Structural basis for dimerization of ICAM-1 on the cell surface. (Q47729587)

5 February 2018

title

Structural basis for dimerization of ICAM-1 on the cell surface. (English)

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5 February 2018

5

Andrzej Joachimiak

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5 February 2018

author name string

Yuting Yang

1

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5 February 2018

Chang-Duk Jun

2

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5 February 2018

Jin-Huan Liu

3

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5 February 2018

Rongguang Zhang

4

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5 February 2018

Timothy A Springer

6

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5 February 2018

Jia-Huai Wang

7

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5 February 2018

publication date

1 April 2004

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5 February 2018

published in

Molecular Cell

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5 February 2018

volume

14

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issue

2

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page(s)

269-276

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5 February 2018

The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand

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A dimeric crystal structure for the N-terminal two domains of intercellular adhesion molecule-1

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Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex

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Location of the domains of ICAM-1 by immunolabeling and single-molecule electron microscopy

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The immunological synapse balances T cell receptor signaling and degradation

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Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1.

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Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation

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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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Automated MAD and MIR structure solution

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Cloning and characterization of a new intercellular adhesion molecule ICAM-R

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Identifiers

DOI

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5 February 2018

PubMed ID

15099525

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5 February 2018