About: The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy

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scientific article published in Journal of Biological Chemistry

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rdf:type	Item
description	artículu científicu (ast) wetenschappelijk artikel (nl) наукова стаття, опублікована в серпні 1996 (uk) article publié dans la revue scientifique Journal of Biological Chemistry (fr) im August 1996 veröffentlichter wissenschaftlicher Artikel (de) scientific article published in Journal of Biological Chemistry (en)
publication date	wds:Q58058153-81FD427D-1E68-4539-828C-37635C1C7BD4
publication date	1996-08-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q58058153-AB8BED3A-4004-4C97-B4F4-90FE75650081
language of work or name	English
cites work	wds:Q58058153-01366D90-BEF3-4717-8A5F-CD54BB1F317C wds:Q58058153-18EF5FFD-561C-40A5-9FAE-56DA8AEFA5FD wds:Q58058153-2BD7549C-6395-43C0-B416-96701536479C wds:Q58058153-2CD08841-AEF8-41F3-93B3-7A3EBAF45BDB wds:Q58058153-337346A9-E400-427B-8A81-08DF9361848C wds:Q58058153-3C99A7C3-A048-4B5D-A3D1-84C4AF8F4C8D wds:Q58058153-4C450387-8445-4619-8B79-37D3FCAE6F31 wds:Q58058153-519B19FE-A8C5-49D9-ABE9-66D7B76C5965 wds:Q58058153-577EDFD5-5AE2-443C-B55D-DC019CB40A0A wds:Q58058153-5C5F6DF0-C2E1-461D-B191-FCD2D0C78608 wds:Q58058153-729E6823-216E-473C-B464-7D9C292771FE wds:Q58058153-78A66CD8-541D-4A64-BEE1-8122CF8B4008 wds:Q58058153-7928D98E-112B-4D4D-8FE3-D16C882C5D00 wds:Q58058153-81400797-385A-4C34-B8BB-C084A1D3FDAD wds:Q58058153-89CE82B7-9660-42E6-80B9-61304865279F wds:Q58058153-8A58D908-FD88-47D3-9D38-C74017139D5B wds:Q58058153-945FAAF1-8FCF-4875-A6D6-53A656B4748C wds:Q58058153-9980CF2F-5EC8-4670-BF7A-8E5782DB6071 wds:Q58058153-9BCC93FD-6A2B-4D29-9611-9AB664A01882 wds:Q58058153-ACD7EB4C-7B63-4660-AE26-15FE08F43FDD wds:Q58058153-B46201BC-4A08-4E3A-BE75-3CE6F714E0E1 wds:Q58058153-B655526B-4A30-497D-BA2F-A4E33AA2405C wds:Q58058153-B96EC921-4700-4611-9558-92BFB46F467E wds:Q58058153-BFA66D35-A3C8-4BFC-8A08-FEE58A0A4814 wds:Q58058153-C8ECA363-082B-4941-816A-90B640A00D6D wds:Q58058153-D268FC34-1861-4F27-AC69-4578AF78AAB5 wds:Q58058153-D297A5AD-1B70-4481-A4ED-9C41C079E4A2 wds:Q58058153-E5AEBA1D-15AC-4440-BD78-DC7BEE3C7A44 wds:Q58058153-E617D919-BA37-4E9C-A53F-C3A9BEDB9749 wds:Q58058153-EAEFADA7-A7E0-414F-800E-43869B97934C
cites work	Affinity modulation of integrin alpha 5 beta 1: regulation of the functional response by soluble fibronectin Dualistic nature of adhesive protein function: fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function A monoclonal antibody against an activation epitope on mouse integrin chain beta 1 blocks adhesion of lymphocytes to the endothelial integrin alpha 6 beta 1. A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen Divalent cation regulation of the function of the leukocyte integrin LFA-1 Site-directed mutagenesis of the cell-binding domain of human fibronectin: separable, synergistic sites mediate adhesive function. Integrins: versatility, modulation, and signaling in cell adhesion Multiple functional forms of the integrin VLA-2 can be derived from a single alpha 2 cDNA clone: interconversion of forms induced by an anti-beta 1 antibody Chemical cross-linking leads to two high molecular mass aggregates of rat alpha 1 beta 1 integrin differing in their conformation but not in their composition Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization Adhesion of T and B lymphocytes to extracellular matrix and endothelial cells can be regulated through the beta subunit of VLA Stimulation of integrin-mediated adhesion of T lymphocytes and monocytes: two mechanisms with divergent biological consequences Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin alpha 5 beta 1. A monoclonal antibody to beta 1 integrin (CD29) stimulates VLA-dependent adherence of leukocytes to human umbilical vein endothelial cells and matrix components Ligands "activate" integrin alpha IIb beta 3 (platelet GPIIb-IIIa). Alpha 4 beta 1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand Intracellular Organic Phosphates as Regulators of Oxygen Release by Haemoglobin Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm Regulation of integrin alpha 5 beta 1-fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+. Identification of an alternatively spliced site in human plasma fibronectin that mediates cell type-specific adhesion Ligand intercellular adhesion molecule 1 has a necessary role in activation of integrin lymphocyte function-associated molecule 1 The vitronectin receptor alpha v beta 3 binds fibronectin and acts in concert with alpha 5 beta 1 in promoting cellular attachment and spreading on fibronectin Fibronectin receptors of mononuclear phagocytes: binding characteristics and biochemical isolation. An immunologic approach to the conformational equilibria of polypeptides Identification of a novel anti-integrin monoclonal antibody that recognises a ligand-induced binding site epitope on the β1 subunit Leukocyte integrins Interaction of leukocyte integrins with ligand is necessary but not sufficient for function Interaction of haemoglobin with protons, CO2 and 2,3-diphosphoglycerate
author name string	wds:Q58058153-7C61D6FB-8586-4906-89EA-2C175C9DAE3D
author name string	S K Akiyama
rdfs:label	The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy (en) The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy (nl)
skos:prefLabel	The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy (en) The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy (nl)
name	The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy (en) The Inhibitory Anti-β1 Integrin Monoclonal Antibody 13 Recognizes an Epitope That Is Attenuated by Ligand Occupancy (nl)
author	wds:Q58058153-58C5E198-414A-4205-B1D4-AF36BEBEE0B4 wds:Q58058153-7608E6AC-029E-4508-BC13-EEAAC67A4A33
author	Martin J. Humphries Paul Mould
title	wds:Q58058153-70DF0CDA-9CE9-4710-A475-7AD88921A0CE
title	The inhibitory anti-beta1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy. Evidence for allosteric inhibition of integrin function (en)
page(s)	wds:Q58058153-44C5396F-F2AB-4ACF-8988-E18A7818E944
page(s)	20365-20374
instance of	wds:Q58058153-50B8C165-627B-4373-8724-8B23CAC254D2
instance of	scholarly article
main subject	wds:Q58058153-3ECB6E48-83CD-4390-98DD-1E062AF3855D wds:Q58058153-A8CB1223-28ED-448E-81A1-E9E013455D09
main subject	monoclonal antibody antibody
PubMed ID	wds:Q58058153-856DC617-97B7-447E-9821-61037D70BCDE
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8702772
PubMed ID	8702772
published in	wds:Q58058153-14DFDE30-3C0D-4F4A-9A5A-3DFA7AB62133
published in	Journal of Biological Chemistry
issue	wds:Q58058153-F0ADA4A6-02F3-4EA5-B667-FAC7BA9A61C7
volume	wds:Q58058153-B7FC2BB5-333D-4AF2-BA7B-5F0A5027DB14

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