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Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
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title
Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
(English)
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author name string
Zhucheng Chen
series ordinal
1
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Haijuan Yang
series ordinal
2
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Nikola P Pavletich
series ordinal
3
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language of work or name
English
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publication date
22 May 2008
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published in
Nature
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volume
453
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page(s)
489-4
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issue
7194
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cites work
The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
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Recombination at double-strand breaks and DNA ends: conserved mechanisms from phage to humans.
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DNA double-strand breaks: signaling, repair and the cancer connection
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Clarifying the mechanics of DNA strand exchange in meiotic recombination
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Recombination activities of E. coli recA protein
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7 January 2021
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Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
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7 January 2021
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RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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DNA strand exchange proteins: a biochemical and physical comparison.
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Crossref
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Structure and mechanism of Escherichia coli RecA ATPase
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7 January 2021
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Molecular design and functional organization of the RecA protein
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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The helicity of DNA in complexes with recA protein
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7 January 2021
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Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA.
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Isolation and visualization of active presynaptic filaments of recA protein and single-stranded DNA.
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Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament
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Direct observation of individual RecA filaments assembling on single DNA molecules
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Real-time observation of RecA filament dynamics with single monomer resolution.
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ATP-mediated conformational changes in the RecA filament
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7 January 2021
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Complexes of RecA protein in solution. A study by small angle neutron scattering
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7 January 2021
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Arrangement of RecA protein in its active filament determined by polarized-light spectroscopy
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7 January 2021
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Similarity of the yeast RAD51 filament to the bacterial RecA filament
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7 January 2021
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The structure of the E. coli recA protein monomer and polymer
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7 January 2021
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inferred from DOI database lookup
Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation
1 reference
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7 January 2021
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inferred from DOI database lookup
Crystal structure of a Rad51 filament
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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inferred from DOI database lookup
What is the structure of the RecA-DNA filament?
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNATURE06971
retrieved
7 January 2021
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inferred from DOI database lookup
Structure of helical RecA-DNA complexes. III. The structural polarity of RecA filaments and functional polarity in the RecA-mediated strand exchange reaction.
1 reference
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7 January 2021
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Differential proximity probing of two DNA binding sites in the Escherichia coli recA protein using photo-cross-linking methods
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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inferred from DOI database lookup
Photocross-links between single-stranded DNA and Escherichia coli RecA protein map to loops L1 (amino acid residues 157-164) and L2 (amino acid residues 195-209).
1 reference
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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inferred from DOI database lookup
Saturation mutagenesis of the E. coli RecA loop L2 homologous DNA pairing region reveals residues essential for recombination and recombinational repair.
1 reference
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
based on heuristic
inferred from DOI database lookup
New mutations in and around the L2 disordered loop of the RecA protein modulate recombination and/or coprotease activity
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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Complementation of one RecA protein point mutation by another. Evidence for trans catalysis of ATP hydrolysis.
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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inferred from DOI database lookup
Analysis of the DNA binding site of Escherichia coli RecA protein.
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7 January 2021
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inferred from DOI database lookup
Toxic mutations in the recA gene of E. coli prevent proper chromosome segregation
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7 January 2021
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The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants
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The GTPase-activating protein Rap1GAP uses a catalytic asparagine
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7 January 2021
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Intersubunit proximity of residues in the RecA protein as shown by engineered disulfide cross-links.
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Crossref
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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Allosteric regulation of RecA protein function is mediated by Gln194.
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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DNA replication fidelity
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Crossref
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7 January 2021
based on heuristic
inferred from DOI database lookup
Characterization of a mutant RecA protein that facilitates homologous genetic recombination but not recombinational DNA repair: RecA423.
1 reference
stated in
Crossref
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
based on heuristic
inferred from DOI database lookup
The function of the secondary DNA-binding site of RecA protein during DNA strand exchange
1 reference
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
based on heuristic
inferred from DOI database lookup
The mutant RecA proteins, RecAR243Q and RecAK245N, exhibit defective DNA binding in homologous pairing
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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RecA binding to a single double-stranded DNA molecule: a possible role of DNA conformational fluctuations
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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inferred from DOI database lookup
N-terminal 33 amino acid residues of Escherichia coli RecA protein contribute to its self-assembly
1 reference
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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inferred from DOI database lookup
A partially deficient mutant, recA1730, that fails to form normal nucleoprotein filaments
1 reference
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Crossref
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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Processing of X-ray diffraction data collected in oscillation mode
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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Improved methods for building protein models in electron density maps and the location of errors in these models
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https://api.crossref.org/works/10.1038%2FNATURE06971
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7 January 2021
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Identifiers
DOI
10.1038/NATURE06971
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2442870
Dimensions Publication ID
1006227264
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OpenCitations bibliographic resource ID
2442870
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2442870
PubMed ID
18497818
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2442870
ResearchGate publication ID
5351952
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Springer Nature article ID
10.1038/nature06971
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