Choose your partners: dimerization in eukaryotic transcription factors.
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Protein stickiness, rather than number of functional protein-protein interactions, predicts expression noise and plasticity in yeastMutational robustness of gene regulatory networksNFAT regulates the expression of AIF-1 and IRT-1: yin and yang splice variants of neointima formation and atherosclerosisEvolution of Gene Duplication in PlantsStructural Determinants of DNA Binding by a P. falciparum ApiAP2 Transcriptional RegulatorDesign and characterization of an enhanced repressor of human papillomavirus E2 proteinStaufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decayCrystal Structure of Inhibitor of Growth 4 (ING4) Dimerization Domain Reveals Functional Organization of ING Family of Chromatin-binding ProteinsA stable transcription factor complex nucleated by oligomeric AML1–ETO controls leukaemogenesisThe basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNAMethylated Cytosines Mutate to Transcription Factor Binding Sites that Drive Tetrapod EvolutionRegulation of Transcription Factors by Reactive Oxygen Species and Nitric Oxide in Vascular Physiology and Pathology.A conserved domain in the N-terminus is important for LEAFY dimerization and function in Arabidopsis thaliana.Evolution of a new function by degenerative mutation in cephalochordate steroid receptorsThe capacity for multistability in small gene regulatory networks.The leucine zipper domains of the transcription factors GCN4 and c-Jun have ribonuclease activity.Sequence motifs in MADS transcription factors responsible for specificity and diversification of protein-protein interaction.Elucidation of functional markers from Aspergillus nidulans developmental regulator FlbB and their phylogenetic distribution.Quantitative models for accelerated protein dissociation from nucleosomal DNA.Predicting the impact of alternative splicing on plant MADS domain protein functionLow-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution.Acetylation modulates prolactin receptor dimerization.Accurate discrimination of bHLH domains in plants, animals, and fungi using biologically meaningful sites.NaMYC2 transcription factor regulates a subset of plant defense responses in Nicotiana attenuataModel of how plants sense zinc deficiency.Lineage-specific transcription factors and the evolution of gene regulatory networksMutant Forkhead L2 (FOXL2) proteins associated with premature ovarian failure (POF) dimerize with wild-type FOXL2, leading to altered regulation of genes associated with granulosa cell differentiation.PC-TraFF: identification of potentially collaborating transcription factors using pointwise mutual information.The orientation of transcription factor binding site motifs in gene promoter regions: does it matter?SnRK1-triggered switch of bZIP63 dimerization mediates the low-energy response in plants.The Sweet Potato NAC-Domain Transcription Factor IbNAC1 Is Dynamically Coordinated by the Activator IbbHLH3 and the Repressor IbbHLH4 to Reprogram the Defense Mechanism against Wounding.Splice variant of the SND1 transcription factor is a dominant negative of SND1 members and their regulation in Populus trichocarpa.Phylogenetic analysis of F-bZIP transcription factors indicates conservation of the zinc deficiency response across land plantsThree transcription factors, HFR1, LAF1 and HY5, regulate largely independent signaling pathways downstream of phytochrome A.Heterogeneity of transcription factor binding specificity models within and across cell lines.Toxoplasma transcription factor TgAP2XI-5 regulates the expression of genes involved in parasite virulence and host invasion.Inhibition of BATF/JUN transcriptional activity protects against osteoarthritic cartilage destruction.Mechanisms of transcription factor evolution in Metazoa.bZIPs and WRKYs: two large transcription factor families executing two different functional strategiesDimerization of the DYT6 dystonia protein, THAP1, requires residues within the coiled-coil domain.
P2860
Q21093159-3343DFD2-00C6-47B0-9ADC-1A88D38969CEQ21560876-EFBB536D-9545-4116-8696-147C50AC1B23Q24298285-577CA42B-1846-4B8B-A6F2-7C466DB909CBQ26747070-D6777FE6-9EF1-45A4-9236-84375EA47588Q27658161-4414D4B0-F802-421B-B90A-7441616E0993Q27667487-C3D5FF58-C1BC-4415-8F60-B16D126E697EQ27677008-3E9E4312-4A34-4C0C-833E-4FE01B9991E0Q27677284-955C5648-7BBE-4D9D-A44B-4CEB2F3409E1Q27678844-520E4EC5-0230-4045-BA00-DA631C7C570AQ27688110-1AAA69D2-95CC-4A1B-BF27-08CEB072956FQ28597450-EF95A7BA-F92D-4B78-94DE-FA1607786575Q30275422-107AC86F-3608-4A2A-9367-2DBB7FB9A7F7Q33353351-863B865D-B883-4233-8089-23ED45B7DC1AQ33369082-86301C86-4F4E-4D23-BAA4-2B2BC3D768C6Q33505795-79C4EA02-3C77-49ED-AE62-A19AD2EF0921Q33588654-ED289F4F-3D04-4841-9002-DC5993B9E0B9Q33760996-F4B102F8-8017-4F19-8824-5843370CB950Q33851646-F6BF0AD6-4710-4DFE-A040-F5EE8B2848E3Q34115603-8E59D04A-9644-4DF6-BEC9-8ABF129583FCQ34147600-B6FB364C-C1EB-4206-B7F0-6781CD6F876BQ34171449-CE8924B8-8EDC-4441-A81A-F064118FCBC8Q34320685-C5CFB8C8-3158-4764-9933-3387FB8AF9D9Q34392946-74BD946F-1B61-41C4-95B5-C5D8384AAA7BQ34698884-0F76B592-DA7B-4F93-9DE1-863FFEF68104Q34817701-9E29F48C-41C3-4325-B6B6-D90C424EEFB9Q34987289-2A996D37-E877-41FC-966D-8E818F87BACFQ35222999-C4B1A776-CE36-4985-9D11-8992611E6FA3Q35857834-D073FCC0-9592-41CF-B16F-F0A1D782EFAFQ35945288-C8AD8F80-8C3D-4F7F-8C18-D4605A7685FCQ36022475-6C271B19-07E4-40C2-8D71-69327768367CQ36174005-F4C540E2-52FE-4F3C-B76A-EF8624ED3620Q36221697-3E5D06FA-55B9-412C-B42D-B835559D0176Q36409869-6E670157-93D6-4377-A341-86DEB6288AFBQ36907196-305546E2-8A43-468E-A046-C37F0D207070Q37148623-DEEA6A7B-D1B9-45FA-BCD1-71BB127C7DEFQ37312183-6EA51284-58E1-46F0-A0AE-A9E5C7AF6D9CQ37616997-D7353940-D727-41DE-ACA8-CB33A35978CDQ37623770-A2B32AA0-1756-40CF-AC01-11E39AE8C01FQ38211021-DBB8BC24-81FA-4A98-A594-4A1CC6E5C310Q38294642-00B3A9DE-2E80-4103-BF48-786B65CAF708
P2860
Choose your partners: dimerization in eukaryotic transcription factors.
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Choose your partners: dimerization in eukaryotic transcription factors.
@ast
Choose your partners: dimerization in eukaryotic transcription factors.
@en
Choose your partners: dimerization in eukaryotic transcription factors.
@nl
type
label
Choose your partners: dimerization in eukaryotic transcription factors.
@ast
Choose your partners: dimerization in eukaryotic transcription factors.
@en
Choose your partners: dimerization in eukaryotic transcription factors.
@nl
prefLabel
Choose your partners: dimerization in eukaryotic transcription factors.
@ast
Choose your partners: dimerization in eukaryotic transcription factors.
@en
Choose your partners: dimerization in eukaryotic transcription factors.
@nl
P1476
Choose your partners: dimerization in eukaryotic transcription factors.
@en
P2093
David L Robertson
Stephen G Oliver
P304
P356
10.1016/J.TIBS.2008.02.002
P577
2008-04-09T00:00:00Z