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Titolo:
Protease activated receptors: theme and variations
Autore:
OBrien, PJ; Molino, M; Kahn, M; Brass, LF;
Indirizzi:
Univ Penn, Dept Med, Ctr Expt Therapeut, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Therapeut, Philadelphia, PA 19104 USA Univ Penn, Dept Pharmacol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Pharmacol, Philadelphia, PA 19104 USA Ist Ric Farmacol Mario Negri, Consorzio Mario Negri Sud, I-66030 Santa Maria Imbaro, Italy Ist Ric Farmacol Mario Negri Santa Maria Imbaro Italy I-66030 aro, Italy
Titolo Testata:
ONCOGENE
fascicolo: 13, volume: 20, anno: 2001,
pagine: 1570 - 1581
SICI:
0950-9232(20010326)20:13<1570:PARTAV>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET THROMBIN RECEPTOR; HUMAN-ENDOTHELIAL-CELLS; CATHEPSIN-G; TETHERED-LIGAND; MOLECULAR-CLONING; MAST-CELL; FUNCTIONAL EXPRESSION; AGONIST RECOGNITION; CROSS-REACTIVITY; CYTOPLASMIC TAIL;
Keywords:
protease-activated receptors; thrombin; platelets; endothielial cells; G proteins; G protein coupled receptors;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
115
Recensione:
Indirizzi per estratti:
Indirizzo: Brass, LF Univ Penn, Dept Med, Ctr Expt Therapeut, Room 913 BRB 2-3,421 Curie Blvd, Philadelphia, PA 19104 USA Univ Penn Room 913 BRB 2-3,421 Curie Blvd Philadelphia PA USA 19104
Citazione:
P.J. O'Brien et al., "Protease activated receptors: theme and variations", ONCOGENE, 20(13), 2001, pp. 1570-1581

Abstract

The four PAR family members are G protein coupled receptors that are normally activated by proteolytic exposure of an occult tethered ligand, Three of the family members are thrombin receptors, The fourth (PAR2) is not activated by thrombin, but can be activated by other proteases, including trypsin, tryptase and Factor Xa, This review focuses on recent information about the manner in which signaling through these receptors is initiated and terminated, including evidence for inter- as well as intramolecular modes of activation, and continuing efforts to identify additional, biologically-relevant proteases that can activate PAR family members.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 08:36:04