p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex
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Functional cooperation between FACT and MCM helicase facilitates initiation of chromatin DNA replicationHIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2Histone displacement during nucleotide excision repairNek9, a novel FACT-associated protein, modulates interphase progressionFACT is a sensor of DNA torsional stress in eukaryotic cells.Mutant versions of the S. cerevisiae transcription elongation factor Spt16 define regions of Spt16 that functionally interact with histone H3VMY-1-103, a dansylated analog of purvalanol B, induces caspase-3-dependent apoptosis in LNCaP prostate cancer cells.The histone chaperone FACT: structural insights and mechanisms for nucleosome reorganization.Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements.Myotubularin-related proteins 3 and 4 interact with polo-like kinase 1 and centrosomal protein of 55 kDa to ensure proper abscission.Histone chaperone FACT coordinates nucleosome interaction through multiple synergistic binding events.FACT Assists Base Excision Repair by Boosting the Remodeling Activity of RSC.Biphasic chromatin binding of histone chaperone FACT during eukaryotic chromatin DNA replication.Crystal Structure of Human SSRP1 Middle Domain Reveals a Role in DNA BindingSsrp1a controls organogenesis by promoting cell cycle progression and RNA synthesis.Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.The Structure-Specific Recognition Protein 1 Associates with Lens Epithelium-Derived Growth Factor Proteins and Modulates HIV-1 ReplicationThyroid tumors: novel insights from proteomic studies.CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity.Domain organization of the yeast histone chaperone FACT: the conserved N-terminal domain of FACT subunit Spt16 mediates recovery from replication stressThe role of FACT in making and breaking nucleosomes.Gearing up chromatin: A role for chromatin remodeling during the transcriptional restart upon DNA damageProtein kinase CK2 phosphorylates the high mobility group domain protein SSRP1, inducing the recognition of UV-damaged DNA.Protein kinase CK2 in breast cancer: the CK2β regulatory subunit takes center stage in epithelial plasticity.Targeting CK2-driven non-oncogene addiction in B-cell tumors.Differential responses to genotoxic agents between induced pluripotent stem cells and tumor cell lines.Identification of a novel protein interaction motif in the regulatory subunit of casein kinase 2.Radio-sensitization of human leukaemic MOLT-4 cells by DNA-dependent protein kinase inhibitor, NU7441.Curaxins: anticancer compounds that simultaneously suppress NF-κB and activate p53 by targeting FACT.Dynamic regulation of the translation initiation helicase complex by mitogenic signal transduction to eukaryotic translation initiation factor 4G.Structure-specific recognition protein 1 facilitates microtubule growth and bundling required for mitosis.Differential regulation of mitogen- and stress-activated protein kinase-1 and -2 (MSK1 and MSK2) by CK2 following UV radiation.The high-mobility-group box protein SSRP1/T160 is essential for cell viability in day 3.5 mouse embryos.Control of p53 nuclear accumulation in stressed cells.Activation of Casein Kinase II by Gallic Acid Induces BIK-BAX/BAK-Mediated ER Ca++-ROS-Dependent Apoptosis of Human Oral Cancer Cells.Regulation of TP53 Activity through PhosphorylationSerine 392 phosphorylation modulates p53 mitochondrial translocation and transcription-independent apoptosis.CK2 binds FACTCK2:FACT phosphorylates TP53SSRP1 Cooperates with PARP and XRCC1 to Facilitate Single-Strand DNA Break Repair by Chromatin Priming.
P2860
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P2860
p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@ast
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@en
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@nl
type
label
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@ast
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@en
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@nl
prefLabel
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@ast
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@en
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@nl
P2860
P3181
P356
P1476
p53 serine 392 phosphorylation ...... f the CK2.hSPT16.SSRP1 complex
@en
P2093
David M Keller
P2860
P304
P3181
P356
10.1074/JBC.M209820200
P407
P577
2002-12-20T00:00:00Z