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Journal of Biological Inorganic Chemistry

Volumn 16, Issue 2, 2011, Pages 217-226

Substitution of aspartic acid with glutamic acid at position 67 of the BRCA1 RING domain retains ubiquitin ligase activity and zinc(II) binding with a reduced transition temperature

(3) Atipairin, Apichart a Canyuk, Bhutorn a Ratanaphan, Adisorn a

a PRINCE OF SONGKLA UNIVERSITY (Thailand)

Author keywords

BRCA1; D67E; Transition temperature; Ubiquitin ligase; Zn2+ binding

Indexed keywords

ASPARTIC ACID; BRCA1 ASSOCIATED RING DOMAIN PROTEIN 1; BRCA1 PROTEIN; GLUTAMIC ACID; MUTANT PROTEIN; UBIQUITIN PROTEIN LIGASE; ZINC ION;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMOSTABILITY; TRANSITION TEMPERATURE;

ASPARTIC ACID; BRCA1 PROTEIN; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; FEMALE; GLUTAMIC ACID; HUMANS; MASS SPECTROMETRY; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP; UBIQUITIN-PROTEIN LIGASES; X-RAY ABSORPTION SPECTROSCOPY; ZINC;

EID: 79951553885 PISSN: 09498257 EISSN: None Source Type: Journal
DOI: 10.1007/s00775-010-0718-y Document Type: Article

Times cited : (13)

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