Mechanism by which a recently discovered allosteric inhibitor blocks glutamine metabolism in transformed cells

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 2, 2015, Pages 394-399

  Stalnecker, Clint A ^a   Ulrich, Scott M ^b   Li, Yunxing ^a   Ramachandran, Sekar ^a   McBrayer, Mary Kate ^c   De Berardinis, Ralph J ^d   Cerione, Richard A ^a   Erickson, Jon W ^a  

^a Department of Obstetrics Gynecology   (United States)

^b ITHACA COLLEGE   (United States)

^c NATHAN S KLINE INSTITUTE FOR PSYCHIATRIC RESEARCH   (United States)

^d UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

Benzophenanthridines; FRET; Glutaminase; Glutaminolysis; Rho GTPases

Indexed keywords

GLUTAMINASE; GLUTAMINASE C; GLUTAMINE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; AMINOTRANSFERASE; BENZOPHENANTHRIDINE DERIVATIVE; ENZYME INHIBITOR; GLUTAMINE-PYRUVATE AMINOTRANSFERASE; RECOMBINANT PROTEIN;

ALLOSTERISM; AMINO ACID METABOLISM; ANIMAL CELL; ARTICLE; BREAST EPITHELIUM CELL; CANCER CELL; CELL PROLIFERATION; CELL STRUCTURE; CONTACT INHIBITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVATION; ENZYME ACTIVITY; FIBROBLAST; FLUORESCENCE; FLUORESCENCE ANALYSIS; MOUSE; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; REGULATORY MECHANISM; TRANSFORMED CELL; AMINO ACID SUBSTITUTION; ANIMAL; ANTAGONISTS AND INHIBITORS; CELL TRANSFORMATION; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENETICS; METABOLISM; PROTEIN QUATERNARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; ANIMALS; BENZOPHENANTHRIDINES; CELL TRANSFORMATION, NEOPLASTIC; ENZYME INHIBITORS; FLUORESCENCE RESONANCE ENERGY TRANSFER; GLUTAMINE; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; TRANSAMINASES;

EID: 84920990454     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1414056112     Document Type: Article

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