Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
about
Inhibition of mutation and combating the evolution of antibiotic resistanceThe C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase η and Rev7 subunit of polymerase ζEfficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappaMouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesisHomologous recombination in DNA repair and DNA damage toleranceCircadian clock control of the cellular response to DNA damageThe fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerasesEukaryotic translesion polymerases and their roles and regulation in DNA damage toleranceA mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repairHuman DNA polymerase kappa uses template-primer misalignment as a novel means for extending mispaired termini and for generating single-base deletionsRibozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT geneEvidence for interplay among yeast replicative DNA polymerases alpha, delta and epsilon from studies of exonuclease and polymerase active site mutationsPCNA structure and function: insights from structures of PCNA complexes and post-translationally modified PCNAStructure of a Mutant Form of Proliferating Cell Nuclear Antigen That Blocks Translesion DNA Synthesis † ‡Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchangeStructure and Functional Analysis of the BRCT Domain of Translesion Synthesis DNA Polymerase Rev1The 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae.A ubiquitin-binding motif in the translesion DNA polymerase Rev1 mediates its essential functional interaction with ubiquitinated proliferating cell nuclear antigen in response to DNA damage.The in vivo characterization of translesion synthesis across UV-induced lesions in Saccharomyces cerevisiae: insights into Pol zeta- and Pol eta-dependent frameshift mutagenesis.The 3'->5' exonuclease of Apn1 provides an alternative pathway to repair 7,8-dihydro-8-oxodeoxyguanosine in Saccharomyces cerevisiae.TOR signaling is a determinant of cell survival in response to DNA damage.Mammalian translesion DNA synthesis across an acrolein-derived deoxyguanosine adduct. Participation of DNA polymerase eta in error-prone synthesis in human cellsThe ATR-p53 pathway is suppressed in noncycling normal and malignant lymphocytesDNA polymerase δ and ζ switch by sharing accessory subunits of DNA polymerase δInteraction of hREV1 with three human Y-family DNA polymerasesCharacterization of human Spartan/C1orf124, an ubiquitin-PCNA interacting regulator of DNA damage toleranceMutational specificity of gamma-radiation-induced guanine-thymine and thymine-guanine intrastrand cross-links in mammalian cells and translesion synthesis past the guanine-thymine lesion by human DNA polymerase etaThe mouse genomic instability mutation chaos1 is an allele of Polq that exhibits genetic interaction with AtmA novel variant of DNA polymerase ζ, Rev3ΔC, highlights differential regulation of Pol32 as a subunit of polymerase δ versus ζ in Saccharomyces cerevisiaeControl of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugationOpposing effects of the UV lesion repair protein XPA and UV bypass polymerase eta on ATR checkpoint signaling.The fidelity of DNA synthesis by yeast DNA polymerase zeta alone and with accessory proteins.Two-polymerase mechanisms dictate error-free and error-prone translesion DNA synthesis in mammalsParticipation of DNA polymerase zeta in replication of undamaged DNA in Saccharomyces cerevisiae.Differential roles for DNA polymerases eta, zeta, and REV1 in lesion bypass of intrastrand versus interstrand DNA cross-links.A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesisProcessivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesisMolecular basis of aflatoxin-induced mutagenesis-role of the aflatoxin B1-formamidopyrimidine adductBiochemical evidence for the requirement of Hoogsteen base pairing for replication by human DNA polymerase iotaEvidence for a Watson-Crick hydrogen bonding requirement in DNA synthesis by human DNA polymerase kappa
P2860
Q21146100-5AB651EE-5FB3-4692-8B76-835990C52EE6Q24294205-F93B8FC9-8588-42CA-B63E-DE63ADD3AF84Q24563650-4E4B447C-C237-416B-9323-580251521A07Q24594244-20C86E80-B0D9-4E16-B2AA-D2721999ECE4Q24601150-468452A9-94B5-4EC1-90E0-DDDBE5261C45Q24602881-4C6C05F4-2F90-4EF1-AAB1-19337E2432F5Q24630867-475F8EB1-7C3D-40CD-85D8-53EA7AE81968Q24645172-036C34BA-6791-4C0D-BCD3-37CA06A17607Q24646838-1CEF9F4C-339C-4F65-BC54-18733EDB857DQ24670499-04930530-AED8-4BA5-984A-8B08DD7E02F9Q24685084-FB73BC43-CF82-4BBA-B082-44B3BAB24DCFQ24796773-F24FFE31-443B-4980-B265-FC6647BB24A3Q26821952-233C2803-F07B-4BC9-BA4B-6E4F4587EBDAQ27653033-7CFA9997-1FA5-4444-B3E6-6CB18951B476Q27660297-DE2CB573-E44A-476E-A58A-FD63AE522418Q27675497-D7D38B34-2321-4254-9532-FF7B8D147D85Q27931291-3F6E9817-1D9C-4512-9CB5-21FF453DFDFEQ27931627-61E6AF9E-157D-44D0-BE2D-98A06F0EB5ECQ27934540-C965D152-BAD2-4D20-AD00-531E4205A117Q27936279-DC63EFDE-4D77-48E7-BDE9-0AFFF7D482F6Q27938358-4AB5D84D-1EF7-43C1-AD0F-1386EC39AAB8Q28209176-40D1EB57-52A0-441E-8C83-D127D7928E69Q28241779-63ED3126-C7FE-4E3F-A252-B75ECB63B43DQ28263318-3BDB342A-6702-4FED-9033-F27033F5C8CFQ28266239-A50DB012-1371-4D37-914A-B1779F537E9FQ28275269-ED98363E-92AB-4FE4-9FA3-19828680F6E7Q28286703-E41A7FBC-CCAF-4AE6-AE36-95AC89ABD78AQ28586941-BB3F574E-67A3-4FD8-AB9D-92172B1D2A34Q28652503-967769DE-419F-491A-BC79-F629C86EABA7Q29619155-B463D86F-A00F-401C-8405-B78F161A7D44Q33242349-65012947-4F0A-44A4-8CA8-46FB78332181Q33257520-ED8FC40D-6985-43EA-846A-F52320292B8CQ33400985-E855F3F2-9403-4805-AC87-A58AA7B86FBCQ33628462-62390D7E-9565-42BB-83A8-B343733F0475Q33648841-C59C7EE0-FE93-4CAE-8E27-1D16D5F351D8Q33714583-BB294CC7-0A30-4E41-90A5-3682203751A7Q33756104-664BDCAD-3880-4D17-8BC6-3498565E20DCQ33827666-8336E3FD-1954-4F43-BA50-B8F8BD149ED3Q33906689-C27B10EA-7C06-4D92-9519-4A8AE8CC6EA4Q33924989-DFD911C3-16D5-4967-AC03-3FC24609450B
P2860
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
description
2002 nî lūn-bûn
@nan
2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@ast
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@en
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@nl
type
label
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@ast
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@en
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@nl
prefLabel
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@ast
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@en
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@nl
P356
P1433
P1476
Translesion DNA synthesis in eukaryotes: a one- or two-polymerase affair.
@en
P2093
Louise Prakash
Satya Prakash
P304
P356
10.1101/GAD.1009802
P577
2002-08-01T00:00:00Z