Regulation of integrin function by the urokinase receptor

Science

Volumn 273, Issue 5281, 1996, Pages 1551-1555

  Wei, Ying ^a   Lukashev, Matvey ^b   Simon, Daniel I ^a   Bodary, Sarah C ^c   Rosenberg, Steven ^d   Doyle, Michael V ^d   Chapman, Harold A ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c GENENTECH INC   (United States)

^d NOVARTIS PHARMA AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; PLASMINOGEN ACTIVATOR; UROKINASE; VITRONECTIN;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL ADHESION; ENZYME BINDING; IMMUNITY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; SIGNAL TRANSDUCTION; TUMOR GROWTH;

EID: 0029764639     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.273.5281.1551     Document Type: Article

References (61)

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60. Abbreviations for the amino acid residues are as follows: A. Ala; E, Glu; F, Phe; G, Gly; H, His; I, lie; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; S, Ser; T, Thr; and Y, Tyr.
61. Supported by NIH grants HL44712 (to H.A.C.), HL 02768 (to D.I.S.), and HD 26732 (to Caroline Damsky) and a grant from the American Heart Association (to D.I.S.). We thank L. Gu for technical assistance, N. Rao for helpful discussions, E. Ronne for antibodies to uPAR, M. Robinson for KIM 127, and P. Libby for vascular smooth muscle cells.