Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Gain- and loss-of-function mutants confirm the importance of apical residues to the primary interaction of human glycoprotein VI with collagen.

Journal of thrombosis and haemostasis : JTH - 1 Apr 2006

O'Connor M N, Smethurst P A, Farndale R W, Ouwehand W H

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Collagen
Share to Epitope Mapping

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunoglobulins

Share to Mutagenesis, Site-Directed

Share to Peptides

Share to Platelet Membrane Glycoproteins

Share to Protein Structure, Secondary

Share to Recombinant Proteins

Source

Identifiers

PMID: 16405521
DOI: 10.1111/j.1538-7836.2005.01764.x

Genes

CRP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Gain- and loss-of-function mutants confirm the importance of apical residues to the primary interaction of human glycoprotein VI with collagen.PMID 16405521Read ↗

Identification of the primary collagen-binding surface on human glycoprotein VI by site-directed mutagenesis and by a blocking phage antibodySemantic proximity Read ↗

Selective blockade of glycoprotein VI clustering on collagen helices.Semantic proximity Read ↗

Chimeric Fc receptors identify ligand binding regions in human glycoprotein VI.Semantic proximity Read ↗

Fc Rgamma -independent signaling by the platelet collagen receptor glycoprotein VI.Semantic proximity Read ↗

Consequences of Glycine Mutations in the Fibronectin-binding Sequence of Collagen.Semantic proximity Read ↗

Delineation of the region in the glycoprotein VI tail required for association with the Fc receptor gamma-chain.Semantic proximity Read ↗

An activating mutation reveals a second binding mode of the integrin α2 I domain to the GFOGER motif in collagens.Semantic proximity Read ↗

Computer prediction of paratope on antithrombotic antibody 10B12 and epitope on platelet glycoprotein VI via molecular dynamics simulation.Semantic proximity Read ↗

The basic residue cluster (55)KKWVR(59) in CCL5 is required for in vivo biologic function.Semantic proximity Read ↗

The distal hinge of the reactive site loop and its proximity: a target to modulate plasminogen activator inhibitor-1 activity.Semantic proximity Read ↗

Mapping the collagen-binding site in the I domain of the glycoprotein Ia/IIa (integrin alpha(2)beta(1)).Semantic proximity Read ↗

Structure of collagen receptor integrin α(1)I domain carrying the activating mutation E317A.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.