Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
about
A large scale shRNA barcode screen identifies the circadian clock component ARNTL as putative regulator of the p53 tumor suppressor pathwayNEDD4-1 is a proto-oncogenic ubiquitin ligase for PTENA new role of NUAK1: directly phosphorylating p53 and regulating cell proliferationModulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portionCharge modification at multiple C-terminal lysine residues regulates p53 oligomerization and its nucleus-cytoplasm traffickingDDX3, a DEAD box RNA helicase, is deregulated in hepatitis virus-associated hepatocellular carcinoma and is involved in cell growth controlThe notch regulator MAML1 interacts with p53 and functions as a coactivatorHLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Negative regulation of p53 functions by Daxx and the involvement of MDM2Aurora B interacts with NIR-p53, leading to p53 phosphorylation in its DNA-binding domain and subsequent functional suppressionMetabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylationActivation of p53 by MEG3 non-coding RNAEvolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteinsInduction of SOX4 by DNA damage is critical for p53 stabilization and functionAcetylation is indispensable for p53 activationFBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activitySEI family of nuclear factors regulates p53-dependent transcriptional activationProteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradationAn essential function of the extreme C-terminus of MDM2 can be provided by MDMXING2 regulates the onset of replicative senescence by induction of p300-dependent p53 acetylationThe C terminus of p53 family proteins is a cell fate determinantChloroquine activates the p53 pathway and induces apoptosis in human glioma cellsIdentification, analysis, and prediction of protein ubiquitination sitesRegulation of p53 localization and transcription by the HECT domain E3 ligase WWP1Lysine acetylation: codified crosstalk with other posttranslational modificationsPLAGL2 controls the stability of Pirh2, an E3 ubiquitin ligase for p53PTTG/securin activates expression of p53 and modulates its functionSIRT1 regulates HIV transcription via Tat deacetylationModulation of p53 activity by IkappaBalpha: evidence suggesting a common phylogeny between NF-kappaB and p53 transcription factors.Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathwayApoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategiesRecent findings and technological advances in phosphoproteomics for cells and tissuesEvolution and functional cross-talk of protein post-translational modificationsEvasion of anti-growth signaling: A key step in tumorigenesis and potential target for treatment and prophylaxis by natural compounds.A perspective on dietary phytochemicals and cancer chemoprevention: oxidative stress, nrf2, and epigenomicsGuarding the 'translation apparatus': defective ribosome biogenesis and the p53 signaling pathwayThe protein quality control machinery regulates its misassembled proteasome subunitsStructural Insight into p53 Recognition by the 53BP1 Tandem Tudor DomainProteasome nuclear activity affects chromosome stability by controlling the turnover of Mms22, a protein important for DNA repair.
P2860
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P2860
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@ast
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@en
type
label
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@ast
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@en
prefLabel
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@ast
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@en
P1476
Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation.
@en
P2093
Christopher L Brooks
P304
P356
10.1016/S0955-0674(03)00003-6
P577
2003-04-01T00:00:00Z