553667-91-7Relevant academic research and scientific papers
Modification of the N-terminus of peptidomimetic protein tyrosine phosphatase 1B (PTP1B) inhibitors: Identification of analogues with cellular activity
Larsen, Scott D.,Stevens, F. Craig,Lindberg, Thomas J.,Bodnar, Paul M.,O'Sullivan, Theresa J.,Schostarez, Heinrich J.,Palazuk, Barbara J.,Bleasdale, John E.
, p. 971 - 975 (2007/10/03)
Low molecular weight peptidomimetic compounds based on O-malonyl tyrosine and O-carboxymethyl salicylic acid are potent inhibitors of PTP1B. Modifications of the N-terminal Boc-Phe moiety were undertaken in an effort to improve physical chemical properties and to achieve cellular activity. Although Phe ultimately proved to be the optimal N-terminal amino acid, several viable replacements for the Boc group were identified, two of which afforded analogues that were effective at enhancing the insulin-stimulated uptake of 2-deoxyglucose by L6 myocytes.
Synthesis and biological activity of a novel class of small molecular weight peptidomimetic competitive inhibitors of protein tyrosine phosphatase 1B
Larsen, Scott D.,Barf, Tjeerd,Liljebris, Charlotta,May, Paul D.,Ogg, Derek,O'Sullivan, Theresa J.,Palazuk, Barbara J.,Schostarez, Heinrich J.,Stevens, F. Craig,Bleasdale, John E.
, p. 598 - 622 (2007/10/03)
Protein tyrosine phosphatase 1B (PTP1B) negatively regulates insulin signaling in part by dephosphorylating key tyrosine residues within the regulatory domain of the β-subunit of the insulin receptor (IR), thereby attenuating receptor tyrosine kinase acti
Inhibitors of protein tyrosine phosphatase
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Page column 33,37, (2010/11/29)
The present invention comprises small molecular weight, non-peptidic inhibitors of formula I and II of Protein Tyrosine Phosphatase 1 (PTP1) which are useful for the treatment and/or prevention of Non-Insulin Dependent Diabetes Mellitus (NIDDM).
