Beta 2 (CD18) mutations abolish ligand recognition by I domain integrins LFA-1 (alpha L beta 2, CD11a/CD18) and MAC-1 (alpha M beta 2, CD11b/CD18) (Q72391924)

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scientific article published on 01 January 1995

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English	Beta 2 (CD18) mutations abolish ligand recognition by I domain integrins LFA-1 (alpha L beta 2, CD11a/CD18) and MAC-1 (alpha M beta 2, CD11b/CD18)	scientific article published on 01 January 1995

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26 October 2019

Beta 2 (CD18) mutations abolish ligand recognition by I domain integrins LFA-1 (alpha L beta 2, CD11a/CD18) and MAC-1 (alpha M beta 2, CD11b/CD18) (English)

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26 October 2019

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M L Bajt

1

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26 October 2019

T Goodman

2

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26 October 2019

S L McGuire

3

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1 January 1995

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26 October 2019

Journal of Biological Chemistry

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26 October 2019

270

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26 October 2019

1

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26 October 2019

94-98

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26 October 2019

Leukocyte adhesion molecules deficiency: its structural basis, pathophysiology and implications for modulating the inflammatory response

1 reference

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Adhesion receptors of the immune system

1 reference

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Leucocyte cellular adhesion molecules

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A human leukocyte differentiation antigen family with distinct alpha-subunits and a common beta-subunit: the lymphocyte function-associated antigen (LFA-1), the C3bi complement receptor (OKM1/Mac-1), and the p150,95 molecule

1 reference

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Integrins: a family of cell surface receptors

1 reference

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Amino acid sequence of the alpha subunit of human leukocyte adhesion receptor Mo1 (complement receptor type 3)

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Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily

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VLA proteins in the integrin family: structures, functions, and their role on leukocytes

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Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1)

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Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1

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Intercellular adhesion molecule 3, a third adhesion counter-receptor for lymphocyte function-associated molecule 1 on resting lymphocytes

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Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor

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Identification of the C3bi receptor of human monocytes and macrophages by using monoclonal antibodies

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ICAM-1 (CD54): a counter-receptor for Mac-1 (CD11b/CD18)

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Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen

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Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor

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A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation

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Cloning of the beta subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family.

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The arrangement of the immunoglobulin-like domains of ICAM-1 and the binding sites for LFA-1 and rhinovirus

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Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylation

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The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands.

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A novel divalent cation-binding site in the A domain of the beta 2 integrin CR3 (CD11b/CD18) is essential for ligand binding

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Identifiers

10.1074/JBC.270.1.94

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7814426%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7814426%20AND%20SRC:MED&resulttype=core&format=json

26 October 2019

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