The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair
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The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machineryDNA polymerase family X: function, structure, and cellular rolesLong patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complexConditional inactivation of the DNA damage response gene Hus1 in mouse testis reveals separable roles for components of the RAD9-RAD1-HUS1 complex in meiotic chromosome maintenanceStructure and Functional Implications of the Human Rad9-Hus1-Rad1 Cell Cycle Checkpoint ComplexThe 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae.DNA damage response genes and the development of cancer metastasisUSP37 deubiquitinates Cdt1 and contributes to regulate DNA replicationReplication protein A directs loading of the DNA damage checkpoint clamp to 5'-DNA junctions.Stripped-down DNA repair in a highly reduced parasite.Rad9 modulates the P21WAF1 pathway by direct association with p53.TLK1B promotes repair of DSBs via its interaction with Rad9 and Asf1.Interaction between human mismatch repair recognition proteins and checkpoint sensor Rad9-Rad1-Hus1Pol β associated complex and base excision repair factors in mouse fibroblasts.Visualization of the physical and functional interaction between hMYH and hRad9 by Dronpa bimolecular fluorescence complementation.The RAD9-RAD1-HUS1 (9.1.1) complex interacts with WRN and is crucial to regulate its response to replication fork stallingRad9 is required for B cell proliferation and immunoglobulin class switch recombinationPhosphorylation of Xenopus Rad1 and Hus1 defines a readout for ATR activation that is independent of Claspin and the Rad9 carboxy terminusTargeted deletion of Rad9 in mouse skin keratinocytes enhances genotoxin-induced tumor development.New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins.Need telomere maintenance? Call 911Increased common fragile site expression, cell proliferation defects, and apoptosis following conditional inactivation of mouse Hus1 in primary cultured cells.Genome maintenance defects in cultured cells and mice following partial inactivation of the essential cell cycle checkpoint gene Hus1.Contributions of Rad9 to tumorigenesis.The checkpoint clamp, Rad9-Rad1-Hus1 complex, preferentially stimulates the activity of apurinic/apyrimidinic endonuclease 1 and DNA polymerase beta in long patch base excision repairThe human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates NEIL1 glycosylaseHypersensitivity phenotypes associated with genetic and synthetic inhibitor-induced base excision repair deficiencyMicrohomology-mediated DNA strand annealing and elongation by human DNA polymerases λ and β on normal and repetitive DNA sequences.The human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylaseBypass of a psoralen DNA interstrand cross-link by DNA polymerases β, ι, and κ in vitro.The role of DNA exonucleases in protecting genome stability and their impact on ageing.Multiple functions of rad9 for preserving genomic integrityUnderstanding the role of the Q338H MUTYH variant in oxidative damage repairSuperior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1Rad9 plays an important role in DNA mismatch repair through physical interaction with MLH1The DNA damage checkpoint protein RAD9A is essential for male meiosis in the mouse.Phosphorylation of human DNA ligase I regulates its interaction with replication factor C and its participation in DNA replication and DNA repairA junction branch point adjacent to a DNA backbone nick directs substrate cleavage by Saccharomyces cerevisiae Mus81-Mms4.Alu-miRNA interactions modulate transcript isoform diversity in stress response and reveal signatures of positive selection.Jab1 mediates protein degradation of the Rad9-Rad1-Hus1 checkpoint complex
P2860
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P2860
The human Rad9/Rad1/Hus1 damage sensor clamp interacts with DNA polymerase beta and increases its DNA substrate utilisation efficiency: implications for DNA repair
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@ast
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@en
type
label
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@ast
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@en
prefLabel
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@ast
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@en
P2093
P2860
P356
P1476
The human Rad9/Rad1/Hus1 damag ...... y: implications for DNA repair
@en
P2093
Dorothee Funk
Erica Friedrich-Heineken
Giuseppe Villani
Igor Shevelev
Isabelle Frouin
Magali Toueille
Michael O Hottiger
Nazim El-Andaloussi
Raimundo Freire
Ulrich Hübscher
P2860
P304
P356
10.1093/NAR/GKH652
P407
P577
2004-06-22T00:00:00Z