(Q27675393)

1

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Shruti Malu

2

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Patricia Cortes

3

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Aneel K Aggarwal

Structural Insights into the Role of Domain Flexibility in Human DNA Ligase IV

4

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publication date

27 December 2012

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published in

Cell Reports

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volume

2

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issue

6

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page(s)

1505-12

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cites work

1 reference

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XRCC4 Protein Interactions with XRCC4-like Factor (XLF) Create an Extended Grooved Scaffold for DNA Ligation and Double Strand Break Repair

20 March 2017

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Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining

20 March 2017

1 reference

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Crucial role for DNA ligase III in mitochondria but not in Xrcc1-dependent repair

20 March 2017

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Human DNA ligase III recognizes DNA ends by dynamic switching between two DNA-bound states

20 March 2017

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The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway

20 March 2017

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

20 March 2017

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Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4

20 March 2017

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Eukaryotic DNA ligases: structural and functional insights

20 March 2017

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XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining

20 March 2017

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Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family

20 March 2017

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Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination

20 March 2017

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Crystal structure of an Xrcc4-DNA ligase IV complex

20 March 2017

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Ku recruits the XRCC4-ligase IV complex to DNA ends

20 March 2017

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Crystal structure of NAD+-dependent DNA ligase: modular architecture and functional implications

20 March 2017

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DNA ligase IV is essential for V(D)J recombination and DNA double-strand break repair in human precursor lymphocytes

20 March 2017

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Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV

20 March 2017

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Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells

20 March 2017

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Phasercrystallographic software

20 March 2017

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Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis

20 March 2017

1 reference

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Artemis C-terminal region facilitates V(D)J recombination through its interactions with DNA Ligase IV and DNA-PKcs

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

DNA-PK autophosphorylation facilitates Artemis endonuclease activity

20 March 2017

1 reference

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Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase

20 March 2017

1 reference

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Repair of double-strand DNA breaks by the human nonhomologous DNA end joining pathway: the iterative processing model

20 March 2017

1 reference

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The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and gaps

20 March 2017

1 reference

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Human DNA ligase I completely encircles and partially unwinds nicked DNA

20 March 2017

1 reference

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Impaired nonhomologous end-joining provokes soft tissue sarcomas harboring chromosomal translocations, amplifications, and deletions

20 March 2017

1 reference

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The DNA damage response and cancer therapy

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

XLF regulates filament architecture of the XRCC4·ligase IV complex

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

Molecular mechanism of protein assembly on DNA double-strand breaks in the non-homologous end-joining pathway

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

DNA-dependent protein kinase and XRCC4-DNA ligase IV mobilization in the cell in response to DNA double strand breaks.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

Promotion of Dnl4-catalyzed DNA end-joining by the Rad50/Mre11/Xrs2 and Hdf1/Hdf2 complexes

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

Design, synthesis, and biological evaluation of novel nucleoside and nucleotide analogues as agents against DNA viruses and/or retroviruses

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

Single-stranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: influence of terminal DNA sequence

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

Electron microscopy of Xrcc4 and the DNA ligase IV-Xrcc4 DNA repair complex.

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3538150

10.1016/J.CELREP.2012.11.004

27 November 2018

Identifiers

DOI

1 reference

1 reference

1 reference

PubMed publication ID

23219551

1 reference