A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity
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Genome-wide association study meta-analysis of chronic widespread pain: evidence for involvement of the 5p15.2 regionLabel-free quantitative proteomics and SAINT analysis enable interactome mapping for the human Ser/Thr protein phosphatase 5A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombinationA PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) proteinA positive role of mammalian Tip41-like protein, TIPRL, in the amino-acid dependent mTORC1-signaling pathway through interaction with PP2AAn integrated workflow for charting the human interaction proteome: insights into the PP2A systemPP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4A novel 4EHP-GIGYF2 translational repressor complex is essential for mammalian developmentA PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA replicationThe biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificityWhat goes on must come off: phosphatases gate-crash the DNA damage responseRegulation of pol III transcription by nutrient and stress signaling pathwaysPph3-Psy2 is a phosphatase complex required for Rad53 dephosphorylation and replication fork restart during recovery from DNA damage.Psy2 targets the PP4 family phosphatase Pph3 to dephosphorylate Mth1 and repress glucose transporter gene expression.The Basic Biology of PP2A in Hematologic Cells and MalignanciesPP4 is a gamma H2AX phosphatase required for recovery from the DNA damage checkpointThe metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factorSuppressor of MEK null (SMEK)/protein phosphatase 4 catalytic subunit (PP4C) is a key regulator of hepatic gluconeogenesisComputational and informatics strategies for identification of specific protein interaction partners in affinity purification mass spectrometry experimentsTAB4 stimulates TAK1-TAB1 phosphorylation and binds polyubiquitin to direct signaling to NF-kappaBProtein Ser/Thr phosphatases--the ugly ducklings of cell signalling.Analysis of all protein phosphatase genes in Aspergillus nidulans identifies a new mitotic regulator, fcp1Dephosphorylation enables the recruitment of 53BP1 to double-strand DNA breaks.Distinct phosphatases antagonize the p53 response in different phases of the cell cycleThe CRAPome: a contaminant repository for affinity purification-mass spectrometry data.Quantitative proteomic analysis of protein complexes: concurrent identification of interactors and their state of phosphorylation.PLATINUM SENSITIVE 2 LIKE impacts growth, root morphology, seed set, and stress responses.Analysis of protein complexes through model-based biclustering of label-free quantitative AP-MS data.Two phosphatidylinositol 4-kinases control lysosomal delivery of the Gaucher disease enzyme, β-glucocerebrosidase.Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactionsThe serine/threonine phosphatase PP4 is required for pro-B cell development through its promotion of immunoglobulin VDJ recombination.Centromeric binding and activity of Protein Phosphatase 4Regulation of Rfa2 phosphorylation in response to genotoxic stress in Candida albicans.Elongin C is a mediator of Notch4 activity in human renal tubule cells.Restricted protein phosphatase 2A targeting by Merkel cell polyomavirus small T antigen.DAPPER: a data-mining resource for protein-protein interactionsMEK1 and protein phosphatase 4 coordinate Dictyostelium development and chemotaxis.Protein phosphatases and their regulation in the control of mitosisTIPRL Inhibits Protein Phosphatase 4 Activity and Promotes H2AX Phosphorylation in the DNA Damage Response.Global tumor protein p53/p63 interactome: making a case for cisplatin chemoresistance.
P2860
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P248
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P2860
A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity
description
2005 nî lūn-bûn
@nan
2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@ast
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en-gb
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@nl
type
label
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@ast
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en-gb
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@nl
prefLabel
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@ast
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en-gb
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@nl
P2093
P2860
P50
P3181
P1476
A novel, evolutionarily conser ...... olved in cisplatin sensitivity
@en
P2093
Amy Sanchez
Brian Raught
Ernst Hafen
Marcel Zarske
Michael Caballero
Stanley Fields
P2860
P304
P3181
P356
10.1074/MCP.M500231-MCP200
P407
P577
2005-11-01T00:00:00Z