Biochemical characterization of RAR1 cysteine- and histidine-rich domains (CHORDs): A novel class of zinc-dependent protein-protein interaction modules

Biochemistry

Volumn 46, Issue 6, 2007, Pages 1612-1623

  Heise, Charles T ^a   Le Duff, Cécile S ^b   Boter, Marta ^c   Casais, Catarina ^c   Airey, Joanne E ^a   Leech, Andrew P ^a   Amigues, Béatrice ^d   Guerois, Raphaël ^d   Moore, Geoffrey R ^b   Shirasu, Ken ^c,e   Kleanthous, Colin ^a  

^a UNIVERSITY OF YORK   (United Kingdom)

^b UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^c SAINSBURY LABORATORY   (United Kingdom)

^d CEA SACLAY   (France)

^e RIKEN Center for Sustainable Resource Science   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DENATURATION; HISTIDINE; PROTEIN-PROTEIN INTERACTION; SIGNALING PATHWAYS;

DISEASE CONTROL; FUNGI; IONIZATION; MASS SPECTROMETRY; MOLECULAR BIOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

PROTEINS;

CYSTEINE; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN 90; HISTIDINE; METALLOPROTEIN; PROTEIN CHORD I; PROTEIN CHORD II; PROTEIN RAR1; PROTEIN SGT1; REGULATOR PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; ZINC ION;

ALLELE; AMINO ACID SEQUENCE; ARABIDOPSIS; ARTICLE; ATOMIC ABSORPTION; BARLEY; CIRCULAR DICHROISM; CONTROLLED STUDY; CYSTEINE AND HISTIDINE RICH DOMAIN; ELECTROSPRAY MASS SPECTROMETRY; FLUORESCENCE ANALYSIS; ISOTHERMAL TITRATION CALORIMETRY; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CARRIER PROTEINS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; GLUCOSYLTRANSFERASES; HORDEUM; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLANT PROTEINS; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SPECTROPHOTOMETRY, ATOMIC; ULTRACENTRIFUGATION; ZINC;

ARABIDOPSIS; EUKARYOTA; FUNGI; HORDEUM;

EID: 33846952144     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062174k     Document Type: Article

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