Structure-activity relationship, kinetic mechanism, and selectivity for a new class of ubiquitin C-terminal hydrolase-L1 (UCH-L1) inhibitors

Bioorganic and Medicinal Chemistry Letters

Volumn 17, Issue 13, 2007, Pages 3729-3732

  Mermerian, Ara H ^a   Case, April ^a   Stein, Ross L ^a   Cuny, Gregory D ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

Inhibitor; Kinetic mechanism; Selectivity; Ubiquitin C terminal hydrolase L1; UCH L1

Indexed keywords

3 AMINO 2 KETO 7H THIENO[2,3 B]PYRIDIN 6 ONE; CARBOXYLIC ACID; CASPASE 3; ENZYME; ISOPEPTIDASE T; KETONE; PAPAIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; PYRIDINE DERIVATIVE; PYRIDONE DERIVATIVE; UBIQUITIN CARBOXYTERMINAL HYDROLASE L1; UBIQUITIN CARBOXYTERMINAL HYDROLASE L3; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

ARTICLE; CYTOTOXICITY; DRUG SELECTIVITY; DRUG STRUCTURE; DRUG SYNTHESIS; HYDROLYSIS; KINETICS; MICHAELIS CONSTANT; STRUCTURE ACTIVITY RELATION;

CELL LINE, TUMOR; CHEMISTRY, PHARMACEUTICAL; CYSTEINE; DRUG DESIGN; ENZYME INHIBITORS; HUMANS; KETONES; KINETICS; MODELS, CHEMICAL; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; UBIQUITIN THIOLESTERASE;

EID: 34250160956     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2007.04.027     Document Type: Article

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