about
Both Max and TFE3 cooperate with Smad proteins to bind the plasminogen activator inhibitor-1 promoter, but they have opposite effects on transcriptional activityOpposing roles of FoxP1 and Nfat3 in transcriptional control of cardiomyocyte hypertrophyVisualization by BiFC of different C/EBPβ dimers and their interaction with HP1α reveals a differential subnuclear distribution of complexes in living cellsVisualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementationChanges in the distributions and dynamics of polycomb repressive complexes during embryonic stem cell differentiationCaenorhabditis elegans FOS-1 and JUN-1 regulate plc-1 expression in the spermatheca to control ovulation.Bimolecular fluorescence complementation analysis of inducible protein interactions: effects of factors affecting protein folding on fluorescent protein fragment association.Design and implementation of bimolecular fluorescence complementation (BiFC) assays for the visualization of protein interactions in living cells.Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells.KAP1 represses differentiation-inducible genes in embryonic stem cells through cooperative binding with PRC1 and derepresses pluripotency-associated genesBimolecular fluorescence complementation analysis of eukaryotic fusion products.Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity.Visualization of the Drosophila dKeap1-CncC interaction on chromatin illumines cooperative, xenobiotic-specific gene activation.Gel-based fluorescence resonance energy transfer (gelFRET) analysis of nucleoprotein complex architecture.Opposite orientations of a transcription factor heterodimer bind DNA cooperatively with interaction partners but have different effects on interferon-β gene transcriptionFos and Jun bend the AP-1 site: effects of probe geometry on the detection of protein-induced DNA bendingUbiquitin-mediated fluorescence complementation reveals that Jun ubiquitinated by Itch/AIP4 is localized to lysosomes.Probing FinO-FinP RNA interactions by site-directed protein-RNA crosslinking and gelFRET.DNA bending determines Fos-Jun heterodimer orientation.Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: implications for transcription factor cooperativity.Asymmetric recognition of nonconsensus AP-1 sites by Fos-Jun and Jun-Jun influences transcriptional cooperativity with NFAT1Visualization of ubiquitin conjugates using ubiquitin-mediated fluorescence complementation analysis.Bimolecular fluorescence complementation: visualization of molecular interactions in living cells.Synergistic transcription activation by Maf and Sox and their subnuclear localization are disrupted by a mutation in Maf that causes cataract.Visualization of Myc/Max/Mad family dimers and the competition for dimerization in living cells.DNA bending by Fos-Jun and the orientation of heterodimer binding depend on the sequence of the AP-1 site.Lysosomal localization of ubiquitinated Jun requires multiple determinants in a lysine-27-linked polyubiquitin conjugate.Complementary methods for studies of protein interactions in living cells.The transcription activation domains of Fos and Jun induce DNA bending through electrostatic interactions.Overcoming uncertainty through advances in fluorescence imaging of molecular processes in cells.The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription.Design of fusion proteins for bimolecular fluorescence complementation (BiFC).Visualization of protein interactions in living Caenorhabditis elegans using bimolecular fluorescence complementation analysis.Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in live cells.Visualization of protein interactions in living cells using bimolecular fluorescence complementation (BiFC) analysis.Transcriptional cooperativity: bending over backwards and doing the flip.ATR-101 inhibits cholesterol efflux and cortisol secretion by ATP-binding cassette transporters, causing cytotoxic cholesterol accumulation in adrenocortical carcinoma cells.Zen and the art of Fos and JunRegulation of c-fos expression in transgenic mice requires multiple interdependent transcription control elementsTranscription factor interactions: basics on zippers
P50
Q28205279-3423444E-C709-49DE-837D-F3207F3E2B37Q28579882-008E1A2C-6360-44A0-82F5-3CFEFB85A3C7Q28589158-7707260E-A873-4A98-B00A-DDE6BC5B2CCAQ29616037-C8BDAA4B-35C9-4985-919A-778E4DAC50D6Q30481667-5372E24B-A5CA-42F3-95DF-F2BDA0A4CAF8Q30489897-2E6A8513-31C8-4DC9-90F8-370CDFCAF5A6Q30494297-92FEEE07-5EBB-46F7-B0AF-2EADFF7FA856Q33280958-2DC3E0D4-7A20-4E26-A052-20E69EE71A88Q33345889-69CF7BCD-317C-4E63-8B49-D6CE1890E070Q33602596-ED2C4D80-C98E-4D20-89FB-A3C9F993C359Q34052041-DF3F61A8-6CFD-4EF9-808F-4520F725B5FDQ34279362-7DF13CB2-807F-4659-A3B8-B09C8B0C915EQ34341268-5CE89E67-A96D-4FB3-88B8-F2DF27AFEF8CQ34370584-94A3C3E8-A366-4C98-BEC8-5FDBAC7AB674Q36234728-D70730DF-FBCF-498C-B74D-B42E87C8D0F6Q37326928-7AAEAB71-3E3B-44BA-BDA5-7E0E2F81261FQ37570487-5F57F718-B0F3-4025-BAAF-C610640CDBC9Q38287659-F89D9954-A67A-4FA8-9C72-FE92680269F7Q38332299-91031883-7868-49ED-9C33-9BBA45CCE608Q38334205-AF0585BE-55C5-4B6A-9F0A-6100F239ADA4Q38357668-D3984C97-1A1E-4856-BE4C-CB7AA6EAF056Q39088968-3B4EFDE5-C46C-4DB6-93DC-BFEA0D1EFEAEQ39304667-CE801230-8C2D-42FD-846A-2D74338EAB44Q40544924-AE11FAD8-BEB7-4C9F-B67E-7A1140007AE4Q40560471-A123D40A-6729-48B7-856A-63CE5367BC8CQ41828272-2D811763-03AB-4A90-9814-E85B0EE52A90Q42044297-3907751B-E3A8-4EFB-9E24-B7CC5E0AFFB1Q42380047-E65FD5C5-3136-4111-80F7-EACAFF2E5251Q42618695-DDDA4678-071C-45BF-A39F-75AEF5900E06Q43011788-921EED07-380E-4A45-9267-B552F3A898D4Q44455864-4D4175AC-C910-47A9-935D-6ACD39343EA5Q45534392-7BE9B811-BF3B-4DB9-BB85-A22E2A41FFA2Q46499589-40F8A13B-2319-4B8E-8EFA-5B853EC5341EQ46848084-FE05BA65-ADF4-479C-A42C-6A9BE2574FE2Q47757877-5AA2A465-C621-48D7-8A6E-3483A69AD5D2Q47948874-AB976997-6CA1-4372-AC07-92E8C6D0CE54Q48121227-A39D6792-8CDF-4AC7-9649-81EB8978C22FQ57963145-DF382FB1-CDD8-45D5-B00E-62F1DA24BCAFQ57963165-5762624E-B117-44D4-891A-2ED5B34B49E9Q57963223-EA90D50B-8558-40E2-AB9A-6983352C7707
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Tom K. Kerppola
@ast
Tom K. Kerppola
@en
Tom K. Kerppola
@es
Tom K. Kerppola
@sl
type
label
Tom K. Kerppola
@ast
Tom K. Kerppola
@en
Tom K. Kerppola
@es
Tom K. Kerppola
@sl
altLabel
Tom K. Kerppola
@en
Tom K. W. Kerppola
@en
Tom Kerppola
@en
Tom Klaus Kerppola
@en
Tom Klaus William Kerppola
@en
prefLabel
Tom K. Kerppola
@ast
Tom K. Kerppola
@en
Tom K. Kerppola
@es
Tom K. Kerppola
@sl
P106
P1153
7004377838
P21
P31
P3835
tom-kerppola
P496
0000-0002-0611-9446