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Titolo:
MULTIPLE BINDING MODE OF REVERSIBLE SYNTHETIC THROMBIN INHIBITORS - ACOMPARATIVE STRUCTURAL-ANALYSIS
Autore:
PAVONE V; DESIMONE G; NASTRI F; GALDIERO S; STAIANO N; LOMBARDI A; PEDONE C;
Indirizzi:
UNIV NAPLES,CNR,CTR INTERUNIV RIC PEPTIDI BIOATTIVI,VIA MEZZOCANNONE 4 I-80134 NAPLES ITALY UNIV NAPLES,CNR,CTR INTERUNIV RIC PEPTIDI BIOATTIVI I-80134 NAPLES ITALY UNIV NAPLES,CNR,CTR STUDIO BIOCRISTALLOG I-80134 NAPLES ITALY UNIV NAPLES FEDERICO II,DIPARTIMENTO BIOCHIM & BIOTECNOL MED I-80129 NAPLES ITALY
Titolo Testata:
Biological chemistry
fascicolo: 8-9, volume: 379, anno: 1998,
pagine: 987 - 1006
SICI:
1431-6730(1998)379:8-9<987:MBMORS>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN ALPHA-THROMBIN; ACTIVE-SITE INHIBITORS; PRO-ARG CHLOROMETHYLKETONE; ORALLY BIOAVAILABLE CLASS; SUBSTITUTED L-ARGININE; RAY CRYSTAL-STRUCTURE; P-NITROPHENYL-ESTER; HEPARIN COFACTOR-II; C-TERMINAL REGION; ANTITHROMBIN ACTIVITY;
Keywords:
ANTITHROMBOTICS; HIRUNORMS; THROMBIN; THROMBIN SYNTHETIC INHIBITORS; X-RAY CRYSTAL STRUCTURE;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
140
Recensione:
Indirizzi per estratti:
Citazione:
V. Pavone et al., "MULTIPLE BINDING MODE OF REVERSIBLE SYNTHETIC THROMBIN INHIBITORS - ACOMPARATIVE STRUCTURAL-ANALYSIS", Biological chemistry, 379(8-9), 1998, pp. 987-1006

Abstract

The central role of the serine protease thrombin in hemostasis and thrombosis brought many scientists to develop highly potent and selective thrombin inhibitors. Thrombin-inhibitor complexes have extensively been studied in order to understand structure-function relationships, and to design new inhibitors that can be used with broader efficacy over existing antithrombotic agents. In this paper, we summarize in a comparative manner the state of the art on reversible thrombin inhibitorsand we discuss some structural aspects of thrombin-inhibitor interaction, which account for the different affinity and potency of these molecules. We also report here our approach to develop a new class of synthetic, multisite-directed thrombin inhibitors, named hirunorms, designed to mimic the distinctive binding mode of hirudin, We emphasize here that, despite the high specificity of thrombin action, the interaction of inhibitors in its active site may occur with quite different mechanisms.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 17:22:38