Structural basis for AMPK activation: Natural and synthetic ligands regulate kinase activity from opposite poles by different molecular mechanisms

Structure

Volumn 22, Issue 8, 2014, Pages 1161-1172

  Calabrese, Matthew F ^a   Rajamohan, Francis ^a   Harris, Melissa S ^a   Caspers, Nicole L ^a   Magyar, Rachelle ^a   Withka, Jane M ^a   Wang, Hong ^a   Borzilleri, Kris A ^a   Sahasrabudhe, Parag V ^a   Hoth, Lise R ^a   Geoghegan, Kieran F ^a   Han, Seungil ^a   Brown, Janice ^a   Subashi, Timothy A ^a   Reyes, Allan R ^a   Frisbie, Richard K ^a   Ward, Jessica ^a   Miller, Russell A ^a   Landro, James A ^a   Londregan, Allyn T ^a   Carpino, Philip A ^a   Cabral, Shawn ^a   Smith, Aaron C ^a   Conn, Edward L ^a   Cameron, Kimberly O ^a   Qiu, Xiayang ^a   Kurumbail, Ravi G ^a   more..

^a PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6,7 DIHYDRO 4 HYDROXY 3 (2' HYDROXY 1,1' BIPHENYL 4 YL) 6 OXOTHIENO[2,3 B]PYRIDINE 5 CARBONITRILE; ADENOSINE PHOSPHATE; ADENYLATE KINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; ISOPROTEIN; LIGAND; PYRONE DERIVATIVE; THIOPHENE DERIVATIVE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVATION; ENZYME BINDING; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN PROCESSING; STATIC ELECTRICITY; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DELIVERY SYSTEM; GENETICS; HUMAN; KINETICS; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; SURFACE PLASMON RESONANCE;

MAMMALIA;

ADENOSINE MONOPHOSPHATE; ALLOSTERIC SITE; AMP-ACTIVATED PROTEIN KINASES; DRUG DELIVERY SYSTEMS; ENZYME ACTIVATION; HUMANS; KINETICS; LIGANDS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN ISOFORMS; PYRONES; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PLASMON RESONANCE; THIOPHENES;

EID: 84905719900     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.06.009     Document Type: Article

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