Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface (Q27737553)

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J H Liu

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S C Harrison

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J H Wang

Integrins: versatility, modulation, and signaling in cell adhesion

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language of work or name

English

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publication date

15 May 1997

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published in

Nature

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volume

387

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issue

6630

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page(s)

312-5

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cites work

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7 January 2021

Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm

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Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)

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Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin

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2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

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Crystal structure of an integrin-binding fragment of vascular cell adhesion molecule-1 at 1.8 A resolution

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The crystal structure of an N-terminal two-domain fragment of vascular cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 C-D loop can inhibit VCAM-1-alpha 4 integrin interaction

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Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity

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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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Analysis of the binding site on intercellular adhesion molecule 3 for the leukocyte integrin lymphocyte function-associated antigen 1.

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Localization of the binding site on intercellular adhesion molecule-3 (ICAM-3) for lymphocyte function-associated antigen 1 (LFA-1)

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Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains

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A year in the life of the immunoglobulin superfamily

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Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution

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7 January 2021

Complex salt bridges in proteins: statistical analysis of structure and function

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A Binding Interface on the I Domain of Lymphocyte Function-associated Antigen-1 (LFA-1) Required for Specific Interaction with Intercellular Adhesion Molecule 1 (ICAM-1)

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Folding of the N-terminal, ligand-binding region of integrin alpha-subunits into a beta-propeller domain

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The major human rhinovirus receptor is ICAM-1

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A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses

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Intercellular adhesion molecule-1 is an endothelial cell adhesion receptor for Plasmodium falciparum

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Identification of monoclonal antibody epitopes and critical residues for rhinovirus binding in domain 1 of intercellular adhesion molecule 1

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Plasmodium falciparum-infected erythrocytes bind ICAM-1 at a site distinct from LFA-1, Mac-1, and human rhinovirus

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7 January 2021

The binding site on ICAM-1 for Plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site

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7 January 2021

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

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7 January 2021

Kinetics and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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7 January 2021