Reversible oxidation of HIV-2 protease.
Davis
David A
DA
HIV and AIDS Malignancy Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Newcomb
Fonda M
FM
Moskovitz
Jackob
J
Fales
Henry M
HM
Levine
Rodney L
RL
Yarchoan
Robert
R
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D016333:HIV Protease; D015498:HIV-2 / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D006861:Hydrogen Peroxide; D066298:In Vitro Techniques; D013058:Mass Spectrometry; D008715:Methionine / Q000737:chemistry; D051150:Methionine Sulfoxide Reductases; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D010446:Peptide Fragments; D011994:Recombinant Proteins; D008715:Methionine; D006861:Hydrogen Peroxide; D010088:Oxidoreductases; D051150:Methionine Sulfoxide Reductases; C027219:methionine sulfoxide reductase; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C065184:p16 protease, Human immunodeficiency virus 2