Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates - Test2 - elhamkhani - TriplyDB

Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates

Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates

http://www.wikidata.org/entity/Q28294871

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Signalling of the BCR is regulated by a lipid rafts-localised transcription factor, Bright.Regulation of Cullin-RING ubiquitin ligase 1 by Spliceosome-associated protein 130 (SAP130)PARP-1 transcriptional activity is regulated by sumoylation upon heat shock Chromatin remodeling proteins interact with pericentrin to regulate centrosome integrity SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage A proteomic characterization of factors enriched at nascent DNA molecules Human MMS21/NSE2 is a SUMO ligase required for DNA repair SUMO modification of human XRCC4 regulates its localization and function in DNA double-strand break repair.Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation Phosphorylation-facilitated sumoylation of MEF2C negatively regulates its transcriptional activity Base Excision Repair, a Pathway Regulated by Posttranslational Modifications Scc1 sumoylation by Mms21 promotes sister chromatid recombination through counteracting Wapl Versatile recombinant SUMOylation system for the production of SUMO-modified protein SYT-SSX1 (synovial sarcoma translocated) regulates PIASy ligase activity to cause overexpression of NCOA3 protein SUMOsp: a web server for sumoylation site prediction A novel method for high accuracy sumoylation site prediction from protein sequences ZNF198 stabilizes the LSD1-CoREST-HDAC1 complex on chromatin through its MYM-type zinc fingers Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation.SUMO Wrestles with Recombination A bird's-eye view of post-translational modifications in the spliceosome and their roles in spliceosome dynamics Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics.Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.SUMOylation of GTF2IRD1 regulates protein partner interactions and ubiquitin-mediated degradation.Finishing touches: post-translational modification of protein factors involved in mammalian pre-mRNA 3' end formation.Caveolin-3 undergoes SUMOylation by the SUMO E3 ligase PIASy: sumoylation affects G-protein-coupled receptor desensitization Profiles of SUMO and ubiquitin conjugation in an Alzheimer's disease model Systematic Analysis of the Genetic Variability That Impacts SUMO Conjugation and Their Involvement in Human Diseases.Ubiquitin proteolytic system: focus on SUMO.A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification.It takes two to tango: Ubiquitin and SUMO in the DNA damage response.Profiling of ubiquitin-like modifications reveals features of mitotic control.RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins.Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3.Ubiquitin-family modifications of topoisomerase I in camptothecin-treated human breast cancer cells.SUMO and Alzheimer's disease.Transcriptional Suppression by Transient Recruitment of ARIP4 to Sumoylated nuclear receptor Ad4BP/SF-1.Sumoylation and human disease pathogenesis The ubiquitin-proteasome system in cancer, a major player in DNA repair. Part 1: post-translational regulation.

P2860

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P2860

Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates

http://www.wikidata.org/entity/Q28294871

description

2005 nî lūn-bûn

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2005 թվականի փետրվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Systematic identification and ...... uitin-like modifier substrates

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Systematic identification and ...... uitin-like modifier substrates

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Systematic identification and ...... uitin-like modifier substrates

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type

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Systematic identification and ...... uitin-like modifier substrates

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Systematic identification and ...... uitin-like modifier substrates

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Systematic identification and ...... uitin-like modifier substrates

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prefLabel

Systematic identification and ...... uitin-like modifier substrates

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Systematic identification and ...... uitin-like modifier substrates

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Systematic identification and ...... uitin-like modifier substrates

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P1433

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P1433

Journal of Biological Chemistry

P1476

Systematic identification and ...... uitin-like modifier substrates

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P2093

Christian B Gocke

http://www.w3.org/2001/XMLSchema#string

Hongtao Yu

http://www.w3.org/2001/XMLSchema#string

Jungseog Kang

http://www.w3.org/2001/XMLSchema#string

P2860

Differential regulation of sentrinized proteins by a novel sentrin-specific protease

Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo

Association of the human SUMO-1 protease SENP2 with the nuclear pore

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1

Complex protein interactions within the human polyadenylation machinery identify a novel component

N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome

SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression

SUMOylation regulates nucleo-cytoplasmic shuttling of Elk-1

SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex

P304

5004-12

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scholarly article

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10.1074/JBC.M411718200

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6

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P478

280

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2005-02-11T00:00:00Z

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8165074

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15561718

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P921

MSL complex subunit 1