Literature DB >> 19022671

Biologically relevant chemical properties of peroxymonophosphate (=O3POOH).

Jason N LaButti1, Kent S Gates.   

Abstract

It has been suggested that peroxymonophosphate could serve as an endogenous hydrogen peroxide-derived regulator of cellular protein tyrosine phosphatase activity under physiological or pathophysiological conditions. To facilitate further consideration of the potential role of peroxymonophosphate in biological systems we present studies related to the preparation, characterization, stability, and fluorometric detection of this agent.

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Year:  2008        PMID： 19022671      PMCID： PMC3268127          DOI： 10.1016/j.bmcl.2008.10.133

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN： 0960-894X            Impact factor:   2.823


  26 in total

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3.  Redox regulation of protein tyrosine phosphatase 1B by peroxymonophosphate (=O3POOH).

Authors:  Jason N LaButti; Goutam Chowdhury; Thomas J Reilly; Kent S Gates
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5.  Thiol-dependent recovery of catalytic activity from oxidized protein tyrosine phosphatases.

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Journal:  Biochemistry       Date:  2013-09-04       Impact factor: 3.162

6.  Inactivation of protein tyrosine phosphatases by oltipraz and other cancer chemopreventive 1,2-dithiole-3-thiones.

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Review 7.  Toward selective detection of reactive oxygen and nitrogen species with the use of fluorogenic probes--Limitations, progress, and perspectives.

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Review 9.  Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.

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10.  Evaluation of borinic acids as new, fast hydrogen peroxide-responsive triggers.

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