Physical and functional interactions between MutY glycosylase homologue (MYH) and checkpoint proteins Rad9-Rad1-Hus1.
about
MUTYH DNA glycosylase: the rationale for removing undamaged bases from the DNALong patch base excision repair proceeds via coordinated stimulation of the multienzyme DNA repair complexMUTYH the base excision repair gene family member associated with colorectal cancer polyposisConditional 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 ComplexA Structural Hinge in Eukaryotic MutY Homologues Mediates Catalytic Activity and Rad9–Rad1–Hus1 Checkpoint Complex InteractionsGenome Protection by the 9-1-1 Complex Subunit HUS1 Requires Clamp Formation, DNA Contacts, and ATR Signaling-independent Effector FunctionsInteraction between human mismatch repair recognition proteins and checkpoint sensor Rad9-Rad1-Hus1Synaptonemal complex formation and meiotic checkpoint signaling are linked to the lateral element protein Red1.Visualization of the physical and functional interaction between hMYH and hRad9 by Dronpa bimolecular fluorescence complementation.Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition.Recent advances in the structural mechanisms of DNA glycosylasesThe role of MutY homolog (Myh1) in controlling the histone deacetylase Hst4 in the fission yeast Schizosaccharomyces pombe.A role for the arginine methylation of Rad9 in checkpoint control and cellular sensitivity to DNA damage.Targeted deletion of Rad9 in mouse skin keratinocytes enhances genotoxin-induced tumor development.Need telomere maintenance? Call 911Increased sensitivity of DNA damage response-deficient cells to stimulated microgravity-induced DNA lesionsIncreased common fragile site expression, cell proliferation defects, and apoptosis following conditional inactivation of mouse Hus1 in primary cultured cells.SIRT6 protein deacetylase interacts with MYH DNA glycosylase, APE1 endonuclease, and Rad9-Rad1-Hus1 checkpoint clampGenome maintenance defects in cultured cells and mice following partial inactivation of the essential cell cycle checkpoint gene Hus1.Association of the Rad9-Rad1-Hus1 checkpoint clamp with MYH DNA glycosylase and DNA.Mammalian MutY homolog (MYH or MUTYH) protects cells from oxidative DNA damage.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 glycosylaseThe human checkpoint sensor Rad9-Rad1-Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylaseCancer-associated variants and a common polymorphism of MUTYH exhibit reduced repair of oxidative DNA damage using a GFP-based assay in mammalian cells.Understanding 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 MLH1Jab1 mediates protein degradation of the Rad9-Rad1-Hus1 checkpoint complexA tale of two tails: activation of DNA damage checkpoint kinase Mec1/ATR by the 9-1-1 clamp and by Dpb11/TopBP1.Coordination of MYH DNA glycosylase and APE1 endonuclease activities via physical interactions.Clamping down on mammalian meiosis.Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1.Interaction of apurinic/apyrimidinic endonuclease 2 (Apn2) with Myh1 DNA glycosylase in fission yeastatz-1 Influences meiosis to maintain germline chromosomal stability in Caenorhabditis elegans.Genetic instability in lymphoblastoid cell lines expressing biallelic and monoallelic variants in the human MUTYH gene.Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine.Loss of MUTYH function in human cells leads to accumulation of oxidative damage and genetic instability.A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage.
P2860
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P2860
Physical and functional interactions between MutY glycosylase homologue (MYH) and checkpoint proteins Rad9-Rad1-Hus1.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Physical and functional intera ...... point proteins Rad9-Rad1-Hus1.
@en
Physical and functional interactions between MutY glycosylase homologue
@nl
type
label
Physical and functional intera ...... point proteins Rad9-Rad1-Hus1.
@en
Physical and functional interactions between MutY glycosylase homologue
@nl
prefLabel
Physical and functional intera ...... point proteins Rad9-Rad1-Hus1.
@en
Physical and functional interactions between MutY glycosylase homologue
@nl
P2093
P2860
P356
P1433
P1476
Physical and functional intera ...... point proteins Rad9-Rad1-Hus1.
@en
P2093
Ceslovas Venclovas
Chih-Chien Cheng
Dau-Yin Chang
P2860
P356
10.1042/BJ20060774
P407
P577
2006-11-01T00:00:00Z