Distinct Structural Features of Cyclothiazide Are Responsible for Effects on Peak Current Amplitude and Desensitization Kinetics at iGluR2

Journal of Molecular Biology

Volumn 391, Issue 5, 2009, Pages 906-917

  Hald, Helle ^a,b   Ahring, Philip K ^b   Timmermann, Daniel B ^b   Liljefors, Tommy ^a   Gajhede, Michael ^a   Kastrup, Jette S ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b NEUROSEARCH A S   (Denmark)

Author keywords

allosteric modulators; ionotropic glutamate receptors; ligand binding core; patch clamp electrophysiology; X ray crystallography

Indexed keywords

AMPA RECEPTOR AGONIST; CYCLOPENTANE; CYCLOTHIAZIDE; GLUTAMIC ACID; IONOTROPIC RECEPTOR; IONOTROPIC RECEPTOR 2; NS 1493; NS 5206; NS 5217; UNCLASSIFIED DRUG;

ALLOSTERISM; ANIMAL CELL; ARTICLE; CHEMICAL MODIFICATION; CHO CELL; CONCENTRATION RESPONSE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DRUG CONFORMATION; DRUG EFFICACY; DRUG POTENCY; DRUG RECEPTOR BINDING; DRUG STRUCTURE; ELECTROPHYSIOLOGY; FEMALE; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; NONHUMAN; PATCH CLAMP; PRIORITY JOURNAL; RECEPTOR DOWN REGULATION; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

HUMAN ECHOVIRUS 1;

ALLOSTERIC REGULATION; ANIMALS; ANTIHYPERTENSIVE AGENTS; BENZOTHIADIAZINES; CHO CELLS; CRICETINAE; CRICETULUS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GLUTAMIC ACID; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PATCH-CLAMP TECHNIQUES; PIPERAZINES; PROTEIN STRUCTURE, QUATERNARY; RATS; RECEPTORS, AMPA;

EID: 68349086837     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.002     Document Type: Article

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