NMR indicates that the small molecule RITA does not block p53-MDM2 binding in vitro [1]

Nature Medicine

Volumn 11, Issue 11, 2005, Pages 1135-1136

  Krajewski, Marcin ^a   Ozdowy, Przemyslaw ^a   D'Silva, Loyola ^a   Rothweiler, Ulli ^a   Holak, Tad A ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; PROTEIN; PROTEIN MDM2; PROTEIN P53; SMALL MOLECULE RITA; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; BINDING SITE; FLUORESCENCE CORRELATION SPECTROSCOPY; LETTER; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION;

AMINO ACID SEQUENCE; BINDING SITES; CHROMATOGRAPHY, AFFINITY; DIFFUSION; DNA-BINDING PROTEINS; GENE DELETION; GLUTATHIONE TRANSFERASE; HISTIDINE; HUMANS; KINETICS; NEOPLASM PROTEINS; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-MDM2; PROTONS; RECOMBINANT FUSION PROTEINS; SPECTROMETRY, FLUORESCENCE; TITRIMETRY; TUMOR SUPPRESSOR PROTEIN P53;

EID: 30744449974     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm1105-1135     Document Type: Letter

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