Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
about
sameAs
Variant base excision repair proteins: contributors to genomic instabilityThe human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machineryUbiquitin ligase ARF-BP1/Mule modulates base excision repairIsolation of human Dna2 endonuclease and characterization of its enzymatic propertiesSIRT1 deacetylates APE1 and regulates cellular base excision repairStimulation of NEIL2-mediated oxidized base excision repair via YB-1 interaction during oxidative stressAPE1-dependent repair of DNA single-strand breaks containing 3'-end 8-oxoguanineRepair of oxidative DNA damage and cancer: recent progress in DNA base excision repairHuman AP endonuclease 1: a potential marker for the prediction of environmental carcinogenesis riskA proposal: Evolution of PCNA's role as a marker of newly replicated DNAProliferating cell nuclear antigen (PCNA): a key factor in DNA replication and cell cycle regulationTranscriptional regulatory functions of mammalian AP-endonuclease (APE1/Ref-1), an essential multifunctional protein.Isolation of novel coregulatory protein networks associated with DNA-bound estrogen receptor alpha.Membrane association of mitochondrial DNA facilitates base excision repair in mammalian mitochondria.Human RECQL5beta stimulates flap endonuclease 1APE1/Ref-1 as an emerging therapeutic target for various human diseases: phytochemical modulation of its functionsKinetics of endogenous mouse FEN1 in base excision repair.Functional regulation of FEN1 nuclease and its link to cancerHuman Fanconi anemia complementation group a protein stimulates the 5' flap endonuclease activity of FEN1.Fen1 mutations that specifically disrupt its interaction with PCNA cause aneuploidy-associated cancerA fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cellsNuclease-deficient FEN-1 blocks Rad51/BRCA1-mediated repair and causes trinucleotide repeat instabilityUbiquitin ligase UBR3 regulates cellular levels of the essential DNA repair protein APE1 and is required for genome stabilityDNA polymerase delta-dependent repair of DNA single strand breaks containing 3'-end proximal lesions.AP endonuclease 1 prevents trinucleotide repeat expansion via a novel mechanism during base excision repair.Disruption of the FEN-1/PCNA interaction results in DNA replication defects, pulmonary hypoplasia, pancytopenia, and newborn lethality in mice.APE1/Ref-1 role in redox signaling: translational applications of targeting the redox function of the DNA repair/redox protein APE1/Ref-1.Base excision repair activities differ in human lung cancer cells and corresponding normal controls.A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification.Interaction between APC and Fen1 during breast carcinogenesis.Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1Role of the multifunctional DNA repair and redox signaling protein Ape1/Ref-1 in cancer and endothelial cells: small-molecule inhibition of the redox function of Ape1Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathwaysCoordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions.An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase lambda.The FEN1 L209P mutation interferes with long-patch base excision repair and induces cellular transformation.Cellular radiosensitivity: how much better do we understand it?Proliferating cell nuclear antigen prevents trinucleotide repeat expansions by promoting repeat deletion and hairpin removal.A review on protein-protein interaction network of APE1/Ref-1 and its associated biological functions.BERing the burden of damage: Pathway crosstalk and posttranslational modification of base excision repair proteins regulate DNA damage management.
P2860
Q21558646-E20BF783-5B1B-4965-95EA-EF7519FDCC19Q24301431-58E4C07E-6E7A-4433-AE12-B66656B87559Q24310413-8E9DAFB8-0406-4304-BF31-6F14338D621EQ24314558-48515204-F280-4B58-8B8B-C638383A66EDQ24320136-35C3787A-C333-4989-8894-4B302ED32090Q24648095-562BD075-D37C-41C7-8F9D-B89F45F664E5Q24797229-65DA1950-DF5B-487A-A0D1-2D6208139758Q26822957-86FD3F7E-18B1-41B8-83F2-0F2D211A3D27Q26863138-2AB94272-A6BE-45F7-BDBA-28E23834C54FQ28082955-7BA4A79C-C66F-423D-BC37-C719FD5877D0Q30397641-0A2879DA-386F-4BBF-8835-99122D1258B7Q30434808-906D51D4-A4C4-4EE3-9A34-996315F89273Q33381413-B8599C5B-AA4A-4AEA-8B36-809D6CCEE0F7Q33719407-8AB389F5-EF74-4492-99EA-3FDDD79EB365Q33871215-8BE9171A-1152-4450-96AA-AA575E9A41C3Q33990581-6B43E15E-A2DC-4582-8203-A4626F4564EDQ34343255-40E505C6-E15C-42B4-894E-331C5E3E27BDQ34559690-F1FEDC88-A92D-4B13-8BA8-EB6E81DC4591Q35070427-2688415D-0DE4-47E0-A705-0F3B16E39818Q35085696-8C04F28B-4619-409B-9502-EAF820DBB4A7Q35648418-7A95B70D-DA66-4C61-835C-9A33FB6D9E4EQ35661319-3DC2A5F4-659D-4A8B-8194-1D15B7AF26B4Q35672223-00F1A263-96BE-4211-ABD1-7549C78B33EBQ35749686-CB7ED3BF-C40A-44F3-9292-63B9BBD46238Q35842536-D6AFC5EF-AA51-4768-89A5-011D441C32B3Q35856777-9A530304-7FBA-4F89-82ED-3869C91E1709Q35870045-506EFA39-90F1-44BE-A655-124F09711539Q36101204-50771D05-BA8E-4665-8A59-B538D945FB91Q36751371-CA3316A4-18D5-460B-9FEE-F29819775B91Q36853315-F870CD79-D265-4EDB-B669-3C596ED70B6DQ36914462-BE1D40F4-C867-4459-9E00-2BC828CAE64CQ36983872-F79BF6EA-9DA1-4B14-AD95-A0B641AA8CA2Q37188352-59C3C169-03B3-4FAE-82F5-B11FDA8B1CD2Q37379745-F01012E5-834C-4109-8953-0A91E9EDCE95Q37416571-8BF1281F-B0EE-4524-8CE0-2019E2702B71Q37478615-2FE53740-2784-4414-8DCF-E509E5CCDC3DQ37648742-238B37A9-4C8D-4DB5-A7F2-E4B42E585026Q37677271-C8F2B273-BBC8-4AD4-A145-422039D1AEBDQ38383985-161AEA8D-C0F6-4BC4-9A4C-394C4E216C48Q38669183-8F6B86A8-3E5E-418C-A914-06573E947D6C
P2860
Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Interaction of human AP endonu ...... ong-patch base excision repair
@ast
Interaction of human AP endonu ...... ong-patch base excision repair
@en
Interaction of human AP endonu ...... ong-patch base excision repair
@nl
type
label
Interaction of human AP endonu ...... ong-patch base excision repair
@ast
Interaction of human AP endonu ...... ong-patch base excision repair
@en
Interaction of human AP endonu ...... ong-patch base excision repair
@nl
prefLabel
Interaction of human AP endonu ...... ong-patch base excision repair
@ast
Interaction of human AP endonu ...... ong-patch base excision repair
@en
Interaction of human AP endonu ...... ong-patch base excision repair
@nl
P2093
P3181
P356
P1433
P1476
Interaction of human AP endonu ...... ong-patch base excision repair
@en
P2093
P304
P3181
P356
10.1021/BI011117I
P407
P577
2001-10-23T00:00:00Z