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Journal of Molecular Graphics and Modelling

Volumn 23, Issue 4, 2005, Pages 381-388

The function of the amino terminal domain in NMDA receptor modulation

(2) Huggins, David J a Grant, Guy H a,b

a UNIVERSITY OF OXFORD (United Kingdom)

b UNIVERSITY OF CAMBRIDGE (United Kingdom)

Author keywords

Desensitization; Docking; Glutamate; Glycine; Homology modelling; Inhibition; NMDA; Receptors; Spermine; Zinc

Indexed keywords

ACTIVATION ANALYSIS; AMINES; COMPUTER SIMULATION; DIMERS; DRUG PRODUCTS; ENZYME INHIBITION; MUTAGENESIS; ZINC;

N-METHYL-D-ASPARTATE (NMDA); NEUROTRANSMISSION; POLYAMINES; RECEPTORS;

NEUROLOGY;

CYSTEINE; DIMER; HISTIDINE; IFENPRODIL; METABOTROPIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN SUBUNIT; ZINC ION;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; DISULFIDE BOND; METAL BINDING; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN STABILITY; RECEPTOR DOWN REGULATION; RECEPTOR INTRINSIC ACTIVITY; REGULATORY MECHANISM; STRUCTURAL HOMOLOGY;

AMINO ACID SEQUENCE; BINDING SITES; DIMERIZATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PIPERIDINES; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, AMPA; RECEPTORS, N-METHYL-D-ASPARTATE; SEQUENCE HOMOLOGY, AMINO ACID; SPERMINE; ZINC;

EID: 12844268621 PISSN: 10933263 EISSN: None Source Type: Journal
DOI: 10.1016/j.jmgm.2004.11.006 Document Type: Article

Times cited : (40)

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