about
APLF promotes the assembly and activity of non-homologous end joining protein complexesFunctions of PARylation in DNA Damage Repair PathwaysChromatin Dynamics in Vivo: A Game of Musical ChairsThe role of ADP-ribosylation in regulating DNA interstrand crosslink repairHPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation ActivitySerine ADP-Ribosylation Depends on HPF1Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome cNonhomologous end joining: a good solution for bad endsMolecular Insights into Poly(ADP-ribose) Recognition and Processing.Non-homologous end joining: emerging themes and unanswered questions.Structural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a timeNew facets in the regulation of gene expression by ADP-ribosylation and poly(ADP-ribose) polymerases.HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth.Non-homologous end joining: Common interaction sites and exchange of multiple factors in the DNA repair process.Histone chaperones in nucleosome assembly and human diseaseHistone chaperones in Arabidopsis and rice: genome-wide identification, phylogeny, architecture and transcriptional regulation.ATP-dependent chromatin remodeling in the DNA-damage response.Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c.Regulation of chromatin structure by poly(ADP-ribosyl)ation.The right place at the right time: chaperoning core histone variantsThe PIN domain of EXO1 recognizes poly(ADP-ribose) in DNA damage response.Chromatin plasticity in response to DNA damage: The shape of things to come.Reshaping chromatin after DNA damage: the choreography of histone proteins.An Intrinsically Disordered APLF Links Ku, DNA-PKcs, and XRCC4-DNA Ligase IV in an Extended Flexible Non-homologous End Joining Complex.Chromatin and the DNA damage response: the cancer connection.Epigenetic regulation of genomic integrity.On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1.Resolution of complex ends by Nonhomologous end joining - better to be lucky than good?Detection and repair of ionizing radiation-induced DNA double strand breaks: new developments in nonhomologous end joining.Macro domains as metabolite sensors on chromatin.The recognition and removal of cellular poly(ADP-ribose) signals.At the intersection of non-coding transcription, DNA repair, chromatin structure, and cellular senescence.Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response.Non-homologous end joining often uses microhomology: implications for alternative end joining.The PARP3- and ATM-dependent phosphorylation of APLF facilitates DNA double-strand break repair.New factors in mammalian DNA repair-the chromatin connection.Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.The Herpesvirus Nuclear Egress Complex Component, UL31, Can Be Recruited to Sites of DNA Damage Through Poly-ADP Ribose Binding.What Combined Measurements From Structures and Imaging Tell Us About DNA Damage Responses.MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD+ consumption.
P2860
Q24304501-DFDA2B93-C925-4F1D-A252-FD425241FEA6Q26744796-49B5FD03-73A8-49C6-87C0-855627C5B7C6Q26799305-B4E8CF12-16AF-4F2A-A410-EC09347C7A72Q27727978-EA08885F-DDFC-47BC-BDEC-652D334536FBQ28118267-95BE709A-1FDB-423D-9A6F-2F6E644FC963Q28975776-6FC7BC43-7FBA-45E8-B5C9-9EDF6CEBBF7CQ33558339-97940F55-7C8E-4799-B116-EB4EB1CE31EAQ33625010-2D6AB036-E57E-4812-ABF6-94485F6D6988Q33649646-C7F6F158-4524-43D3-9244-D9A99DBB224DQ33854272-664BD598-EC73-433F-8C6D-68387B5E0B8BQ33914715-07FD73FC-BBC0-443E-9EED-EE027FED7011Q34042969-41D8A2A0-D16E-4009-9E55-08DF058627BFQ34461782-FD84E15D-DCC1-4036-AC00-BC82D918A974Q34550224-1924EDAD-41BC-4069-B6ED-9CE67EF1FD68Q34647041-C2B4FEDC-7F05-4D31-8F70-97419B820F6EQ35169968-DC8E0025-E1FB-4EA3-90D1-34E44A872F0AQ35744850-10A168D8-08BA-45E0-BC55-9B51621CE7FBQ35961467-A321CC83-204D-4801-BA8B-83EF246FA497Q36204365-A3256DFA-A0CB-4724-871B-42785DF49074Q36270857-FD306070-0C85-4730-BFA5-689614428FA8Q36370917-B198DE87-6754-4EE9-B6A9-FC5C051F576EQ37418006-C222D6AD-884B-4843-9AE2-DEEDCFF4F27CQ37418010-19DF938B-B403-4BF4-B3A9-EB6F8268A2CEQ37551399-41F5CA44-3869-4EA6-A798-5A63FB43CE29Q37904144-00CB6174-D96C-4D77-A5FB-0B37EA901CC2Q37976267-FB73CF38-FBA9-4546-BC9C-DFDCD7DF7130Q37990715-B4DB5681-7D5C-47BA-84B9-E75A0E33525CQ38070431-6A8203CA-7169-4865-BBE8-836284ECE3B5Q38083939-4C51E1A1-6426-4FF5-8B06-F3E132DF507CQ38086003-6778874E-795E-4A0D-A9E6-3B24B3199C67Q38109700-8F5705B7-313A-45FD-B297-23B81A9509D3Q38130677-710E38C5-D15A-400E-9367-9D53F342AE28Q38155805-D7F39841-8AAF-4DC2-923D-B8CA8F7CDAB3Q38194755-B42D3C56-317C-4E4B-9B11-2DE69F637330Q39187205-3CB0BEBF-53F0-4F4F-8C5F-899FEF5813AFQ39231599-DDADD39A-3319-4AA7-8FDE-652AD3EBFF6DQ39370444-2E6F5E06-2FF0-4557-A93A-29CEF5CE2E09Q40200374-B78C3FF1-2801-4ED9-850C-8A8253B92E04Q41319392-298EE5EE-D370-4783-82CF-6D063765EE90Q42516548-63C3F4A7-0042-48FD-BD24-77D731A4AC23
P2860
description
2011 nî lūn-bûn
@nan
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
2011年论文
@zh
2011年论文
@zh-cn
name
DNA repair factor APLF is a histone chaperone.
@ast
DNA repair factor APLF is a histone chaperone.
@en
type
label
DNA repair factor APLF is a histone chaperone.
@ast
DNA repair factor APLF is a histone chaperone.
@en
prefLabel
DNA repair factor APLF is a histone chaperone.
@ast
DNA repair factor APLF is a histone chaperone.
@en
P2093
P2860
P50
P1433
P1476
DNA repair factor APLF is a histone chaperone.
@en
P2093
Dragana Ahel
Nicola Wiechens
Pawan Vinod Mehrotra
Rolf Kraehenbuehl
P2860
P356
10.1016/J.MOLCEL.2010.12.008
P577
2011-01-01T00:00:00Z