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Molecular comparison of soluble intercellular adhesion molecule (sICAM)-1 and sICAM-3 binding to lymphocyte function-associated antigen-1.

Autor: Woska, J R, Morelock, M M, Jeanfavre, D D, Caviness, G O, Bormann, B J, Rothlein, R

Publikováno v: Journal of Biological Chemistry; February 1998, Vol. 273 Issue: 8 p4725-33, 9p

A small-molecule antagonist of LFA-1 blocks a conformational change important for LFA-1 function.

Autor: Woska JR Jr; Department of Biology and. Department of Medicinal Chemistry, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, Connecticut 06877, USA. jwoska@rdg.boehringer-ingelheim.com, Shih D, Taqueti VR, Hogg N, Kelly TA, Kishimoto TK

Publikováno v: Journal of leukocyte biology [J Leukoc Biol] 2001 Aug; Vol. 70 (2), pp. 329-34.

Broad immunocytochemical localization of the formylpeptide receptor in human organs, tissues, and cells.

Autor: Becker EL; Department of Pathology, University of Connecticut Health Center Farmington, 263 Farmington Avenue, Farmington, CT 06030-3105, USA., Forouhar FA, Grunnet ML, Boulay F, Tardif M, Bormann BJ, Sodja D, Ye RD, Woska JR Jr, Murphy PM

Publikováno v: Cell and tissue research [Cell Tissue Res] 1998 Apr; Vol. 292 (1), pp. 129-35.

The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1.

Autor: Reilly PL; Department of Immunologic Disease, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT 06877, USA., Woska JR Jr, Jeanfavre DD, McNally E, Rothlein R, Bormann BJ

Publikováno v: Journal of immunology (Baltimore, Md. : 1950) [J Immunol] 1995 Jul 15; Vol. 155 (2), pp. 529-32.