about
Interaction of the fork head domain transcription factor MPP2 with the human papilloma virus 16 E7 protein: enhancement of transformation and transactivationMethylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusiveSIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310Regulation of NF-κB signalling by the mono-ADP-ribosyltransferase ARTD10GAR22β regulates cell migration, sperm motility, and axoneme structure.Function and regulation of the transcription factors of the Myc/Max/Mad networkIdentification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimersA human T-cell lymphotropic virus type 1 enhancer of Myc transforming potential stabilizes Myc-TIP60 transcriptional interactionsSH3TC2, a protein mutant in Charcot-Marie-Tooth neuropathy, links peripheral nerve myelination to endosomal recyclingMolecular simulation-based structural prediction of protein complexes in mass spectrometry: the human insulin dimerThe protein kinase DYRK1A phosphorylates the splicing factor SF3b1/SAP155 at Thr434, a novel in vivo phosphorylation sitePhosphorylation by Cdk2 is required for Myc to repress Ras-induced senescence in cotransformation.The transcription factor YY1 is a substrate for Polo-like kinase 1 at the G2/M transition of the cell cycle.TGFβ1 enhances MAD1 expression and stimulates promoter-bound Pol II phosphorylation: basic functions of C/EBP, SP and SMAD3 transcription factorsSignaling by IL-31 and functional consequences.Yersinia enterocolitica YopT and Clostridium difficile toxin B induce expression of GILZ in epithelial cellsAcetylation of the c-MYC oncoprotein is required for cooperation with the HTLV-1 p30(II) accessory protein and the induction of oncogenic cellular transformation by p30(II)/c-MYC.Regulation of cyclin D2 gene expression by the Myc/Max/Mad network: Myc-dependent TRRAP recruitment and histone acetylation at the cyclin D2 promoter.ING5 is phosphorylated by CDK2 and controls cell proliferation independently of p53The c-MYC oncoprotein, the NAMPT enzyme, the SIRT1-inhibitor DBC1, and the SIRT1 deacetylase form a positive feedback loop.Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).A role for the p34cdc2 kinase and phosphatases in the regulation of phosphorylation and disassembly of lamin B2 during the cell cycleStructural prediction of the interaction of the tumor suppressor p27KIP1 with cyclin A/CDK2 identifies a novel catalytically relevant determinantDynamic subcellular localization of the mono-ADP-ribosyltransferase ARTD10 and interaction with the ubiquitin receptor p62.The Mad side of the Max network: antagonizing the function of Myc and more.Inhibition of SIRT2 suppresses hepatic fibrosis.Targeted inactivation of a developmentally regulated neural plectin isoform (plectin 1c) in mice leads to reduced motor nerve conduction velocityNegative charge at the casein kinase II phosphorylation site is important for transformation but not for Rb protein binding by the E7 protein of human papillomavirus type 16.Toward a unified nomenclature for mammalian ADP-ribosyltransferases.MAD1 and its life as a MYC antagonist: an update.Regulation of gene transcription by the oncoprotein MYC.Regulation of sirtuin function by posttranslational modificationsCytokines and the skin barrier.Macrodomain-containing proteins: regulating new intracellular functions of mono(ADP-ribosyl)ation.Function and regulation of the mono-ADP-ribosyltransferase ARTD10.DNA binding of Myc/Max/Mad network complexes to oligonucleotides containing two E box elements: c-Myc/Max heterodimers do not bind DNA cooperatively.Phosphorylation of the transcription factor YY1 by CK2α prevents cleavage by caspase 7 during apoptosis.Myc and Max associate in vivo.YY1 binding to a subset of p53 DNA-target sites regulates p53-dependent transcription.Sulfoximines as ATR inhibitors: Analogs of VE-821.
P50
Q22010674-8E39516B-5678-482A-A47A-D5333C468B60Q24295056-8B021E88-945A-4845-B1DD-B9F137CC3596Q24307545-4B4BF405-B368-4FCB-989C-6A318F586B3EQ24338265-32BE268A-D2DE-447E-81D0-9E314FD65D8FQ27305320-9A51B34E-47C5-4FE8-99A8-B045F65339D0Q28198743-198C5AF8-7068-45DD-963F-28A64B7CC2CDQ28256828-EEE06D76-F312-42BB-A576-18AB134877EEQ28259102-9803978A-5D32-4A3B-B381-774B9305412FQ28292722-1363B861-8B65-40CF-88C5-53E347CEDDAEQ28655834-2557F467-FC6E-4307-BD8A-6D8700F7CA14Q33235281-7A99F120-2B68-40C4-90C4-2D2C29BA80B2Q33591386-3BF8D66E-28DC-4A17-B1DA-4416F41F911EQ33799237-3907FCF4-0031-4B8F-8298-978BED4E4BD1Q33827621-D2496636-42B2-44FF-8A42-21C1629A3D4FQ34222387-DA75D5D8-F097-45E9-A1A9-83403C0283F4Q34336672-CFC1C2D1-9C05-41B7-A0BD-8C9B7AB62AD6Q35071356-F41DC97F-E719-4007-B055-E49EF426AEE5Q35080744-E6DD4EDF-E4C0-4F55-A7FA-CEA8769736B1Q35599241-DD8BFA1A-6ED9-4ADB-B2C2-5FB26A634800Q35709058-FF4B20C3-4A12-4A9C-BA0C-B64ADF885422Q35788698-58D9D4DE-863E-40C3-82FA-53505A3EA2DDQ35923400-57361C63-3749-40F4-94D5-606F6DB860BBQ36240680-ACCF215F-5B0C-4ACD-BAEA-2A6DDD141DFDQ36430648-968FDC99-29F6-4A7B-BA11-84F86101DC40Q36451356-880523E0-9D17-49F5-9E79-19D0DF3811BAQ37071786-EE0C2F1D-3CCD-407A-BECC-F0E6E58DDF08Q37446692-3FCF8C3B-048F-4A8B-AC64-DA86F0FF5AA6Q37531695-AE949EE5-FD2A-4FAA-B687-039145C3865EQ37682470-A1C848CF-3E35-4818-8AC5-8D9EBAFC5495Q37932115-1DF0C4FB-898B-4253-9451-1DA1EDC860A4Q37974026-172DF8D4-97F3-4023-9926-4A7E625E7735Q37992055-A386D37F-AB0B-4503-BBD1-2C6D4AE97809Q38093338-34F2D85E-B1AA-4596-B8CA-FE343F794464Q38111969-99D6FB56-D707-4888-9CF1-90E571B316BEQ38216167-E1D8B446-EFF0-452C-B515-B7C7161A04D7Q38319001-AA727B76-1631-419C-8EE4-BCFB86480C99Q38329332-E206CBED-306C-4164-A26C-077889CFFE67Q38331177-0D268261-992F-4FB5-B406-383776045825Q38341827-2098DB3A-67E2-43AC-8887-4586854CF29DQ38704443-FB7D3C8C-2845-47BB-8891-702A658FB74A
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Bernhard Lüscher
@ast
Bernhard Lüscher
@en
Bernhard Lüscher
@es
Bernhard Lüscher
@sl
type
label
Bernhard Lüscher
@ast
Bernhard Lüscher
@en
Bernhard Lüscher
@es
Bernhard Lüscher
@sl
prefLabel
Bernhard Lüscher
@ast
Bernhard Lüscher
@en
Bernhard Lüscher
@es
Bernhard Lüscher
@sl
P1053
A-7330-2011
P106
P21
P31
P3829
P496
0000-0002-9622-8709