FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2093722104> ?p ?o ?g. }

• W2093722104 endingPage "873" @default.
• W2093722104 startingPage "869" @default.
• W2093722104 abstract "SummaryBackground: By site‐directed mutagenesis of recombinant receptor fragments, we have previously identified residue lysine59 of the platelet collagen receptor glycoprotein VI (GPVI) as being critical for its interaction with the synthetic ligand collagen‐related peptide (CRP) and the inhibitory phage antibody 10B12. Lysine59 is proposed to lie on the apical surface of the receptor near the linker joining the two immunoglobulin (Ig)‐like extracellular domains. Recently, others have postulated the involvement of a portion of the first domain distant from the interdomain hinge as being involved in an extended collagen‐binding site. Aim and Methods: To extend our knowledge of the primary collagen‐binding site of GPVI, a number of neighboring residues on the apical surface of recombinant soluble GPVI were mutated to alanine and binding of these mutants, as well as the lysine59 mutant, to fibrillar collagen was measured. Results: Binding of recombinant GPVI to collagen, like CRP, was dramatically reduced by the mutation of residue lysine59 to glutamate. Remarkably, the mutation of residues arginine60 in domain one and arginine166 in domain two, individually to alanine, which had no significant affect on CRP binding, reduced binding of recombinant GPVI to collagen. Mutation of the residue lysine41 to alanine dramatically increased binding to both CRP and collagen. This mutation abolished 10B12 binding, confirming its position in the epitope of our inhibitory phage antibody. Conclusions: Residues lysine59, arginine60, and arginine166, from both Ig‐like domains of GPVI, are critical for collagen binding by the receptor. This provides additional evidence for a basic patch on the apical surface of the receptor as the primary collagen‐binding site of GPVI. Background: By site‐directed mutagenesis of recombinant receptor fragments, we have previously identified residue lysine59 of the platelet collagen receptor glycoprotein VI (GPVI) as being critical for its interaction with the synthetic ligand collagen‐related peptide (CRP) and the inhibitory phage antibody 10B12. Lysine59 is proposed to lie on the apical surface of the receptor near the linker joining the two immunoglobulin (Ig)‐like extracellular domains. Recently, others have postulated the involvement of a portion of the first domain distant from the interdomain hinge as being involved in an extended collagen‐binding site. Aim and Methods: To extend our knowledge of the primary collagen‐binding site of GPVI, a number of neighboring residues on the apical surface of recombinant soluble GPVI were mutated to alanine and binding of these mutants, as well as the lysine59 mutant, to fibrillar collagen was measured. Results: Binding of recombinant GPVI to collagen, like CRP, was dramatically reduced by the mutation of residue lysine59 to glutamate. Remarkably, the mutation of residues arginine60 in domain one and arginine166 in domain two, individually to alanine, which had no significant affect on CRP binding, reduced binding of recombinant GPVI to collagen. Mutation of the residue lysine41 to alanine dramatically increased binding to both CRP and collagen. This mutation abolished 10B12 binding, confirming its position in the epitope of our inhibitory phage antibody. Conclusions: Residues lysine59, arginine60, and arginine166, from both Ig‐like domains of GPVI, are critical for collagen binding by the receptor. This provides additional evidence for a basic patch on the apical surface of the receptor as the primary collagen‐binding site of GPVI." @default.
• W2093722104 created "2016-06-24" @default.
• W2093722104 creator A5003324626 @default.
• W2093722104 creator A5014699562 @default.
• W2093722104 creator A5043887900 @default.
• W2093722104 creator A5074848089 @default.
• W2093722104 date "2006-04-01" @default.
• W2093722104 modified "2023-10-16" @default.
• W2093722104 title "Gain‐ and loss‐of‐function mutants confirm the importance of apical residues to the primary interaction of human glycoprotein VI with collagen" @default.
• W2093722104 cites W1604870150 @default.
• W2093722104 cites W1966495991 @default.
• W2093722104 cites W1990451715 @default.
• W2093722104 cites W1996003806 @default.
• W2093722104 cites W2027330791 @default.
• W2093722104 cites W2053159146 @default.
• W2093722104 cites W2053521976 @default.
• W2093722104 cites W2116621437 @default.
• W2093722104 cites W2199497140 @default.
• W2093722104 cites W4256475235 @default.
• W2093722104 cites W4321429627 @default.
• W2093722104 doi "https://doi.org/10.1111/j.1538-7836.2005.01764.x" @default.
• W2093722104 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16405521" @default.
• W2093722104 hasPublicationYear "2006" @default.
• W2093722104 type Work @default.
• W2093722104 sameAs 2093722104 @default.
• W2093722104 citedByCount "36" @default.
• W2093722104 countsByYear W20937221042012 @default.
• W2093722104 countsByYear W20937221042014 @default.
• W2093722104 countsByYear W20937221042015 @default.
• W2093722104 countsByYear W20937221042016 @default.
• W2093722104 countsByYear W20937221042017 @default.
• W2093722104 countsByYear W20937221042019 @default.
• W2093722104 countsByYear W20937221042020 @default.
• W2093722104 countsByYear W20937221042021 @default.
• W2093722104 countsByYear W20937221042022 @default.
• W2093722104 countsByYear W20937221042023 @default.
• W2093722104 crossrefType "journal-article" @default.
• W2093722104 hasAuthorship W2093722104A5003324626 @default.
• W2093722104 hasAuthorship W2093722104A5014699562 @default.
• W2093722104 hasAuthorship W2093722104A5043887900 @default.
• W2093722104 hasAuthorship W2093722104A5074848089 @default.
• W2093722104 hasBestOaLocation W20937221041 @default.
• W2093722104 hasConcept C104317684 @default.
• W2093722104 hasConcept C107824862 @default.
• W2093722104 hasConcept C108625454 @default.
• W2093722104 hasConcept C119524353 @default.
• W2093722104 hasConcept C125823703 @default.
• W2093722104 hasConcept C143065580 @default.
• W2093722104 hasConcept C153911025 @default.
• W2093722104 hasConcept C159654299 @default.
• W2093722104 hasConcept C16318435 @default.
• W2093722104 hasConcept C170493617 @default.
• W2093722104 hasConcept C185592680 @default.
• W2093722104 hasConcept C195616568 @default.
• W2093722104 hasConcept C195687474 @default.
• W2093722104 hasConcept C203014093 @default.
• W2093722104 hasConcept C26828662 @default.
• W2093722104 hasConcept C2779856020 @default.
• W2093722104 hasConcept C2780227090 @default.
• W2093722104 hasConcept C2780573682 @default.
• W2093722104 hasConcept C40767141 @default.
• W2093722104 hasConcept C515207424 @default.
• W2093722104 hasConcept C55493867 @default.
• W2093722104 hasConcept C86803240 @default.
• W2093722104 hasConceptScore W2093722104C104317684 @default.
• W2093722104 hasConceptScore W2093722104C107824862 @default.
• W2093722104 hasConceptScore W2093722104C108625454 @default.
• W2093722104 hasConceptScore W2093722104C119524353 @default.
• W2093722104 hasConceptScore W2093722104C125823703 @default.
• W2093722104 hasConceptScore W2093722104C143065580 @default.
• W2093722104 hasConceptScore W2093722104C153911025 @default.
• W2093722104 hasConceptScore W2093722104C159654299 @default.
• W2093722104 hasConceptScore W2093722104C16318435 @default.
• W2093722104 hasConceptScore W2093722104C170493617 @default.
• W2093722104 hasConceptScore W2093722104C185592680 @default.
• W2093722104 hasConceptScore W2093722104C195616568 @default.
• W2093722104 hasConceptScore W2093722104C195687474 @default.
• W2093722104 hasConceptScore W2093722104C203014093 @default.
• W2093722104 hasConceptScore W2093722104C26828662 @default.
• W2093722104 hasConceptScore W2093722104C2779856020 @default.
• W2093722104 hasConceptScore W2093722104C2780227090 @default.
• W2093722104 hasConceptScore W2093722104C2780573682 @default.
• W2093722104 hasConceptScore W2093722104C40767141 @default.
• W2093722104 hasConceptScore W2093722104C515207424 @default.
• W2093722104 hasConceptScore W2093722104C55493867 @default.
• W2093722104 hasConceptScore W2093722104C86803240 @default.
• W2093722104 hasIssue "4" @default.
• W2093722104 hasLocation W20937221041 @default.
• W2093722104 hasLocation W20937221042 @default.
• W2093722104 hasOpenAccess W2093722104 @default.
• W2093722104 hasPrimaryLocation W20937221041 @default.
• W2093722104 hasRelatedWork W1975310897 @default.
• W2093722104 hasRelatedWork W1982359421 @default.
• W2093722104 hasRelatedWork W2002183278 @default.
• W2093722104 hasRelatedWork W2012727169 @default.
• W2093722104 hasRelatedWork W2058959137 @default.
• W2093722104 hasRelatedWork W2073379847 @default.
• W2093722104 hasRelatedWork W2082874149 @default.

• next