invertebrate vitellogenin is homologous to human von Willebrand factor N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin Heterogeneity of plasma von Willebrand factor multimers resulting from proteolysis of the constituent subunit Molecular biology of von Willebrand factor Two Cys residues essential for von Willebrand factor multimer assembly in the Golgi A pH-regulated dimeric bouquet in the structure of von Willebrand factor Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab Composition of the von Willebrand factor storage organelle (Weibel-Palade body) isolated from cultured human umbilical vein endothelial cells Domains involved in multimer assembly of von willebrand factor (vWF): multimerization is independent of dimerization. An evolving view of the eukaryotic oligosaccharyltransferase Functional mapping of SPARC: peptides from two distinct Ca+(+)-binding sites modulate cell shape Binding of platelet glycoprotein Ibalpha to von Willebrand factor domain A1 stimulates the cleavage of the adjacent domain A2 by ADAMTS13. Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family Von Willebrand factor-cleaving protease and Upshaw-Schulman syndrome Identification of a cleavage site directing the immunochemical detection of molecular abnormalities in type IIA von Willebrand factor The influence of flanking sequences on O-glycosylation. Molecular mechanisms of platelet adhesion and activation The C-type lectin receptor CLEC4M binds, internalizes, and clears von Willebrand factor and contributes to the variation in plasma von Willebrand factor levels Activation-independent platelet adhesion and aggregation under elevated shear stress Extensive contacts between ADAMTS13 exosites and von Willebrand factor domain A2 contribute to substrate specificity Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites Identification of the half-cystine residues in porcine submaxillary mucin critical for multimerization through the D-domains. Roles of the CGLCG motif in the D1- and D3-domains Optimization of a recombinant von Willebrand factor fragment as an antagonist of the platelet glycoprotein Ib receptor cDNA sequence for the alpha M subunit of the human neutrophil adherence receptor indicates homology to integrin alpha subunits Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids Norrie disease is caused by mutations in an extracellular protein resembling C-terminal globular domain of mucins Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type VI collagen reveals internal triplication of globular domains similar to the A domains of von Willebrand factor and two alpha 2(VI) chain variants that differ in the carboxy termi Mosaic structure of globular domains in the human type VI collagen alpha 3 chain: similarity to von Willebrand factor, fibronectin, actin, salivary proteins and aprotinin type protease inhibitors New gene, nel, encoding a M(r) 93 K protein with EGF-like repeats is strongly expressed in neural tissues of early stage chick embryos In vivo analysis of the role of O-glycosylations of von Willebrand factor.

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