Structural basis for inhibition of protein-tyrosine phosphatase 1B by isothiazolidinone heterocyclic phosphonate mimetics. (Q54457522)

30 May 2018

title

Structural basis for inhibition of protein-tyrosine phosphatase 1B by isothiazolidinone heterocyclic phosphonate mimetics. (English)

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author name string

Paul J Ala

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30 May 2018

Lucie Gonneville

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Milton C Hillman

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Mary Becker-Pasha

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Min Wei

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Brian G Reid

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Ronald Klabe

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Eddy W Yue

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Brian Wayland

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Brent Douty

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Padmaja Polam

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Zelda Wasserman

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Michael Bower

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Andrew P Combs

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Timothy C Burn

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Gregory F Hollis

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Richard Wynn

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language of work or name

English

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publication date

17 August 2006

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Journal of Biological Chemistry

published in

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volume

281

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issue

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page(s)

32784-32795

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30 May 2018

The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence

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Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene

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Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice

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PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice

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Crystal structure of human protein tyrosine phosphatase 1B

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Protein tyrosine phosphatase 1B inhibition: opportunities and challenges

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Recent advances in protein tyrosine phosphatase 1B inhibitors

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Inhibition of protein tyrosine phosphatase 1B as a potential treatment of diabetes and obesity

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Inhibitors for proteins endowed with catalytic and non-catalytic activity which recognize pTyr

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Inhibitors of protein tyrosine phosphatases: next-generation drugs?

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Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B

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Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B

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Structural and evolutionary relationships among protein tyrosine phosphatase domains

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Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design

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Structure of protein tyrosine phosphatase 1B in complex with inhibitors bearing two phosphotyrosine mimetics

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Phosphotyrosyl mimetics in the development of signal transduction inhibitors

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Structure-based design and discovery of protein tyrosine phosphatase inhibitors incorporating novel isothiazolidinone heterocyclic phosphotyrosine mimetics

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Potent benzimidazole sulfonamide protein tyrosine phosphatase 1B inhibitors containing the heterocyclic (S)-isothiazolidinone phosphotyrosine mimetic

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Discovery of a potent, selective protein tyrosine phosphatase 1B inhibitor using a linked-fragment strategy

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The Protein Data Bank

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Water-molecule network and active-site flexibility of apo protein tyrosine phosphatase 1B.

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Structure-based design of protein tyrosine phosphatase-1B inhibitors.

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The structure of PTP-1B in complex with a peptide inhibitor reveals an alternative binding mode for bisphosphonates

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Crystal structure of PTP1B complexed with a potent and selective bidentate inhibitor

21 January 2018

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Thermodynamic consequences of burial of polar and non-polar amino acid residues in the protein interior

21 January 2018

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The Entropic Cost of Bound Water in Crystals and Biomolecules

21 January 2018

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Synthesis and evaluation of potent and selective beta(3) adrenergic receptor agonists containing acylsulfonamide, sulfonylsulfonamide, and sulfonylurea carboxylic acid isosteres

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M606873200

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30 May 2018

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30 May 2018