Docking and molecular dynamics studies toward the binding of new natural phenolic marine inhibitors and aldose reductase

Journal of Molecular Graphics and Modelling

Volumn 28, Issue 2, 2009, Pages 162-169

  Wang, Zhiguo ^a,c   Ling, Baoping ^b   Zhang, Rui ^a,c   Suo, Yourui ^a   Liu, Yongjun ^a,b   Yu, Zhangyu ^b   Liu, Chengbu ^b  

^a NORTHWEST INSTITUTE OF PLATEAU BIOLOGY   (China)

^b SHANDONG UNIVERSITY   (China)

^c UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Aldose reductase; Dynamics; Inhibition; Molecular docking; Phenolic ARIs

Indexed keywords

ACTIVE SPACES; ALDOSE REDUCTASE; ALDOSE REDUCTASE INHIBITORS; BINDING FREE ENERGY; BINDING MODES; BOUND INHIBITORS; ELECTRON-WITHDRAWING EFFECTS; ELECTROSTATIC EFFECT; HIGH STABILITY; INHIBITION; INHIBITION EFFECT; INHIBITION MECHANISMS; INHIBITOR MOLECULES; IONIZED STATE; MARINE NATURAL PRODUCTS; MOLECULAR DOCKING; PHENOLIC ARIS; PHYSIOLOGICAL ENVIRONMENT; STERIC HINDRANCES;

BINDING SITES; CHEMICAL REACTIONS; DOCKING; DYNAMICS; HYDROGEN; HYDROGEN BONDS; MOLECULAR DYNAMICS; MOLECULAR MODELING; PHENOLS;

BINDING ENERGY;

ALDEHYDE REDUCTASE; EPALRESTAT; FIDARESTAT; LACTONE; NATURAL PRODUCT; PHENOL; SORBINIL; TOLRESTAT;

ARTICLE; CHEMICAL STRUCTURE; IONIZATION; MOLECULAR DOCKING; MOLECULAR DYNAMICS; PRIORITY JOURNAL;

ALDEHYDE REDUCTASE; ENZYME INHIBITORS; HYDROGEN BONDING; IMIDAZOLIDINES; MOLECULAR DYNAMICS SIMULATION; NAPHTHALENES; PROTEIN STRUCTURE, SECONDARY; RHODANINE; THIAZOLIDINES;

EID: 70349332928     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2009.06.003     Document Type: Article

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