The Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding Domain
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Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic InterfaceStructure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteinsCrystal structure of the ubiquitin-like domain of human TBK1Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro.Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding.Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.The ubiquitin-proteasome system of Saccharomyces cerevisiae.A New Method, "Reverse Yeast Two-Hybrid Array" (RYTHA), Identifies Mutants that Dissociate the Physical Interaction Between Elg1 and Slx5.Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation.Ufd2p synthesizes branched ubiquitin chains to promote the degradation of substrates modified with atypical chains.Three old and one new: protein import into red algal-derived plastids surrounded by four membranes.Emerging mechanistic insights into AAA complexes regulating proteasomal degradation.(1)H, (15)N, (13)C resonance assignments for Saccharomyces cerevisiae Rad23 UBL domain.Ubiquilin1 promotes antigen-receptor mediated proliferation by eliminating mislocalized mitochondrial proteins.Yeast Irc22 Is a Novel Dsk2-Interacting Protein that Is Involved in Salt ToleranceStructures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.Sumoylation, Phosphorylation, and Acetylation Fine-Tune the Turnover of Plant Immunity Components Mediated by Ubiquitination.UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.
P2860
Q27675050-7DD402B3-0FF1-4F18-AFD3-99960FAC62A8Q27675806-18135565-31D9-4A55-8095-9B25B358D180Q27679207-21A85380-1643-4EC9-8829-FEBFFE0D284DQ34344682-D038BFE1-2584-4710-8F7D-1487B10F996CQ35102083-5171A5C4-7489-41E8-B2AC-374EE99DD9F9Q35469778-FF073632-7A72-44F6-BD54-94CDAC750BBCQ36268060-8AB39614-CAB3-4162-A500-F8F8F5372B88Q36364639-6C735771-727A-46FC-83EC-E7BFF4E29DE4Q36506506-B4648318-14CB-4ACC-B613-67ABFD1952F7Q37637735-CEEBEDB1-C028-4859-B448-5B7F1AE821D4Q38101256-6D240CC6-5A7D-48C2-A033-B94A6AF3DA66Q38237803-0B6091CC-89B4-4EF1-9E52-C8680E09D6D4Q39759648-746F3B58-F6FA-441C-9D23-F77FE7125FB5Q41691918-68DB7EA7-9826-487A-8BB1-56C99A10207FQ42288684-4A6E31F0-7BB5-4230-A866-67644F47E294Q42382149-9A96B7AD-2CA4-4ACB-AEF4-918A66AAF38EQ42700483-961D9FC8-42A9-411B-BC25-29A2904AED92Q48113345-42E353A0-BAF7-4E83-909A-958E687812FB
P2860
The Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding Domain
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@ast
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@en
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@nl
type
label
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@ast
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@en
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@nl
prefLabel
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@ast
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@en
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@nl
P2860
P50
P356
P1476
The Yeast E4 Ubiquitin Ligase ...... Ubiquitin-like Binding Domain
@en
P2093
Kay Hofmann
Shahri Raasi
P2860
P304
P356
10.1074/JBC.M110.112532
P407
P577
2010-06-25T00:00:00Z