Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases - Test2 - elhamkhani - TriplyDB

Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases

Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases

http://www.wikidata.org/entity/Q24302258

about

Large-scale structural analysis of the classical human protein tyrosine phosphatome Structural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase † , ‡Visualizing Active-Site Dynamics in Single Crystals of HePTP: Opening of the WPD Loop Involves Coordinated Movement of the E Loop Striatal-enriched protein tyrosine phosphatase in Alzheimer's disease.Inhibitor of the tyrosine phosphatase STEP reverses cognitive deficits in a mouse model of Alzheimer's disease Interface analysis of the complex between ERK2 and PTP-SL Cdc25B dual-specificity phosphatase inhibitors identified in a high-throughput screen of the NIH compound library.The protein tyrosine phosphatase receptor type R gene is an early and frequent target of silencing in human colorectal tumorigenesis Therapeutic implications for striatal-enriched protein tyrosine phosphatase (STEP) in neuropsychiatric disorders.Inhibition of hematopoietic protein tyrosine phosphatase augments and prolongs ERK1/2 and p38 activation Missense Variant in MAPK Inactivator PTPN5 Is Associated with Decreased Severity of Post-Burn Hypertrophic Scarring Protein tyrosine phosphatases: structure-function relationships.The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase.Protein tyrosine phosphatases as drug targets: strategies and challenges of inhibitor development.Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.Protein tyrosine phosphatases in health and disease.A common STEP in the synaptic pathology of diverse neuropsychiatric disorders.Gene expression profiling of post-mortem orbitofrontal cortex in violent suicide victims.Crystallization of PTP Domains.Effects of protonation state of Asp181 and position of active site water molecules on the conformation of PTP1B.An iminocoumarin-based fluorescent probe for the selective detection of dual-specific protein tyrosine phosphatases.Reduced body weight in male Tspan8-deficient mice.X-ray Characterization and Structure-Based Optimization of Striatal-Enriched Protein Tyrosine Phosphatase Inhibitors.Sequence-specific backbone ¹H, ¹³C and ¹⁵N assignments of the 34 kDa catalytic domain of PTPN5 (STEP).

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Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases

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2006 nî lūn-bûn

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2006年論文

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Crystal structures and inhibit ...... protein tyrosine phosphatases

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Crystal structures and inhibit ...... protein tyrosine phosphatases

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Andrew Turnbull

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Brian Marsden

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Emilie Ugochukwu

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Emma Longman

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Jens Peter von Kries

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Jeyanthy Eswaran

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Judit E Debreczeni

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P2860

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

Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)

PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.

Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation

Crystal structure of human protein tyrosine phosphatase 1B

Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization

The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu

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

Likelihood-enhanced fast rotation functions

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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10.1042/BJ20051931

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3

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395

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Alastair J. Barr

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2006-05-01T00:00:00Z

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16441242

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phosphotyrosine residue binding

Protein tyrosine phosphatase non-receptor type 5

crystal structure

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1462698

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