Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
about
Functions of PARylation in DNA Damage Repair PathwaysInterplay between Ubiquitin, SUMO, and Poly(ADP-Ribose) in the Cellular Response to Genotoxic StressReal Estate in the DNA Damage Response: Ubiquitin and SUMO Ligases Home in on DNA Double-Strand BreaksReaders of poly(ADP-ribose): designed to be fit for purposeRING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitinationRecognition of the iso-ADP-ribose moiety in poly(ADP-ribose) by WWE domains suggests a general mechanism for poly(ADP-ribosyl)ation-dependent ubiquitinationBase Excision Repair, a Pathway Regulated by Posttranslational ModificationsADP-ribosyltransferases and poly ADP-ribosylationMolecular Insights into Poly(ADP-ribose) Recognition and Processing.Poly(ADP-ribose) polymerase 1 (PARP1) associates with E3 ubiquitin-protein ligase UHRF1 and modulates UHRF1 biological functionsNeuroprotectin D1 upregulates Iduna expression and provides protection in cellular uncompensated oxidative stress and in experimental ischemic stroke.Elovanoids are novel cell-specific lipid mediators necessary for neuroprotective signaling for photoreceptor cell integrityNew facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases.Modulation of poly(ADP-ribose) polymerase-1 (PARP-1)-mediated oxidative cell injury by ring finger protein 146 (RNF146) in cardiac myocytesThe level of Ets-1 protein is regulated by poly(ADP-ribose) polymerase-1 (PARP-1) in cancer cells to prevent DNA damage.The guanine-quadruplex structure in the human c-myc gene's promoter is converted into B-DNA form by the human poly(ADP-ribose)polymerase-1.Poly(ADP-ribose) contributes to an association between poly(ADP-ribose) polymerase-1 and xeroderma pigmentosum complementation group A in nucleotide excision repair.A quantitative assay reveals ligand specificity of the DNA scaffold repair protein XRCC1 and efficient disassembly of complexes of XRCC1 and the poly(ADP-ribose) polymerase 1 by poly(ADP-ribose) glycohydrolase.Analysis of poly(ADP-Ribose) polymerases in Arabidopsis telomere biology.Cyclic AMP signaling reduces sirtuin 6 expression in non-small cell lung cancer cells by promoting ubiquitin-proteasomal degradation via inhibition of the Raf-MEK-ERK (Raf/mitogen-activated extracellular signal-regulated kinase/extracellular signal-Ring finger protein 146/Iduna is a poly(ADP-ribose) polymer binding and PARsylation dependent E3 ubiquitin ligase.Tankyrases Promote Homologous Recombination and Check Point Activation in Response to DSBs.Scaffold function of long non-coding RNA HOTAIR in protein ubiquitinationDoxorubicin-induced necrosis is mediated by poly-(ADP-ribose) polymerase 1 (PARP1) but is independent of p53.PHRF1 promotes genome integrity by modulating non-homologous end-joining.Cocaine elicits autophagic cytotoxicity via a nitric oxide-GAPDH signaling cascadeDamage response of XRCC1 at sites of DNA single strand breaks is regulated by phosphorylation and ubiquitylation after degradation of poly(ADP-ribose).PARP1 regulates the protein stability and proapoptotic function of HIPK2.Overexpression of RNF146 in non-small cell lung cancer enhances proliferation and invasion of tumors through the Wnt/β-catenin signaling pathwayTXNL1-XRCC1 pathway regulates cisplatin-induced cell death and contributes to resistance in human gastric cancer.PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes.RNF146 Inhibits Excessive Autophagy by Modulating the Wnt-β-Catenin Pathway in Glutamate Excitotoxicity Injury.On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1.New synaptic and molecular targets for neuroprotection in Parkinson's disease.Reprogramming cellular events by poly(ADP-ribose)-binding proteinsStructural biology of the writers, readers, and erasers in mono- and poly(ADP-ribose) mediated signaling.The recognition and removal of cellular poly(ADP-ribose) signals.Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response.ADP-ribosylation: activation, recognition, and removalRegulation of Wnt/β-catenin signaling by posttranslational modifications
P2860
Q26744796-B238D377-6814-4F76-8AF9-B8401D3A16D5Q26752447-D47BF4D0-10F5-4A0D-B0A0-B32CB08C4CD9Q26752453-C6487D62-5157-4D98-BF32-849E8B45530EQ26775561-F9D678C2-C59C-494C-803A-02E910072518Q26850008-C2ECC67D-9DD4-417F-A9EA-AD6C6EE38F3BQ27676844-FB25FB5E-571C-4182-864F-F1E85E2ECD68Q28078441-E944C050-962E-45E6-B24F-62A98FF1858EQ28082350-8916E5BA-56AC-47E6-B4D1-057DBAE15BE1Q33649646-BCB75727-3D7B-4C4B-8725-690EA00788CBQ33718499-5B315DC1-CA87-4A72-B5A2-7A121222DEE3Q33721387-BDEB47DB-8CBF-468E-9BD6-9C5B1BD219F6Q33902944-38BA6276-2934-4808-9AE1-01FABBDA27E1Q34042969-26961940-0A01-40ED-8C60-AB02ADAB911DQ34129753-D80818CE-A4D4-413F-93E9-215544308AD6Q34327567-37195995-8666-4B95-A2B6-1BD4902053C0Q34374607-04F6365F-18D5-4BA1-AF58-FBC2EAB4C2A8Q34434424-BC91F10C-B138-4B2D-B879-EEF7A8AC3954Q35055636-47B2E462-15A9-4EFD-A9AE-E7DF80735852Q35097621-D6E83068-D99C-48EF-967F-9681FEE2D9C8Q35351777-97C64D16-013F-4D84-95BC-143202B7AFDFQ35751718-6661ADF7-CE33-4476-A81D-04E04B626ECCQ35914314-F8399F5D-1F2B-4707-AC1B-86A406A630E3Q36015904-9B3727D1-A252-4548-B3E4-C203CA351DD2Q36237705-45F4EADA-EAE6-4283-83FD-941126E84ED3Q36293289-02726820-1D30-4F2B-A0D7-D597D87DA00AQ36563394-5D8E7453-EC48-4E20-A3E1-BE2F8DB2BA7FQ37201500-DCAD1407-1A45-4EA7-A8E1-E2DD479856A7Q37465994-1212A43E-E41F-45FC-8923-BFEA1511CB43Q37479033-A703AFAF-E7EF-491E-B7D4-88745346123EQ37620658-4E3AF48B-4CFA-4BF7-AA05-69E8F19FD686Q37661664-F50EEEDD-A491-46A2-BCD1-78C5742ACD52Q37681289-B4FA42B2-9CDC-43F3-A471-89FBFF6B89C4Q37990715-B71833D4-2E06-4D0A-B736-06E045E5A76BQ38038559-D1BD5441-A2E7-411E-83D6-020592F20CD8Q38069879-CD8149D1-B2F0-4EFB-9665-4DBB15742E46Q38086332-99C4B016-C99B-42DC-BF5A-27A9D1A817DEQ38109700-E5288567-0BF7-4C31-BAFA-D688EB6ED654Q38155805-04E8D2AA-666E-472F-83A7-5B89884AED1BQ38189514-FE48261C-8AD8-4660-A0C4-E21C648848A9Q38193259-F787061D-912B-44A8-8E5D-AC5B57C1986E
P2860
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@ast
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@en
type
label
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@ast
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@en
prefLabel
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@ast
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@en
P2093
P2860
P356
P1476
Iduna is a poly(ADP-ribose) (PAR)-dependent E3 ubiquitin ligase that regulates DNA damage
@en
P2093
Byoung Dae Lee
Guy G Poirier
Han Seok Ko
Ho Chul Kang
Jean-Philippe Gagné
Joo-Ho Shin
Shaida A Andrabi
Valina L Dawson
Yun-Il Lee
Yunjong Lee
P2860
P304
14103-14108
P356
10.1073/PNAS.1108799108
P407
P577
2011-08-08T00:00:00Z