Correlation of biochemical properties with the oligomeric state of human rad52 protein (Q38363023)

2 September 2017

title

Correlation of biochemical properties with the oligomeric state of human rad52 protein (English)

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2 September 2017

Janice A Lloyd

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2 September 2017

Anthony L Forget

series ordinal

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2 September 2017

Kendall L Knight

series ordinal

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2 September 2017

language of work or name

English

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publication date

10 September 2002

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

277

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2 September 2017

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2 September 2017

page(s)

46172-46178

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DNA double strand break repair in mammalian cells

2 September 2017

cites work

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Chromosomal stability and the DNA double-stranded break connection

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Homologous DNA recombination in vertebrate cells

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Homologous recombinational repair of DNA ensures mammalian chromosome stability

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Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing

21 January 2018

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Visualisation of human rad52 protein and its complexes with hRad51 and DNA.

21 January 2018

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Binding of double-strand breaks in DNA by human Rad52 protein

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The human Rad52 protein exists as a heptameric ring

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M207262200

DNA strand annealing is promoted by the yeast Rad52 protein

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Human Rad52 protein promotes single-strand DNA annealing followed by branch migration

21 January 2018

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DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M207262200

Identification of novel isoforms of human RAD52

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Homologous pairing promoted by the human Rad52 protein

21 January 2018

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Visualization of recombination intermediates produced by RAD52-mediated single-strand annealing

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Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52.

21 January 2018

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Studies of the interaction between Rad52 protein and the yeast single-stranded DNA binding protein RPA.

21 January 2018

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Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells

21 January 2018

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Function of Yeast Rad52 Protein as a Mediator between Replication Protein A and the Rad51 Recombinase

21 January 2018

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Synergistic actions of Rad51 and Rad52 in recombination and DNA repair

21 January 2018

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Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A

21 January 2018

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Stimulation by Rad52 of yeast Rad51-mediated recombination

21 January 2018

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Functional interactions among yeast Rad51 recombinase, Rad52 mediator, and replication protein A in DNA strand exchange

21 January 2018

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Rad52 forms DNA repair and recombination centers during S phase

21 January 2018

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Nuclear foci of mammalian recombination proteins are located at single-stranded DNA regions formed after DNA damage

21 January 2018

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Localization and dynamic relocalization of mammalian Rad52 during the cell cycle and in response to DNA damage

21 January 2018

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Coordinated response of mammalian Rad51 and Rad52 to DNA damage

21 January 2018

1 reference

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Nuclear dynamics of RAD52 group homologous recombination proteins in response to DNA damage.

21 January 2018

1 reference

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Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M207262200

Human RAD52 exhibits two modes of self-association

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M207262200

21 January 2018

Identifiers

DOI

10.1074/JBC.M207262200

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2 September 2017

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