The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair
about
Wild-type p53-induced phosphatase 1 dephosphorylates histone variant gamma-H2AX and suppresses DNA double strand break repairLZAP inhibits p38 MAPK (p38) phosphorylation and activity by facilitating p38 association with the wild-type p53 induced phosphatase 1 (WIP1)PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpointsOncogenic Wip1 phosphatase is inhibited by miR-16 in the DNA damage signaling pathwayPhosphorylation of human oxoguanine DNA glycosylase (alpha-OGG1) modulates its functionBase Excision Repair, a Pathway Regulated by Posttranslational ModificationsRegulation of the antioncogenic Chk2 kinase by the oncogenic Wip1 phosphataseA chemical inhibitor of PPM1D that selectively kills cells overexpressing PPM1D.Cell cycle-specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA.The oncogenic phosphatase WIP1 negatively regulates nucleotide excision repairWIP1 phosphatase as pharmacological target in cancer therapy.Expression of a homeostatic regulator, Wip1 (wild-type p53-induced phosphatase), is temporally induced by c-Jun and p53 in response to UV irradiation.Involvement of oxidatively damaged DNA and repair in cancer development and aging.Single-strand selective monofunctional uracil-DNA glycosylase (SMUG1) deficiency is linked to aggressive breast cancer and predicts response to adjuvant therapy.Viewing serine/threonine protein phosphatases through the eyes of drug designersTruncating mutations of PPM1D are found in blood DNA samples of lung cancer patients.Human base excision repair complex is physically associated to DNA replication and cell cycle regulatory proteinsMolecular determinants of ovarian cancer chemoresistance: new insights into an old conundrumRegulation of the Wip1 phosphatase and its effects on the stress response.The type 2C phosphatase Wip1: an oncogenic regulator of tumor suppressor and DNA damage response pathways.Protein phosphatase 1 inhibits p53 signaling by dephosphorylating and stabilizing Mdmx.DNA damage signaling induced by the G-quadruplex ligand 12459 is modulated by PPM1D/WIP1 phosphatase.A unified view of base excision repair: lesion-dependent protein complexes regulated by post-translational modification.Discovery of protein phosphatase 2C inhibitors by virtual screening.Essential phosphatases and a phospho-degron are critical for regulation of SRC-3/AIB1 coactivator function and turnoverRole of type 2C protein phosphatases in growth regulation and in cellular stress signaling.The dark side of a tumor suppressor: anti-apoptotic p53.Loss of Wip1 sensitizes cells to stress- and DNA damage-induced apoptosis.Substrate specificity and excision kinetics of natural polymorphic variants and phosphomimetic mutants of human 8-oxoguanine-DNA glycosylase.Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase.Oxidized base damage and single-strand break repair in mammalian genomes: role of disordered regions and posttranslational modifications in early enzymes.Wip1 phosphatase in breast cancer.Ugene, a newly identified protein that is commonly overexpressed in cancer and binds uracil DNA glycosylase.The role of DNA damage responses in p53 biology.Investigation of N-Terminal Phospho-Regulation of Uracil DNA Glycosylase Using Protein Semisynthesis.BERing the burden of damage: Pathway crosstalk and posttranslational modification of base excision repair proteins regulate DNA damage management.Glycogen Synthase Kinase 3 (GSK-3)-mediated Phosphorylation of Uracil N-Glycosylase 2 (UNG2) Facilitates the Repair of Floxuridine-induced DNA Lesions and Promotes Cell Survival.The protein p17 signaling pathways in cancer.Knockdown of protein phosphatase magnesium-dependent 1 (PPM1D) through lentivirus-mediated RNA silencing inhibits colorectal carcinoma cell proliferation.Wip1 phosphatase is associated with chromatin and dephosphorylates gammaH2AX to promote checkpoint inhibition.
P2860
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P2860
The p53-induced oncogenic phosphatase PPM1D interacts with uracil DNA glycosylase and suppresses base excision repair
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
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
name
The p53-induced oncogenic phos ...... uppresses base excision repair
@ast
The p53-induced oncogenic phos ...... uppresses base excision repair
@en
The p53-induced oncogenic phos ...... uppresses base excision repair
@nl
type
label
The p53-induced oncogenic phos ...... uppresses base excision repair
@ast
The p53-induced oncogenic phos ...... uppresses base excision repair
@en
The p53-induced oncogenic phos ...... uppresses base excision repair
@nl
prefLabel
The p53-induced oncogenic phos ...... uppresses base excision repair
@ast
The p53-induced oncogenic phos ...... uppresses base excision repair
@en
The p53-induced oncogenic phos ...... uppresses base excision repair
@nl
P2093
P1433
P1476
The p53-induced oncogenic phos ...... uppresses base excision repair
@en
P2093
Bonnie Nannenga
Dora Bocangel
Hiroshi Yamaguchi
Lawrence A Donehower
Xiongbin Lu
P304
P356
10.1016/J.MOLCEL.2004.08.007
P407
P577
2004-08-27T00:00:00Z