Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases. - Wikidata - wikimedia - TriplyDB

Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases.

Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases.

http://www.wikidata.org/entity/Q33888460

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Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution Structure and function of type II restriction endonucleases Molecular mechanisms of the whole DNA repair system: a comparison of bacterial and eukaryotic systems Identification of a new family of putative PD-(D/E)XK nucleases with unusual phylogenomic distribution and a new type of the active site Structure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI.Identification of novel restriction endonuclease-like fold families among hypothetical proteins.The PD-(D/E)XK superfamily revisited: identification of new members among proteins involved in DNA metabolism and functional predictions for domains of (hitherto) unknown function.Crystal structure of NaeI--an evolutionary bridge between DNA endonuclease and topoisomerase Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I Structural and biochemical analyses of hemimethylated DNA binding by the SeqA protein Restriction endonuclease MvaI is a monomer that recognizes its target sequence asymmetrically The Crystal Structure of D212 from Sulfolobus Spindle-Shaped Virus Ragged Hills Reveals a New Member of the PD-(D/E)XK Nuclease Superfamily DNA mismatch repair and mutation avoidance pathways Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases.Detection of protein-DNA interaction with a DNA probe: distinction between single-strand and double-strand DNA-protein interaction.SURVEY AND SUMMARY: holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories.Sequence-specific cleavage by bacteriophage T4 endonuclease II in vitro.Mutational analysis of the MutH protein from Escherichia coli.PrfA protein of Bacillus species: prediction and demonstration of endonuclease activity on DNA Identifying an interaction site between MutH and the C-terminal domain of MutL by crosslinking, affinity purification, chemical coding and mass spectrometry.MutL homologs in restriction-modification systems and the origin of eukaryotic MORC ATPases.Identification of new homologs of PD-(D/E)XK nucleases by support vector machines trained on data derived from profile-profile alignments Mutants with temperature-sensitive defects in the Escherichia coli mismatch repair system: sensitivity to mispairs generated in vivo Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein.A phylogenomic study of DNA repair genes, proteins, and processes.Human DNA mismatch repair in vitro operates independently of methylation status at CpG sites The structural basis of damaged DNA recognition and endonucleolytic cleavage for very short patch repair endonuclease.Cooperation and competition in mismatch repair: very short-patch repair and methyl-directed mismatch repair in Escherichia coli.Identification of a novel human mitochondrial endo-/exonuclease Ddk1/c20orf72 necessary for maintenance of proper 7S DNA levels.Functional interactions and signaling properties of mammalian DNA mismatch repair proteins.DNA Mismatch Repair.MLH1 mutations differentially affect meiotic functions in Saccharomyces cerevisiae Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.Activation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System.Meiotic recombination intermediates and mismatch repair proteins.Involvement of mismatch repair in the reciprocal control of motility and adherence of uropathogenic Escherichia coli.Resolving the relationships of resolving enzymes.Structural, functional, and evolutionary relationships between lambda-exonuclease and the type II restriction endonucleases.

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P2860

Structural basis for MutH activation in E.coli mismatch repair and relationship of MutH to restriction endonucleases.

http://www.wikidata.org/entity/Q33888460

description

1998 nî lūn-bûn

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1998 թուականի Մարտին հրատարակուած գիտական յօդուած

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1998 թվականի մարտին հրատարակված գիտական հոդված

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1998年の論文

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1998年論文

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1998年論文

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1998年論文

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Structural basis for MutH acti ...... to restriction endonucleases.

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Structural basis for MutH acti ...... to restriction endonucleases.

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Structural basis for MutH acti ...... to restriction endonucleases.

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Structural basis for MutH acti ...... to restriction endonucleases.

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Structural basis for MutH acti ...... to restriction endonucleases.

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Ban C

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Yang W

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracing

Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding

Crystal structure of PvuII endonuclease reveals extensive structural homologies to EcoRV

Mg2+ binding to the active site of EcoRV endonuclease: a crystallographic study of complexes with substrate and product DNA at 2 A resolution

Structure of PvuII endonuclease with cognate DNA

The crystal structure of EcoRV endonuclease and of its complexes with cognate and non-cognate DNA fragments

Structure of the multimodular endonuclease FokI bound to DNA

Protein structure comparison by alignment of distance matrices

Multiple sequence alignment with hierarchical clustering

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Escherichia coli

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