Structure-based design of selective and potent inhibitors of protein-tyrosine phosphatase beta (Q44801456)

6 December 2017

title

Structure-based design of selective and potent inhibitors of protein-tyrosine phosphatase beta (English)

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6 December 2017

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Ida Katrine Lund

1

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6 December 2017

Henrik Sune Andersen

2

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6 December 2017

Lars Fogh Iversen

3

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6 December 2017

Ole Hvilsted Olsen

4

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6 December 2017

Karin Bach Møller

5

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6 December 2017

Anja Kallesøe Pedersen

6

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6 December 2017

Yu Ge

7

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6 December 2017

Daniel D Holsworth

8

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6 December 2017

Michael J Newman

9

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6 December 2017

Frank U Axe

10

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6 December 2017

Niels Peter Hundahl Møller

11

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6 December 2017

language of work or name

English

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publication date

15 March 2004

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Journal of Biological Chemistry

6 December 2017

number of pages

10

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based on heuristic

inferred from page(s)

published in

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6 December 2017

volume

279

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6 December 2017

issue

23

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6 December 2017

page(s)

24226-24235

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PTP1B: from the sidelines to the front lines!

6 December 2017

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

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Structure-based design of a low molecular weight, nonphosphorus, nonpeptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B

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Discovery and SAR of a novel selective and orally bioavailable nonpeptide classical competitive inhibitor class of protein-tyrosine phosphatase 1B.

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

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

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Coordinated action of protein tyrosine phosphatases in insulin signal transduction

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Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B

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Antitumor and anticarcinogenic actions of Cpd 5: a new class of protein phosphatase inhibitor.

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Sodium stibogluconate is a potent inhibitor of protein tyrosine phosphatases and augments cytokine responses in hemopoietic cell lines

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2-(oxalylamino)-benzoic acid is a general, competitive inhibitor of protein-tyrosine phosphatases

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Structural and evolutionary relationships among protein tyrosine phosphatase domains

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Steric hindrance as a basis for structure-based design of selective inhibitors of protein-tyrosine phosphatases

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Protein tyrosine phosphatases: their role in insulin action and potential as drug targets.

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An overview of the protein tyrosine phosphatase superfamily

21 January 2018

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VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts

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Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers

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1002 protein phosphatases?

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21 January 2018

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Modification of the N-terminus of peptidomimetic protein tyrosine phosphatase 1B (PTP1B) inhibitors: identification of analogues with cellular activity

21 January 2018

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Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1).

21 January 2018

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The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn)

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Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2

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

21 January 2018

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

21 January 2018

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

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M313027200

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6 December 2017

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