Proline primed helix length as a modulator of the nuclear receptor-coactivator interaction

Journal of the American Chemical Society

Volumn 135, Issue 11, 2013, Pages 4364-4371

  Fuchs, Sascha ^a   Nguyen, Hoang D ^a,b   Phan, Trang T P ^b   Burton, Matthew F ^a   Nieto, Lidia ^a   De Vries Van Leeuwen, Ingrid J ^a   Schmidt, Andrea ^a   Goodarzifard, Monireh ^a   Agten, Stijn M ^a   Rose, Rolf ^b   Ottmann, Christian ^a,b   Milroy, Lech Gustav ^a   Brunsveld, Luc ^a,b  

^a EINDHOVEN UNIVERSITY OF TECHNOLOGY   (Netherlands)

^b CHEMICAL GENOMICS CENTRE OF THE MAX PLANCK SOCIETY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

GENE TRANSCRIPTIONS; OPTIMAL INTERACTIONS; PEPTIDE RECOGNITION; PROTEIN-PROTEIN INTERACTIONS; PROTEINOGENIC AMINO ACIDS; RECEPTOR ACTIVATION; SEQUENCE SPECIFICITY; STRUCTURAL PARAMETER;

AMINO ACIDS; DNA SEQUENCES; DRUG THERAPY; TRANSCRIPTION FACTORS; X RAY CRYSTALLOGRAPHY;

TRANSCRIPTION;

AMINO ACID; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; NUCLEAR RECEPTOR COACTIVATOR; PROLINE; SYNTHETIC PEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; DIPOLE; DNA LIBRARY; FLUORESCENCE POLARIZATION IMMUNOASSAY; GENETIC TRANSCRIPTION; HYDROGEN BOND; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR MODEL; PEPTIDE SYNTHESIS; PHAGE DISPLAY; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; RIBOSOME; SURFACE CHARGE; X RAY CRYSTALLOGRAPHY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CONSENSUS SEQUENCE; CRYSTALLOGRAPHY, X-RAY; GENE LIBRARY; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES; PROLINE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECEPTORS, ESTROGEN;

EID: 84875420702     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja311748r     Document Type: Article

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