Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions - Test2 - elhamkhani - TriplyDB

Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

http://www.wikidata.org/entity/Q29619958

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Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 The C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase η and Rev7 subunit of polymerase ζ Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen Human DNA polymerase iota protects cells against oxidative stress Human DINB1-encoded DNA polymerase kappa is a promiscuous extender of mispaired primer termini Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template.Unique misinsertion specificity of poliota may decrease the mutagenic potential of deaminated cytosines Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA.Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells.Translesion replication of benzo[a]pyrene and benzo[c]phenanthrene diol epoxide adducts of deoxyadenosine and deoxyguanosine by human DNA polymerase iota Role of human DNA polymerase kappa as an extender in translesion synthesis High-efficiency bypass of DNA damage by human DNA polymerase Q Efficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappa Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis Managing DNA polymerases: coordinating DNA replication, DNA repair, and DNA recombination A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair Human DNA polymerase kappa uses template-primer misalignment as a novel means for extending mispaired termini and for generating single-base deletions Eukaryotic DNA polymerase ζ A rescue act: Translesion DNA synthesis past N(2) -deoxyguanosine adducts Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the -clamp Insertion of dNTPs Opposite the 1, N 2 -Propanodeoxyguanosine Adduct by Sulfolobus solfataricus P2 DNA Polymerase IV † ‡Lesion Bypass of N2-Ethylguanine by Human DNA Polymerase ι Structure of a Mutant Form of Proliferating Cell Nuclear Antigen That Blocks Translesion DNA Synthesis † ‡DNA Synthesis across an Abasic Lesion by Human DNA Polymerase ι Structural basis of error-prone replication and stalling at a thymine base by human DNA polymerase ι Structure of the Human Rev1–DNA–dNTP Ternary Complex Replication across Template T/U by Human DNA Polymerase-ι DNA Polymerase Substrate Specificity: SIDE CHAIN MODULATION OF THE"A-RULE"Structural Basis for Proficient Incorporation of dTTP Opposite O6-Methylguanine by Human DNA Polymerase ι DNA Synthesis across an Abasic Lesion by Yeast Rev1 DNA Polymerase Bypass of Aflatoxin B 1 Adducts by the Sulfolobus solfataricus DNA Polymerase IV Structure and Functional Analysis of the BRCT Domain of Translesion Synthesis DNA Polymerase Rev1 Replication Bypass of the trans -4-Hydroxynonenal-Derived (6 S ,8 R ,11 S )-1, N 2 -Deoxyguanosine DNA Adduct by the Sulfolobus solfataricus DNA Polymerase IV Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy Three Residues of the Interdomain Linker Determine the Conformation and Single-base Deletion Fidelity of Y-family Translesion Polymerases The mechanisms of UV mutagenesis.Requirement of Nse1, a subunit of the Smc5-Smc6 complex, for Rad52-dependent postreplication repair of UV-damaged DNA 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.Reversal of PCNA ubiquitylation by Ubp10 in Saccharomyces cerevisiae.Yeast DNA polymerase zeta (zeta) is essential for error-free replication past thymine glycol

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Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

http://www.wikidata.org/entity/Q29619958

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2000 nî lūn-bûn

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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի օգոստոսին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

@zh-hant

2000年論文

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2000年論文

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2000年論文

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2000年论文

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name

Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

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Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

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type

label

Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

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Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

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Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

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Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

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Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesions

@en

P2093

Haracska L

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

Johnson RE

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

Prakash L

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

Prakash S

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

P2860

hRAD30 mutations in the variant form of xeroderma pigmentosum

A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes the catalytic subunit of DNA polymerase zeta

Fidelity and processivity of Saccharomyces cerevisiae DNA polymerase eta.

Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Poleta.

Thymine-thymine dimer bypass by yeast DNA polymerase zeta.

The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase eta

Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta

The T-T pyrimidine (6-4) pyrimidinone UV photoproduct is much less mutagenic in yeast than in Escherichia coli.

Extension of base mispairs by Taq DNA polymerase: implications for single nucleotide discrimination in PCR.

The frequency and accuracy of replication past a thymine-thymine cyclobutane dimer are very different in Saccharomyces cerevisiae and Escherichia coli.

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1015-1019

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scholarly article

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4419355

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10.1038/35023030

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6799

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406

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1039157319

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10984059

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