Exploration of natural product ingredients as inhibitors of human HMG-CoA reductase through structure-based virtual screening

Drug Design, Development and Therapy

Volumn 9, Issue , 2015, Pages 3313-3324

  Lin, Shih Hung ^a   Huang, Kao Jean ^a,b   Weng, Ching Feng ^a   Shiuan, David ^a  

^a NATIONAL DONG HWA UNIVERSITY   (Taiwan)

^b Div Agricultural Biotechnology   (Taiwan)

Author keywords

Curcumin; HMG CoA reductase; Salvianolic acid C; Virtual screening

Indexed keywords

ALCOHOL DERIVATIVE; AMPELOPSISIN; ANTILIPEMIC AGENT; ARGININE; ASPARTIC ACID; ATORVASTATIN; BEHENYL ALCOHOL; CERIVASTATIN; COMPACTIN; CURCUMIN; EPIGALLOCATECHIN GALLATE; FLUINDOSTATIN; FOLIC ACID; HETEROCYCLIC COMPOUND; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; ISOQUERCITRIN; LIGUSTILIDE; LYSINE; NATURAL PRODUCT; POLYPHENOL DERIVATIVE; SALVIANOLIC ACID C; SERINE; TENELLIN; TETRACOSANOL; UNCLASSIFIED DRUG; VALINE; ALKENE; HERBACEOUS AGENT; HMGCR PROTEIN, HUMAN; LIGAND; POLYPHENOL; PROTEIN BINDING; RECOMBINANT PROTEIN;

ARTICLE; CHINESE MEDICINE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG ABSORPTION; DRUG CYTOTOXICITY; DRUG DISTRIBUTION; DRUG EXCRETION; DRUG METABOLISM; ENZYME INHIBITION; HUMAN; HUMAN CELL; IC50; IN VITRO STUDY; LIGAND BINDING; MOLECULAR DOCKING; NONHUMAN; PREDICTIVE VALUE; PROTEIN DATA BANK; PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; STRUCTURE BASED VIRTUAL SCREENING; TRADITIONAL MEDICINE; BINDING SITE; CHEMISTRY; DOSE RESPONSE; DRUG DEVELOPMENT; FEASIBILITY STUDY; HEP-G2 CELL LINE; METABOLISM; PROCEDURES; PROTEIN CONFORMATION; PROTEIN DATABASE;

ALKENES; BINDING SITES; CURCUMIN; DATABASES, PROTEIN; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG DISCOVERY; DRUGS, CHINESE HERBAL; FEASIBILITY STUDIES; HEP G2 CELLS; HUMANS; HYDROXYMETHYLGLUTARYL COA REDUCTASES; HYDROXYMETHYLGLUTARYL-COA REDUCTASE INHIBITORS; LIGANDS; MOLECULAR DOCKING SIMULATION; POLYPHENOLS; PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84936852429     PISSN: None     EISSN: 11778881     Source Type: Journal    
DOI: 10.2147/DDDT.S84641     Document Type: Article

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