Reversible Oxidative Modification as a Mechanism for Regulating Retroviral Protease Dimerization and Activation
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چکیده
منابع مشابه
Reversible oxidative modification as a mechanism for regulating retroviral protease dimerization and activation.
Human immunodeficiency virus protease activity can be regulated by reversible oxidation of a sulfur-containing amino acid at the dimer interface. We show here that oxidation of this amino acid in human immunodeficiency virus type 1 protease prevents dimer formation. Moreover, we show that human T-cell leukemia virus type 1 protease can be similarly regulated through reversible glutathionylation...
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Angiotensin II (Ang II) inhibits the cardiac sarcolemmal Na(+)-K(+) pump via protein kinase (PK)C-dependent activation of NADPH oxidase. We examined whether this is mediated by oxidative modification of the pump subunits. We detected glutathionylation of beta(1), but not alpha(1), subunits in rabbit ventricular myocytes at baseline. beta(1) Subunit glutathionylation was increased by peroxynitri...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 2003
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.77.5.3319-3325.2003