Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket

Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket

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http://www.wikidata.org/entity/Q24324478
Large-scale structural analysis of the classical human protein tyrosine phosphatomeKinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphataseStructural Basis for Selective Inhibition of Mycobacterium tuberculosis Protein Tyrosine Phosphatase PtpBVisualizing Active-Site Dynamics in Single Crystals of HePTP: Opening of the WPD Loop Involves Coordinated Movement of the E LoopProtein tyrosine phosphatases as potential therapeutic targets.Opposite roles of FAP-1 and dynamin in the regulation of Fas (CD95) translocation to the cell surface and susceptibility to Fas ligand-mediated apoptosisRational design of allosteric-inhibition sites in classical protein tyrosine phosphatases.Role of TAPP1 and TAPP2 adaptor binding to PtdIns(3,4)P2 in regulating insulin sensitivity defined by knock-in analysis.The PDZ binding motif of human papillomavirus type 16 E6 induces PTPN13 loss, which allows anchorage-independent growth and synergizes with ras for invasive growth.PTPL1: a large phosphatase with a split personality.Protein tyrosine phosphatases: structure-function relationships.miR-26a desensitizes non-small cell lung cancer cells to tyrosine kinase inhibitors by targeting PTPN13.A missense methionine mutation augments catalytic activity but reduces thermal stability in two protein tyrosine phosphatases.Impaired PTPN13 phosphatase activity in spontaneous or HPV-induced squamous cell carcinomas potentiates oncogene signaling through the MAP kinase pathwayKinetic, inhibition and structural studies on 3-oxoacyl-ACP reductase from Plasmodium falciparum, a key enzyme in fatty acid biosynthesis.An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering
P2860

Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket

Item
http://www.wikidata.org/entity/Q24324478
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2005年論文
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Crystal structure of the PTPL1 ...... e substrate recognition pocket
@ast
Crystal structure of the PTPL1 ...... e substrate recognition pocket
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Crystal structure of the PTPL1 ...... e substrate recognition pocket
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Crystal structure of the PTPL1 ...... e substrate recognition pocket
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type
label
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@ast
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@en
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@en-gb
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@nl
prefLabel
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@ast
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@en
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@en-gb
Crystal structure of the PTPL1 ...... e substrate recognition pocket
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P1433
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P2093
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P304
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P1476
Crystal structure of the PTPL1 ...... e substrate recognition pocket
@en
P2093
P2860
P304
P31
P3181
P356
P407
P433
P478
P50
P577
P698
P921