Human RNase H1 activity is regulated by a unique redox switch formed between adjacent cysteines

Journal of Biological Chemistry

Volumn 278, Issue 17, 2003, Pages 14906-14912

  Lima, Walt F ^a   Wu, Hongjiang ^b   Nichols, Josh G ^b   Manalili, Sherilynn M ^b   Drader, Jared J ^b   Hofstadler, Steven A ^b   Crooke, Stanley T ^b  

^a ISIS PHARMACEUTICALS   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; BIOCATALYSTS; CHEMICAL BONDS; ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; OXIDATION; REDOX REACTIONS; SUBSTRATES;

ELECTROSPRAY IONIZATION;

BIOCHEMISTRY;

ALANINE; ARGININE; ASPARTIC ACID; CYSTEINE DERIVATIVE; MUTANT PROTEIN; N ETHYLMALEIMIDE; PANCREATIC RIBONUCLEASE; TRYPSIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CYCLOTRON; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DEGRADATION; ENZYME MECHANISM; ENZYME REGULATION; ENZYME SUBSTRATE COMPLEX; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; MASS SPECTROMETRY; OXIDATION; OXIDATION REDUCTION REACTION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CYSTEINE; DISULFIDES; ENZYME ACTIVATION; HUMANS; KINETICS; MERCAPTOETHANOL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; RIBONUCLEASE H, CALF THYMUS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 0037675863     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M211279200     Document Type: Article

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