Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C. (Q36858513)

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scientific article published on 18 March 2016

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English	Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C.	scientific article published on 18 March 2016

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scholarly article

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Europe PubMed Central

PMC publication ID

16 August 2017

Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C. (English)

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16 August 2017

crystal structure

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based on heuristic

inferred from title

Anne-Claude Gingras

15

object named as

Anne-Claude Gingras

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Jennifer E. Golden

object named as

Jennifer E Golden

13

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author name string

Debasish Chattopadhyay

1

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16 August 2017

Mark R Swingle

2

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16 August 2017

Edward A Salter

3

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Eric Wood

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Brandon D'Arcy

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Catherine Zivanov

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Kevin Abney

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Alla Musiyenko

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Scott F Rusin

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Arminja Kettenbach

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Larry Yet

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Chad E Schroeder

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Wade H Dunham

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Surajit Banerjee

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David Forbes

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Andrzej Wierzbicki

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Richard E Honkanen

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publication date

18 March 2016

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Biochemical Pharmacology

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109

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14-26

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16 August 2017

Quantitative phosphoproteomics reveals new roles for the protein phosphatase PP6 in mitotic cells

1 reference

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Development and validation of a robust and sensitive assay for the discovery of selective inhibitors for serine/threonine protein phosphatases PP1α (PPP1C) and PP5 (PPP5C).

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Protein Ser/Thr/Tyr phosphorylation in the Archaea

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Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation

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A simple procedure for preparation of N-thiazol, thiadiazol, pyridyl and sulfanylamidocantharidinimines analogues and evaluation of their cytotoxicities against human HL-60, MCF7, Neuro-2a and A549 carcinoma cell

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REFMAC5 for the refinement of macromolecular crystal structures

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Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin

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Structure-activity relationship studies of fostriecin, cytostatin, and key analogs, with PP1, PP2A, PP5, and( beta12-beta13)-chimeras (PP1/PP2A and PP5/PP2A), provide further insight into the inhibitory actions of fostriecin family inhibitors

1 reference

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Crystal Structures of Protein Phosphatase-1 Bound to Nodularin-R and Tautomycin: A Novel Scaffold for Structure-based Drug Design of Serine/Threonine Phosphatase Inhibitors

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Identifiers

10.1016/J.BCP.2016.03.011

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

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