Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling.
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The human Rad9 checkpoint protein stimulates the carbamoyl phosphate synthetase activity of the multifunctional protein CADInteraction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cellsHuman checkpoint protein hRad9 functions as a negative coregulator to repress androgen receptor transactivation in prostate cancer cellsThe human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilonHsp90: A New Player in DNA Repair?Human RAD18 interacts with ubiquitylated chromatin components and facilitates RAD9 recruitment to DNA double strand breaksGli1 protein regulates the S-phase checkpoint in tumor cells via Bid protein, and its inhibition sensitizes to DNA topoisomerase 1 inhibitorsThe effect of Hus1 on ionizing radiation sensitivity is associated with homologous recombination repair but is independent of nonhomologous end-joiningViral transport of DNA damage that mimics a stalled replication fork.Loss of RPA1 induces Chk2 phosphorylation through a caffeine-sensitive pathway.Rad9 modulates the P21WAF1 pathway by direct association with p53.In my end is my beginning: control of end resection and DSBR pathway 'choice' by cyclin-dependent kinases.TLK1B promotes repair of DSBs via its interaction with Rad9 and Asf1.Functional compartmentalization of Rad9 and Hus1 reveals diverse assembly of the 9-1-1 complex components during the DNA damage response in Leishmania.Rad9A is required for G2 decatenation checkpoint and to prevent endoreduplication in response to topoisomerase II inhibitionATR autophosphorylation as a molecular switch for checkpoint activation.Cell cycle G2/M arrest through an S phase-dependent mechanism by HIV-1 viral protein R.The RAD9-RAD1-HUS1 (9.1.1) complex interacts with WRN and is crucial to regulate its response to replication fork stallingPhosphorylation of Xenopus Rad1 and Hus1 defines a readout for ATR activation that is independent of Claspin and the Rad9 carboxy terminusHuman RAD9 checkpoint control/proapoptotic protein can activate transcription of p21.Phenothiazine Inhibitors of TLKs Affect Double-Strand Break Repair and DNA Damage Response Recovery and Potentiate Tumor Killing with Radiomimetic Therapy.A role for the arginine methylation of Rad9 in checkpoint control and cellular sensitivity to DNA damage.Tousled-like kinase-dependent phosphorylation of Rad9 plays a role in cell cycle progression and G2/M checkpoint exit.Mechanisms of apoptosis induction by nucleoside analogs.Increased 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.Association of the Rad9-Rad1-Hus1 checkpoint clamp with MYH DNA glycosylase and DNA.Contributions of Rad9 to tumorigenesis.Regulation of NEIL1 protein abundance by RAD9 is important for efficient base excision repairHeat shock protein 90 inhibition sensitizes acute myelogenous leukemia cells to cytarabine.Chk1 Activation Protects Rad9A from Degradation as Part of a Positive Feedback Loop during Checkpoint Signalling.TLK1B mediated phosphorylation of Rad9 regulates its nuclear/cytoplasmic localization and cell cycle checkpoint.ATM-dependent phosphorylation of the checkpoint clamp regulates repair pathways and maintains genomic stabilityMultiple functions of rad9 for preserving genomic integrityCandidate protein biodosimeters of human exposure to ionizing radiation.TopBP1 activates ATR through ATRIP and a PIKK regulatory domainThe checkpoint clamp protein Rad9 facilitates DNA-end resection and prevents alternative non-homologous end joining.Cisplatin-induced DNA damage activates replication checkpoint signaling components that differentially affect tumor cell survival.Role of the checkpoint clamp in DNA damage response.The Rad9-Hus1-Rad1 (9-1-1) clamp activates checkpoint signaling via TopBP1.
P2860
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P2860
Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling.
@en
type
label
Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling.
@en
prefLabel
Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling.
@en
P2093
P2860
P356
P1476
Phosphorylation of human Rad9 is required for genotoxin-activated checkpoint signaling.
@en
P2093
Andrea J Oestreich
Benjamin T Vroman
Howard B Lieberman
Kenneth L Johnson
Kevin M Hopkins
Larry M Karnitz
Pia Roos-Mattjus
Stephen Naylor
P2860
P304
24428-24437
P356
10.1074/JBC.M301544200
P407
P577
2003-04-21T00:00:00Z