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Proceedings of the National Academy of Sciences of the United States of America

Volumn 98, Issue 5, 2001, Pages 2387-2392

An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond

(6) Lu, Chafen a,c Shimaoka, Motomu b Ferzly, Mazen a Oxvig, Claus a,d Takagi, Junichi a Springer, Timothy A a

a CENTER FOR BLOOD RESEARCH (United States)

b HARVARD MEDICAL SCHOOL (United States)

c MILLENNIUM PHARMACEUTICALS INC (United States)

d AARHUS UNIVERSITY (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; IMMUNOGLOBULIN A; INTEGRIN; INTERCELLULAR ADHESION MOLECULE 1; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MEVINOLIN;

ARTICLE; CELL ADHESION; CELL STRAIN K 562; DISULFIDE BOND; DRUG MECHANISM; DRUG PROTEIN BINDING; GENE MUTATION; HUMAN; HUMAN CELL; LIGAND BINDING; MOLECULAR MODEL; PRIORITY JOURNAL;

CELL ADHESION; DIMERIZATION; DISULFIDES; INTERCELLULAR ADHESION MOLECULE-1; LOVASTATIN; LYMPHOCYTE FUNCTION-ASSOCIATED ANTIGEN-1; MUTATION; PROTEIN CONFORMATION;

EID: 0035956969 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.041606398 Document Type: Article

Times cited : (120)

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