Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartatesensitive glutamate receptor

Journal of Biological Chemistry

Volumn 288, Issue 31, 2013, Pages 22506-22515

  Choi, Ucheor B ^a   Kazi, Rashek ^a   Stenzoski, Natalie ^a   Wollmuth, Lonnie P ^a   Uversky, Vladimir N ^b,c   Bowen, Mark E ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b UNIVERSITY OF SOUTH FLORIDA   (United States)

^c INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC REGULATION; CONFORMATIONAL DYNAMICS; CYTOPLASMIC DOMAINS; DISORDERED PROTEINS; GLUTAMATE RECEPTOR; INTRINSIC DISORDER; PROLINE RESIDUES; UNDERLYING DYNAMICS;

PROTEINS;

BIOACTIVITY;

N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROLINE;

ALLOSTERISM; ARTICLE; CHANNEL GATING; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; FLUORESCENCE; MOLECULAR DYNAMICS; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; SOLUBILITY;

ELECTROPHYSIOLOGY; FLUORESCENCE RESONANCE ENERGY TRANSFER (FRET); GLUTAMATE RECEPTORS IONOTROPIC (AMPA, NMDA); INTRINSICALLY DISORDERED PROTEINS; SINGLE MOLECULE BIOPHYSICS;

ALLOSTERIC REGULATION; CYTOPLASM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEK293 CELLS; HUMANS; PROTEIN BINDING; RECEPTORS, N-METHYL-D-ASPARTATE; SOLUBILITY;

EID: 84881261693     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.477810     Document Type: Article

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