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Structure of a Mutant Form of Proliferating Cell Nuclear Antigen That Blocks Translesion DNA Synthesis † ‡Crystal Structure of SUMO-Modified Proliferating Cell Nuclear AntigenThe Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1Eukaryotic polymerases iota and zeta act sequentially to bypass DNA lesionsVariations on a theme: eukaryotic Y-family DNA polymerasesPre-steady state kinetic studies of the fidelity of nucleotide incorporation by yeast DNA polymerase deltaRequirement of Watson-Crick hydrogen bonding for DNA synthesis by yeast DNA polymerase eta.Human DNA polymerase kappa forms nonproductive complexes with matched primer termini but not with mismatched primer termini.Structurally distinct ubiquitin- and sumo-modified PCNA: implications for their distinct roles in the DNA damage response.Solution X-ray scattering combined with computational modeling reveals multiple conformations of covalently bound ubiquitin on PCNADead-End Elimination with a Polarizable Force Field Repacks PCNA Structures.Bridging the gap: a family of novel DNA polymerases that replicate faulty DNA.Human DNA polymerase iota utilizes different nucleotide incorporation mechanisms dependent upon the template base.Mechanism of nucleotide incorporation opposite a thymine-thymine dimer by yeast DNA polymerase eta.Efficient and error-free replication past a minor-groove N2-guanine adduct by the sequential action of yeast Rev1 and DNA polymerase zeta.The Many Roles of PCNA in Eukaryotic DNA ReplicationThe mechanism of nucleotide incorporation by human DNA polymerase eta differs from that of the yeast enzyme.Accuracy of lesion bypass by yeast and human DNA polymerase eta.PCNA tool belts and polymerase bridges form during translesion synthesisR.I.P. to the PIP: PCNA-binding motif no longer considered specific: PIP motifs and other related sequences are not distinct entities and can bind multiple proteins involved in genome maintenance.DNA Polymerase Fidelity: Beyond Right and Wrong.Mechanism of efficient and accurate nucleotide incorporation opposite 7,8-dihydro-8-oxoguanine by Saccharomyces cerevisiae DNA polymerase eta.The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility.Analyzing the Catalytic Activities and Interactions of Eukaryotic Translesion Synthesis Polymerases.Crystal structures of PCNA mutant proteins defective in gene silencing suggest a novel interaction site on the front face of the PCNA ring.Mismatch extension ability of yeast and human DNA polymerase etaFidelity of human DNA polymerase etaIncreased DNA unwinding efficiency of bacteriophage T7 DNA helicase mutant protein 4A'/E348KYeast DNA polymerase eta utilizes an induced-fit mechanism of nucleotide incorporationPre-steady-state kinetic studies of protein-template-directed nucleotide incorporation by the yeast Rev1 proteinA lag-phase in the reduction of flavin dependent thymidylate synthase (FDTS) revealed a mechanistic missing linkConformational flexibility of fork-remodeling helicase Rad5 shown by full-ensemble hybrid methods
P50
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P50
description
researcher
@en
name
M T Washington
@en
M T Washington
@nl
type
label
M T Washington
@en
M T Washington
@nl
prefLabel
M T Washington
@en
M T Washington
@nl
P106
P31
P496
0000-0001-8680-2992