Degringolade, a SUMO-targeted ubiquitin ligase, inhibits Hairy/Groucho-mediated repression.
about
Function and regulation of SUMO proteasesKaposi's sarcoma-associated herpesvirus K-Rta exhibits SUMO-targeting ubiquitin ligase (STUbL) like activity and is essential for viral reactivationThe Drosophila STUbL protein Degringolade limits HES functions during embryogenesis.Developmental regulation and spatiotemporal redistribution of the sumoylation machinery in the rat central nervous system.SUMOylation of FOXM1B alters its transcriptional activity on regulation of MiR-200 family and JNK1 in MCF7 human breast cancer cellsRNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage.Drosophila COP9 signalosome subunit 7 interacts with multiple genomic loci to regulate development.Sumoylation controls the timing of Tup1-mediated transcriptional deactivation.STUbL-mediated degradation of the transcription factor MATα2 requires degradation elements that coincide with corepressor binding sitesThe SUMO pathway promotes basic helix-loop-helix proneural factor activity via a direct effect on the Zn finger protein senselessGlobal SUMO Proteome Responses Guide Gene Regulation, mRNA Biogenesis, and Plant Stress Responses.STUbLs in chromatin and genome stability.Global analysis of SUMO chain function reveals multiple roles in chromatin regulation.Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin-related modifiers.Evolution of SUMO Function and Chain Formation in Insects.Long-Term Memory in Drosophila Is Influenced by Histone Deacetylase HDAC4 Interacting with SUMO-Conjugating Enzyme Ubc9.Screening and Analysis of Janelia FlyLight Project Enhancer-Gal4 Strains Identifies Multiple Gene Enhancers Active During Hematopoiesis in Normal and Wasp-Challenged Drosophila Larvae.Protein sumoylation in brain development, neuronal morphology and spinogenesis.SUMOylation in Drosophila Development.The Groucho/Transducin-like enhancer of split protein family in animal development.SUMO in Drosophila Development.Roles of FoxM1 in cell regulation and breast cancer targeting therapy.Loss of SUMOylation on ATF3 inhibits proliferation of prostate cancer cells by modulating CCND1/2 activity.SUMOylation of ATF3 alters its transcriptional activity on regulation of TP53 gene.SUMOylation of Wor1 by a novel SUMO E3 ligase controls cell fate in Candida albicans.RNF4-Dependent Oncogene Activation by Protein Stabilization.Acidic residue Glu199 increases SUMOylation level of nuclear hormone receptor NR5A1.A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA.The Hydra small ubiquitin-like modifier.DNA Binding by the MATα2 Transcription Factor Controls its Access to Alternative Ubiquitin-modification Pathways.DNA Damage Tolerance Pathway Choice Through Uls1 Modulation of Srs2 SUMOylation in Saccharomyces cerevisiae.Multiple crosstalks between mRNA biogenesis and SUMO.The Biology of SUMO-Targeted Ubiquitin Ligases in Drosophila Development, Immunity, and Cancer.SUMO-triggered ubiquitination of NR4A1 controls macrophage cell death.
P2860
Q26991707-13BB3D81-FB0C-41DE-84AD-A97A04148C3BQ28535568-AD36C6CA-9F0B-423E-8385-51CE8818D5A8Q30499442-7FB7C9DF-4BCD-4DF5-954F-272AA7511413Q31052469-0084CFC1-0E0B-4368-8C3E-0306B5A59A70Q33907729-9AC1EFCF-21CB-48A8-A47A-906999E41D71Q34040089-B3FE64C4-AD67-45DC-8E3F-6835CF0A8BF1Q34115607-6334E0E6-1D3B-4BBB-9D16-997E78EE1762Q35180097-437BE0D0-BB3E-401E-9A1F-67BCE58CF9E8Q36115369-F4ED6894-7E53-4A72-ABB6-1F3F95C7B0E9Q36155106-70C08B3A-FFD5-40F7-99CE-FEFD4C2459A4Q36238048-205D97E6-736A-4EEE-878C-B75BB2223048Q36426331-68B9D550-2222-4830-AD00-80FA183A5183Q36732737-81D5B1EE-2116-4CB9-967F-7323D87CF342Q36763766-56CD10C1-6002-4063-AEBE-83C413F193F9Q36899962-EA55DF67-6811-4DDC-B96C-43343E127668Q37076788-65F49F6E-7BCF-4FAE-907F-1D4DB81E4603Q37629297-BC055B12-215C-48D1-84A1-46D839979168Q38125942-3822762A-68AA-466F-8A8A-D9AA3074C4A7Q38223674-22F49042-A923-471E-A36D-75177BDDFC73Q38546813-1E872D89-5463-4876-B946-D527BA46F61FQ38961122-BA9A5A76-D6D5-4922-BB26-F652CD17D74CQ39125526-63B04595-B2F9-474A-A50D-634D1321F6FBQ39165172-F828258B-708D-4BCA-8D17-0D30708A5FF0Q39275947-1067DF97-11DD-40CB-B353-4B212FDCDAA8Q40796318-2AB823DD-04B5-4198-B2F8-BE9E282FEF52Q41988752-6E666EC5-C468-42D6-8448-9DC96D34AB74Q42144598-41A4D6B3-BA7F-4176-BDD0-0B96D2C14344Q42178008-440925DD-B087-4C73-B3D3-DC4E22AE0EB5Q43638817-78C7C615-5F09-4253-8796-636E3339FD64Q47212910-BD2A54FF-F294-4A4E-B827-1AA2671D0A89Q48363794-62E14A9F-46A1-40F5-93C0-020FCAEF104FQ51069800-C9EB3EAA-A258-440D-A3BC-9749923015EAQ52721924-CDFBFBF8-FFF5-4590-810A-A9EDE05C4D32Q53793540-C9164860-E33C-4B17-B806-DEB0457C76C2
P2860
Degringolade, a SUMO-targeted ubiquitin ligase, inhibits Hairy/Groucho-mediated repression.
description
2011 nî lūn-bûn
@nan
2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@ast
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@en
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@nl
type
label
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@ast
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@en
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@nl
prefLabel
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@ast
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@en
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@nl
P2093
P2860
P356
P1433
P1476
Degringolade, a SUMO-targeted ...... y/Groucho-mediated repression.
@en
P2093
Amir Orian
Bella Koltun
Dorit Kenyagin
Jeffrey J Delrow
Kevin C Barry
Susan M Parkhurst
Taryn M Phippen
P2860
P304
P356
10.1038/EMBOJ.2011.42
P407
P577
2011-02-22T00:00:00Z