Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein.
about
Phosphorylation: the molecular switch of double-strand break repairPhosphorylation and regulation of DNA ligase IV stability by DNA-dependent protein kinaseInvolvement of human polynucleotide kinase in double-strand break repair by non-homologous end joiningSynapsis of DNA ends by DNA-dependent protein kinaseSubnuclear localization of Ku protein: functional association with RNA polymerase II elongation sites.Processing of DNA for nonhomologous end-joining by cell-free extractThe dynamics of Ku70/80 and DNA-PKcs at DSBs induced by ionizing radiation is dependent on the complexity of damageDifferential activation of DNA-PK based on DNA strand orientation and sequence biasInhibition of double-strand break non-homologous end-joining by cisplatin adducts in human cell extractsThe leucine rich region of DNA-PKcs contributes to its innate DNA affinity.Terminal DNA structure and ATP influence binding parameters of the DNA-dependent protein kinase at an early step prior to DNA synapsis.C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage responseBeyond DNA repair: DNA-PK function in cancerDNA-PK: a dynamic enzyme in a versatile DSB repair pathwayGenotypic characteristics of resistant tumors to pre-operative ionizing radiation in rectal cancerCrystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats.Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair.Processing and joining of DNA ends coordinated by interactions among Dnl4/Lif1, Pol4, and FEN-1.Replication fork instability and the consequences of fork collisions from rereplicationThe DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosisTRF2 interaction with Ku heterotetramerization interface gives insight into c-NHEJ prevention at human telomeresInteractions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinaseDNA ligase IV and XRCC4 form a stable mixed tetramer that functions synergistically with other repair factors in a cell-free end-joining systemThe mechanism of human nonhomologous DNA end joiningRole of non-homologous end joining in V(D)J recombinationFunctional intersection of ATM and DNA-dependent protein kinase catalytic subunit in coding end joining during V(D)J recombinationA moonlighting function of Mycobacterium smegmatis Ku in zinc homeostasis?Kinetic analysis of the Ku-DNA binding activity reveals a redox-dependent alteration in protein structure that stimulates dissociation of the Ku-DNA complexMolecular analysis of Ku redox regulation.Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex.TRF2/RAP1 and DNA-PK mediate a double protection against joining at telomeric ends.Structural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a timeActivation and autoregulation of DNA-PK from structured single-stranded DNA and coding end hairpins.Coincident In Vitro Analysis of DNA-PK-Dependent and -Independent Nonhomologous End Joining.BRCA1 and BRCA2: breast/ovarian cancer susceptibility gene products and participants in DNA double-strand break repair.Mechanisms of double-strand break repair in somatic mammalian cells.XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair.Cooperative assembly of a protein-DNA filament for nonhomologous end joiningA stochastic model of DNA fragments rejoiningDistinct roles of Ape1 protein, an enzyme involved in DNA repair, in high or low linear energy transfer ionizing radiation-induced cell killing.
P2860
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P2860
Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Geometry of a complex formed b ...... d translocation of Ku protein.
@ast
Geometry of a complex formed b ...... d translocation of Ku protein.
@en
Geometry of a complex formed b ...... d translocation of Ku protein.
@nl
type
label
Geometry of a complex formed b ...... d translocation of Ku protein.
@ast
Geometry of a complex formed b ...... d translocation of Ku protein.
@en
Geometry of a complex formed b ...... d translocation of Ku protein.
@nl
altLabel
Geometry of a complex formed b ...... rd translocation of Ku protein
@en
prefLabel
Geometry of a complex formed b ...... d translocation of Ku protein.
@ast
Geometry of a complex formed b ...... d translocation of Ku protein.
@en
Geometry of a complex formed b ...... d translocation of Ku protein.
@nl
P356
P1476
Geometry of a complex formed b ...... d translocation of Ku protein.
@en
P304
P356
10.1093/NAR/27.24.4679
P407
P577
1999-12-15T00:00:00Z