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Titolo:
Receptor for motilin identified in the human gastrointestinal system
Autore:
Feighner, SD; Tan, CP; McKee, KK; Palyha, OC; Hreniuk, DL; Pong, SS; Austin, CP; Figueroa, D; MacNeil, D; Cascieri, MA; Nargund, R; Bakshi, R; Abramovitz, M; Stocco, R; Kargman, S; ONeill, G; Van der Ploeg, LHT; Evans, J; Patchett, AA; Smith, RG; Howard, AD;
Indirizzi:
Merck Res Labs, Dept Metab Disorders, Rahway, NJ 07065 USA Merck Res LabsRahway NJ USA 07065 Metab Disorders, Rahway, NJ 07065 USA Merck Res Labs, Dept Human Genet, W Point, PA 19486 USA Merck Res Labs W Point PA USA 19486 pt Human Genet, W Point, PA 19486 USA MerckL1,osst Ctr Therapeut Res, Dept Biochem & Mol Biol, Kirkland, PQ H3H 3 Merck Frosst Ctr Therapeut Res Kirkland PQ Canada H3H 3L1 kland, PQ H3H 3 Merck Res Labs, Dept Med Chem, Rahway, NJ 07065 USA Merck Res Labs RahwayNJ USA 07065 s, Dept Med Chem, Rahway, NJ 07065 USA Baylor Coll Med, Dept Cell Biol, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 ept Cell Biol, Houston, TX 77030 USA Baylor Coll Med, Huffington Ctr Aging, Houston, TX 77030 USA Baylor Coll Med Houston TX USA 77030 ton Ctr Aging, Houston, TX 77030 USA
Titolo Testata:
SCIENCE
fascicolo: 5423, volume: 284, anno: 1999,
pagine: 2184 - 2188
SICI:
0036-8075(19990625)284:5423<2184:RFMIIT>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-HORMONE SECRETAGOGUE; BINDING-SITES; SMOOTH-MUSCLE; SEQUENCE; RABBIT; EXPRESSION; LOCALIZATION; ERYTHROMYCIN; PRECURSOR; PITUITARY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Howard, AD Merckhway,Labs, Dept Metab Disorders, Bldg RY-80Y-265,126 E Lincoln Ave, Ra Merck Res Labs Bldg RY-80Y-265,126 E Lincoln Ave Rahway NJ USA07065
Citazione:
S.D. Feighner et al., "Receptor for motilin identified in the human gastrointestinal system", SCIENCE, 284(5423), 1999, pp. 2184-2188

Abstract

Motilin is a 22-amino acid peptide hormone expressed throughout the gastrointestinal (GI) tract of humans and other species. It affects gastric motility by stimulating interdigestive antrum and duodenal contractions. A heterotrimeric guanosine triphosphate-binding protein (G protein)-coupled receptor for motilin was isolated from human stomach, and its amino acid sequencewas found to be 52 percent identical to the human receptor for growth hormone secretagogues. The macrolide antibiotic erythromycin also interacted with the cloned motilin receptor, providing a molecular basis for its effectson the human GI tract. The motilin receptor is expressed in enteric neurons of the human duodenum and colon. Development of motilin receptor agonistsand antagonists may be useful in the treatment of multiple disorders of GImotility.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:03:33