The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens.
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Discoidin domain receptors promote α1β1- and α2β1-integrin mediated cell adhesion to collagen by enhancing integrin activationCrystallographic insight into collagen recognition by discoidin domain receptor 2Evolution of collagensCollagen binding specificity of the discoidin domain receptors: binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1Structural basis of the collagen-binding mode of discoidin domain receptor 2Collagen XXIII, novel ligand for integrin alpha2beta1 in the epidermisLaminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chainsCandidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebratesRole of integrins in the periodontal ligament: organizers and facilitatorsStructural basis of sequence-specific collagen recognition by SPARCImplications for collagen I chain registry from the structure of the collagen von Willebrand factor A3 domain complexThe Structure of Integrin 1I Domain in Complex with a Collagen-mimetic PeptideStructural basis of type VI collagen dimer formation.Collagen: a network for regenerative medicineFertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilizationMammalian collagen IVType XXIII collagen, a new transmembrane collagen identified in metastatic tumor cellsNanotechnology in the regulation of stem cell behaviorEvaluation of cell binding to collagen and gelatin: a study of the effect of 2D and 3D architecture and surface chemistryWhat we don't know about the structure of ryanodine receptor calcium release channels.Revealing early steps of alpha2beta1 integrin-mediated adhesion to collagen type I by using single-cell force spectroscopy.Synergism between platelet collagen receptors defined using receptor-specific collagen-mimetic peptide substrata in flowing blood.A role for adhesion and degranulation-promoting adapter protein in collagen-induced platelet activation mediated via integrin α(2) β(1)Melanoma cell CD44 interaction with the alpha 1(IV)1263-1277 region from basement membrane collagen is modulated by ligand glycosylation.Nanomaterials design and tests for neural tissue engineering.Complete primary structure of rainbow trout type I collagen consisting of alpha1(I)alpha2(I)alpha3(I) heterotrimers.Designer self-assembling peptide nanofiber scaffolds for adult mouse neural stem cell 3-dimensional cultures.First analysis of a bacterial collagen-binding protein with collagen Toolkits: promiscuous binding of YadA to collagens may explain how YadA interferes with host processesMolecular mechanism of alpha2beta1 integrin interaction with human echovirus 1.Coating of biomaterial scaffolds with the collagen-mimetic peptide GFOGER for bone defect repairBone regeneration using an alpha 2 beta 1 integrin-specific hydrogel as a BMP-2 delivery vehicle.Exploiting bacterial peptide display technology to engineer biomaterials for neural stem cell culturePorphyromonas gingivalis GroEL induces osteoclastogenesis of periodontal ligament cells and enhances alveolar bone resorption in rats.Glycosylation modulates melanoma cell α2β1 and α3β1 integrin interactions with type IV collagenBioactive coatings for orthopaedic implants-recent trends in development of implant coatings.Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen.Comparative evaluation of the biological properties of fibrin for bone regeneration.The fibril-associated collagen IX provides a novel mechanism for cell adhesion to cartilaginous matrix.Measurement of the Interaction Between Recombinant I-domain from Integrin alpha 2 beta 1 and a Triple Helical Collagen Peptide with the GFOGER Binding Motif Using Molecular Force SpectroscopyEndothelial cell response to chemical, biological, and physical cues in bioactive hydrogels.
P2860
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P2860
The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens.
description
2000 nî lūn-bûn
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name
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@en
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@nl
type
label
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@en
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@nl
prefLabel
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@en
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@nl
P2093
P356
P1476
The collagen-binding A-domains ...... ve (triple-helical) collagens.
@en
P2093
Farndale RW
Peachey AR
Tuckwell DS
P356
10.1074/JBC.275.1.35
P407
P577
2000-01-01T00:00:00Z