A unique mechanism of curcumin inhibition on F1 ATPase

Biochemical and Biophysical Research Communications

Volumn 452, Issue 4, 2014, Pages 940-944

  Sekiya, Mizuki ^a   Hisasaka, Ryosuke ^a   Iwamoto Kihara, Atsuko ^b   Futai, Masamitsu ^a   Nakanishi Matsui, Mayumi ^a  

^a IWATE MEDICAL UNIVERSITY   (Japan)

^b NAGAHAMA INSTITUTE OF BIO SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

ATP synthase; ATPase rotational catalysis; Curcumin; F1 ATPase; Piceatannol; Quercetin

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CURCUMIN; PICEATANNOL; POLYPHENOL; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; QUERCETIN; PROTEIN BINDING; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ALPHA HELIX; ARTICLE; BACTERIAL GENE; BETA SHEET; BINDING SITE; BIOASSAY; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME INHIBITION; ESCHERICHIA COLI; GENE MUTATION; HINGE REGION; HYDROLYSIS; NONHUMAN; ROTATION; ROTATION ASSAY; WILD TYPE; AMINO ACID SEQUENCE; ANTAGONISTS AND INHIBITORS; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME SPECIFICITY; MOLECULAR GENETICS; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; ULTRASTRUCTURE;

AMINO ACID SEQUENCE; BINDING SITES; CURCUMIN; ENZYME ACTIVATION; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 84907899430     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.09.027     Document Type: Article

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