Inactivation of Protein Tyrosine Phosphatases by Peracids Correlates with the Hydrocarbon Chain Length | Zendy

Alicja KubanJankowska | Zendy; Magdalena GórskaPonikowska | Zendy; Jack A. Tuszyński | Zendy; Cassandra D. M. Churchill | Zendy; Philip Winter | Zendy; Mariusz Kłobukowski | Zendy; Michał Woźniak | Zendy

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Inactivation of Protein Tyrosine Phosphatases by Peracids Correlates with the Hydrocarbon Chain Length

Author(s) -

Alicja KubanJankowska,

Magdalena GórskaPonikowska,

Jack A. Tuszyński,

Cassandra D. M. Churchill,

Philip Winter,

Mariusz Kłobukowski,

Michał Woźniak

Publication year - 2015

Publication title -

cellular physiology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.486

H-Index - 87

eISSN - 1421-9778

pISSN - 1015-8987

DOI - 10.1159/000430280

Subject(s) - enzyme , chemistry , biochemistry , protein tyrosine phosphatase , active site , hydrogen peroxide , recombinant dna , phosphatase , jurkat cells , tyrosine , biology , t cell , immune system , immunology , gene

Protein tyrosine phosphatases are crucial enzymes controlling numerous physiological and pathophysiological events and can be regulated by oxidation of the catalytic domain cysteine residue. Peracids are highly oxidizing compounds, and thus may induce inactivation of PTPs. The aim of the present study was to evaluate the inhibitory effect of peracids with different length of hydrocarbon chain on the activity of selected PTPs.

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