In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
about
Stabilization and activation of p53 by the coactivator protein TAFII31Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimerStructures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin.Importin α/β mediates nuclear import of individual SUMO E1 subunits and of the holo-enzymeSUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damageCrystal Structure of UBA2ufd-Ubc9: Insights into E1-E2 Interactions in Sumo PathwaysSIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase IIYeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates.Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins.SUMO-1 conjugation to human DNA topoisomerase II isozymesActivation of transforming growth factor-beta signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4Transforming growth factor-beta-mediated signaling via the p38 MAP kinase pathway activates Smad-dependent transcription through SUMO-1 modification of Smad4Sumo-1 modification regulates the DNA binding activity of heat shock transcription factor 2, a promyelocytic leukemia nuclear body associated transcription factorSumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymesPIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcriptionPleiotropic effects of ATP.Mg2+ binding in the catalytic cycle of ubiquitin-activating enzymeA novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphaseBiosynthesis of SUMOylated Proteins in Bacteria Using the Trypanosoma brucei Enzymatic SystemConstruction of a mouse Aos1-Uba2 chimeric SUMO-E1 enzyme, mAU, and its expression in baculovirus-insect cellsSmall ubiquitin-like modifier (SUMO) modification of zinc finger protein 131 potentiates its negative effect on estrogen signalingFunctional interaction between human herpesvirus 6 immediate-early 2 protein and ubiquitin-conjugating enzyme 9 in the absence of sumoylation.Interactions between PIAS proteins and SOX9 result in an increase in the cellular concentrations of SOX9.Genetic and proteomic evidence for roles of Drosophila SUMO in cell cycle control, Ras signaling, and early pattern formation.A manually curated network of the PML nuclear body interactome reveals an important role for PML-NBs in SUMOylation dynamics.Regulation of double-strand break-induced mammalian homologous recombination by UBL1, a RAD51-interacting proteinIdentification of the non-structural influenza A viral protein NS1A as a bona fide target of the Small Ubiquitin-like MOdifier by the use of dicistronic expression constructsSUMO/sentrin: protein modifiers regulating important cellular functions.Regulation of Ets function by protein - protein interactions.Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation.Emerging roles of SUMO modification in arthritis.The aryl hydrocarbon receptor nuclear transporter is modulated by the SUMO-1 conjugation system.CBX4-mediated SUMO modification regulates BMI1 recruitment at sites of DNA damageSUMOylation represses Nanog expression via modulating transcription factors Oct4 and Sox2Small ubiquitin-related modifier-1 modification mediates resolution of CREB-dependent responses to hypoxiaPML-mediated signaling and its role in cancer stem cells.SUMO: of branched proteins and nuclear bodies.Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation.Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport.Versatile protein tag, SUMO: its enzymology and biological function.
P2860
Q24291008-5E46E56C-45EE-4324-9650-1112BF4F27E7Q24301571-BCE91E2F-9F35-4C43-A34A-283F0693694FQ24338548-4C13EC57-5E41-44B8-BBF6-766466C1C9D3Q24537390-27D589E5-982E-441A-A33E-BFF28681742CQ24613093-25EBBC77-2D2B-44D2-BEA5-DE09C5ADB5C8Q24682811-AF69950C-D8B6-41D5-AEA2-5A918B42B770Q27666500-65C1BEC2-0EC1-49A3-92B5-E8A282BA0CDAQ27931553-5D7E37A1-F82B-4685-88A8-444A0A7CF325Q27935103-0C32F3EA-F257-4A60-BD55-EE346D1435A0Q27936336-1E0FAEFF-B9CB-4AC9-B370-F806E35CD6AEQ28138899-2137E3E4-98B2-4FE7-A279-9631364C47ACQ28181238-7E1E1E18-A576-41BF-B9DF-8805E8D15294Q28205342-B94A4A9A-C5E5-4586-9F45-D832217189CDQ28207780-7FBB022E-6BE1-4812-84CD-60490D44B797Q28210085-D57AE94E-D070-4AC3-9A6A-978A432949C5Q28217862-A59F9E38-B4CF-46ED-9EBA-25EBD22B6C34Q28305802-DAD8CED6-DD4B-4158-A185-4E399FDE3D53Q28509495-E1569F19-F35C-432F-95D7-BF8BF3D484BDQ28547134-BD9EBEF4-2C7D-4BC1-8EE1-48087A895F1AQ30360283-D86A002D-9E5F-4C44-A13E-E2C6A8DC889EQ30419271-ADE39B74-AAC9-41B7-9DB3-FD0BC786CA1BQ30827308-96EE288A-B601-4D34-BF13-825B9490FDD1Q33237313-4BC236FD-BB90-4E59-9458-726B90F1A1B2Q33468445-97F8C8AF-F4D4-4275-9D4C-0BE63C37292BQ33596988-E64A7059-70E6-4253-8039-EF8EEE60CED5Q33615409-84C63C15-FA77-4CDC-AC5B-5ADDBDA1D804Q33711733-39100461-9AC5-4161-9449-F02AF5500936Q33765355-E82FDE20-BFFF-4F1D-9591-9C15CB802137Q33933221-8662E360-C0AA-4DA1-B5DC-BF87284438CFQ34086058-D5688572-E4A2-419C-BC9A-970DD8F3BA1DQ34108064-853F3988-9771-4375-B118-96FA64C91AB1Q34152334-BDCEDC75-C994-40FC-8938-35C22280EA00Q34188958-BF5C1645-6987-4B58-80AD-FB75C08752D2Q34321578-8766359D-6A5B-4E8B-B612-57E02446243EQ34328352-922D03BE-DAE4-4A88-AAEB-FB6BADC634C4Q34337626-CF45435B-4C6E-467C-82BA-3688606A3419Q34435551-47D1B3F6-FB95-40F3-B90C-F81343D3CEC9Q34467024-78EA53F8-8FA6-4AC0-9DD3-9A97F2F4EE7AQ34637173-657B165C-638D-43CC-9B2D-966B5982801AQ34638636-4887AB97-0F3A-4189-BABC-99D31AD34B81
P2860
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@ast
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@en
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@en-gb
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@nl
type
label
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@ast
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@en
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@en-gb
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@nl
prefLabel
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@ast
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@en
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@en-gb
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2
@nl
P2093
P3181
P356
P1476
In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2.
@en
P2093
P3181
P356
10.1006/BBRC.1998.9995
P407
P577
1999-01-27T00:00:00Z