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- W2496188466 endingPage "1355" @default.
- W2496188466 startingPage "1339" @default.
- W2496188466 abstract "Originally identified as a low molecular weight acid phosphatase, LMW-PTP is actually a protein tyrosine phosphatase that acts on many phosphotyrosine-containing cellular proteins that are primarily involved in signal transduction. Differences in sequence, structure, and substrate recognition as well as in subcellular localization in different organisms enable LMW-PTP to exert many different functions. In fact, during evolution, the LMW-PTP structure adapted to perform different catalytic actions depending on the organism type. In bacteria, this enzyme is involved in the biosynthesis of group 1 and 4 capsules, but it is also a virulence factor in pathogenic strains. In yeast, LMW-PTPs dephosphorylate immunophilin Fpr3, a peptidyl-prolyl-cis-trans isomerase member of the protein chaperone family. In humans, LMW-PTP is encoded by the ACP1 gene, which is composed of three different alleles, each encoding two active enzymes produced by alternative RNA splicing. In animals, LMW-PTP dephosphorylates a number of growth factor receptors and modulates their signalling processes. The involvement of LMW-PTP in cancer progression and in insulin receptor regulation as well as its actions as a virulence factor in a number of pathogenic bacterial strains may promote the search for potent, selective and bioavailable LMW-PTP inhibitors." @default.
- W2496188466 created "2016-08-23" @default.
- W2496188466 creator A5003476805 @default.
- W2496188466 creator A5020915701 @default.
- W2496188466 creator A5039489092 @default.
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- W2496188466 creator A5055832234 @default.
- W2496188466 creator A5057913154 @default.
- W2496188466 creator A5060186437 @default.
- W2496188466 date "2016-10-01" @default.
- W2496188466 modified "2023-10-16" @default.
- W2496188466 title "Low molecular weight protein tyrosine phosphatase: Multifaceted functions of an evolutionarily conserved enzyme" @default.
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