Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme.
about
MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNAElectrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsAtomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylaseA Structural Hinge in Eukaryotic MutY Homologues Mediates Catalytic Activity and Rad9–Rad1–Hus1 Checkpoint Complex InteractionsMutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamilyEnhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatchIntact MutY and its catalytic domain differentially contact with A/8-oxoG-containing DNA.Insights into the role of Val45 and Gln182 of Escherichia coli MutY in DNA substrate binding and specificity.Molecular cloning and functional analysis of the MutY homolog of Deinococcus radiodurans.Functional expression of hMYH, a human homolog of the Escherichia coli MutY protein.A phylogenomic study of DNA repair genes, proteins, and processes.Protein-DNA charge transport: redox activation of a DNA repair protein by guanine radical.Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain.The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities.Chlorella virus PBCV-1 encodes a homolog of the bacteriophage T4 UV damage repair gene denVPhysical and functional interactions between Escherichia coli MutY glycosylase and mismatch repair protein MutSDNA-mediated charge transport for DNA repair.DNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport?Repair of hydantoins, one electron oxidation product of 8-oxoguanine, by DNA glycosylases of Escherichia coli.The active site of the Escherichia coli MutY DNA adenine glycosylase.A dimeric mechanism for contextual target recognition by MutY glycosylase.Hyperrecombination in Streptococcus pneumoniae depends on an atypical mutY homologue.Differential subcellular localization of human MutY homolog (hMYH) and the functional activity of adenine:8-oxoguanine DNA glycosylase.Dispensability of the [4Fe-4S] cluster in novel homologues of adenine glycosylase MutY.DNA glycosylases in the base excision repair of DNAFunctional interaction of MutY homolog with proliferating cell nuclear antigen in fission yeast, Schizosaccharomyces pombe.Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates.Flipping duplex DNA inside out: a double base-flipping reaction mechanism by Escherichia coli MutY adenine glycosylase.Reaction intermediates in the catalytic mechanism of Escherichia coli MutY DNA glycosylase.An Escherichia coli MutY mutant without the six-helix barrel domain is a dimer in solution and assembles cooperatively into multisubunit complexes with DNA.Drosophila Rrp1 domain structure as defined by limited proteolysis and biophysical analyses.Hybrid QM/MM Simulations of Enzyme-Catalyzed DNA Repair Reactions
P2860
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P2860
Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Identification of the structur ...... li DNA mismatch repair enzyme.
@en
type
label
Identification of the structur ...... li DNA mismatch repair enzyme.
@en
prefLabel
Identification of the structur ...... li DNA mismatch repair enzyme.
@en
P2093
P2860
P356
P1476
Identification of the structur ...... li DNA mismatch repair enzyme.
@en
P2093
Czerwinski EW
P2860
P304
16218-16226
P356
10.1074/JBC.271.27.16218
P407
P577
1996-07-01T00:00:00Z