The novolactone natural product disrupts the allosteric regulation of Hsp70

Chemistry and Biology

Volumn 22, Issue 1, 2015, Pages 87-97

  Hassan, A Quamrul ^b   Kirby, Christina A ^b   Zhou, Wenlai ^b   Schuhmann, Tim ^a   Kityk, Roman ^c   Kipp, D Randal ^b   Baird, Jason ^b   Chen, Jinyun ^b   Chen, Yaoyu ^b   Chung, Franklin ^b   Hoepfner, Dominic ^a   Movva, N Rao ^a   Pagliarini, Raymond ^b   Petersen, Frank ^a   Quinn, Christopher ^b   Quinn, Douglas ^b   Riedl, Ralph ^a   Schmitt, Esther K ^a   Schitter, Anne ^a   Stams, Travis ^b   Studer, Christian ^a   Fortin, Pascal D ^b   Mayer, Matthias P ^c   Sadlish, Heather ^a   more..

^a NOVARTIS PHARMA AG   (Switzerland)

^b NOVARTIS INSTITUTES FOR BIOMEDICAL RESEARCH   (United States)

^c GERMAN CANCER RESEARCH CENTER   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; LACTONE DERIVATIVE; NATURAL PRODUCT; NOVOLACTONE; UNCLASSIFIED DRUG; ABIETANE DERIVATIVE; BIOLOGICAL PRODUCT; ISOPROTEIN; PROTEIN BINDING;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; COVALENT BOND; CRYSTAL STRUCTURE; CYTOSOL; ENDOPLASMIC RETICULUM; FUNGAL STRAIN; HYDROGEN BOND; HYDROLYSIS; LIQUID CHROMATOGRAPHY; LUNG CANCER CELL LINE; MASS SPECTROMETRY; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; STEADY STATE; X RAY CRYSTALLOGRAPHY; YEAST; BINDING SITE; CELL LINE; CHEMISTRY; ENZYME SPECIFICITY; FUNGAL GENOME; GENETICS; HUMAN; METABOLISM; MOLECULAR DYNAMICS; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATASES; ALLOSTERIC REGULATION; BINDING SITES; BIOLOGICAL PRODUCTS; CELL LINE; CRYSTALLOGRAPHY, X-RAY; DITERPENES, ABIETANE; ENDOPLASMIC RETICULUM; GENOME, FUNGAL; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

EID: 84921494281     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2014.11.007     Document Type: Article

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