Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution (Q27674919)

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Language	Label	Description	Also known as
English	Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution	scientific article

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scholarly article

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Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution (English)

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Thermus thermophilus

object named as

Thermus thermophilus

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based on heuristic

inferred from title

author name string

Luan Chen

1

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Ke Shi

2

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Zhiqi Yin

3

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Hideki Aihara

4

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language of work or name

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publication date

7 January 2013

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Nucleic Acids Research

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41

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1

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648-56

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copyright license

Creative Commons Attribution-NonCommercial 3.0 Unported

4 October 2016

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April 2022 Public Data File from Crossref

copyright status

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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20 March 2017

Crystal structure of T4 endonuclease VII resolving a Holliday junction

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20 March 2017

The structural basis of Holliday junction resolution by T7 endonuclease I

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20 March 2017

Atomic structure of the RuvC resolvase: a holliday junction-specific endonuclease from E. coli

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20 March 2017

Phasercrystallographic software

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20 March 2017

Refinement of macromolecular structures by the maximum-likelihood method

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20 March 2017

Identification of Holliday junction resolvases from humans and yeast

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20 March 2017

Molecular views of recombination proteins and their control

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20 March 2017

Recombination proteins and rescue of arrested replication forks

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20 March 2017

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29 September 2017

Mechanism of Holliday junction resolution by the human GEN1 protein

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29 September 2017

Efficient second strand cleavage during Holliday junction resolution by RuvC requires both increased junction flexibility and an exposed 5' phosphate

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Retroviral integrase superfamily: the structural perspective

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Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release

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29 September 2017

The junction-resolving enzymes.

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29 September 2017

Evidence that phenylalanine 69 in Escherichia coli RuvC resolvase forms a stacking interaction during binding and destabilization of a Holliday junction DNA substrate.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Ensuring productive resolution by the junction-resolving enzyme RuvC: large enhancement of the second-strand cleavage rate

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

The RuvC protein dimer resolves Holliday junctions by a dual incision mechanism that involves base-specific contacts

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Processing the holliday junction in homologous recombination

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29 September 2017

Analysis of substrate specificity of the RuvC holliday junction resolvase with synthetic Holliday junctions.

1 reference

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29 September 2017

Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

RuvC protein resolves Holliday junctions via cleavage of the continuous (noncrossover) strands.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Identification of four acidic amino acids that constitute the catalytic center of the RuvC Holliday junction resolvase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Escherichia coli RuvC protein is an endonuclease that resolves the Holliday structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

29 September 2017

A mechanism for gene conversion in fungi

1 reference

https://api.crossref.org/works/10.1093%2FNAR%2FGKS1015

21 January 2018

ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli.

1 reference

https://api.crossref.org/works/10.1093%2FNAR%2FGKS1015

21 January 2018

Structure of a multisubunit complex that promotes DNA branch migration.

1 reference

https://api.crossref.org/works/10.1093%2FNAR%2FGKS1015

21 January 2018

Genetic recombination in E. coli: RuvC protein cleaves Holliday junctions at resolution hotspots in vitro.

1 reference

https://api.crossref.org/works/10.1093%2FNAR%2FGKS1015

21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

1 reference

https://api.crossref.org/works/10.1093%2FNAR%2FGKS1015

21 January 2018

Cleavage of Holliday Junctions by theEscherichia coliRuvABC Complex

1 reference

https://api.crossref.org/works/10.1093%2FNAR%2FGKS1015

21 January 2018

Structural requirements of substrate DNA for binding to and cleavage by RuvC, a Holliday junction resolvase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3592405

27 November 2018

Cleavage of symmetric immobile DNA junctions by Escherichia coli RuvC

1 reference

https://pubmed.ncbi.nlm.nih.gov/23118486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

High affinity of endonuclease VII for the Holliday structure containing one nick ensures productive resolution

1 reference

https://pubmed.ncbi.nlm.nih.gov/23118486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick and counternick mechanism

1 reference

https://pubmed.ncbi.nlm.nih.gov/23118486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mutational analysis on structure-function relationship of a holliday junction specific endonuclease RuvC

1 reference

https://pubmed.ncbi.nlm.nih.gov/23118486

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1093/NAR/GKS1015

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ResearchGate publication ID

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