In vitro assembly and recognition of Lys-63 polyubiquitin chains.
about
Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysisRad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chainsSequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradationRNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localizationThe HECT domain of TRIP12 ubiquitinates substrates of the ubiquitin fusion degradation pathwayWhy do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes?Distinct consequences of posttranslational modification by linear versus K63-linked polyubiquitin chainsEmerging role of Lys-63 ubiquitination in protein kinase and phosphatase activation and cancer developmentChfr acts with the p38 stress kinases to block entry to mitosis in mammalian cellsUbc13: the Lys63 ubiquitin chain building machineFunctions of the 19S complex in proteasomal degradationInteractions between the quality control ubiquitin ligase CHIP and ubiquitin conjugating enzymesStructure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13Structure of Proteasome Ubiquitin Receptor hRpn13 and Its Activation by the Scaffolding Protein hRpn2Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligasePromiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin ChainsMultiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysisSynthesis of free and proliferating cell nuclear antigen-bound polyubiquitin chains by the RING E3 ubiquitin ligase Rad5.The NEF4 complex regulates Rad4 levels and utilizes Snf2/Swi2-related ATPase activity for nucleotide excision repair.Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome.Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteinsTargeting proteins for degradationWwp2 mediates Oct4 ubiquitination and its own auto-ubiquitination in a dosage-dependent mannerRecognition and processing of ubiquitin-protein conjugates by the proteasomeExploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release.Factors affecting the use of 13C(alpha) chemical shifts to determine, refine, and validate protein structuresCharacterizing ubiquitination sites by peptide-based immunoaffinity enrichment.Ubiquitination is involved in secondary growth, not initial formation of polyglutamine protein aggregates in C. elegans.Lysine 63-polyubiquitination guards against translesion synthesis-induced mutations.Ubiquitin domain proteins in disease.Overexpression of EVE1, a novel ubiquitin family protein, arrests inflorescence stem development in Arabidopsis.Ubiquitin, hormones and biotic stress in plantsNonenzymatic polymerization of ubiquitin: single-step synthesis and isolation of discrete ubiquitin oligomersDegradation or maintenance: actions of the ubiquitin system on eukaryotic chromatinThe essential functions of NEDD8 are mediated via distinct surface regions, and not by polyneddylation in Schizosaccharomyces pombe.Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics.Innate antiviral response targets HIV-1 release by the induction of ubiquitin-like protein ISG15.The ubiquitin-proteasome system and assays to determine responses to inhibitors.Hax-1 is rapidly degraded by the proteasome dependent on its PEST sequence.Lys6-modified ubiquitin inhibits ubiquitin-dependent protein degradation.
P2860
Q24294410-79D2A02B-6D44-4E03-8884-8B27236C5268Q24298011-71991806-F974-46BC-8484-AC4D2EB97418Q24305254-3DD2493D-95FD-43FA-B53F-02CDE5A62154Q24308703-F4405AD6-8DBD-43C6-A51B-1B1F086F7323Q24317229-6A52E95A-0742-4317-A40E-042FED7320EAQ24617857-40930BB2-9298-4126-80EC-625AC340AA2EQ24621713-1ED64B1D-B154-4548-B3C7-2352FADB558DQ24622802-1989DEB8-0AD8-480B-A476-77200A8EB912Q24676923-FAA05879-8262-4C85-AE67-A6AAF64EF04AQ26739716-1DA6E102-EFA3-43A9-BCBD-970108870BAAQ26996345-F174D2BB-DCCC-4C28-86CB-810A8974663BQ27650632-D330CC5C-B480-460C-BFB1-4D88AB48F522Q27657027-6EC2028F-47D1-44DE-8046-372F4D2D8ED9Q27661655-46140C36-E242-4926-9EB4-2F236CB09AB5Q27673792-637B9645-7708-4E5A-85B5-4492E8760E2DQ27674961-416BFEA0-0E11-4DE9-9B25-646098DAB2ACQ27931879-57C9BA7E-EB72-49DD-801D-F0ABA9336282Q27935517-7336F61A-E00E-4FFB-96E9-87EE962FA76AQ27936146-6F20C642-3412-40BB-833F-4EF625F0BB93Q27937521-FD4BEF40-FAED-4D6E-88B9-82DA34A04D08Q28087183-E07C8BA1-0EEB-46BF-BE73-BEAB813DC55EQ28261886-F78A4F6E-F36B-45DA-AE66-C67E575BA85AQ28585636-E5ADA7BB-CACE-4A2A-8C52-9D4BA6706EB5Q29547616-C6700AFF-4D4C-46A1-888B-8B4631ABF26AQ30157284-4B55713F-5566-406B-A671-E0D5A443CCB8Q30365527-83C0E4AC-5D83-46C8-9FB8-3ADDBA75C005Q30418482-B6E3539F-0183-4984-A7CB-D9C25BF7FC4AQ30515046-83223554-096A-4408-95D1-C621EA94A078Q33247452-736BBF92-304B-41EF-A614-19E4DF705076Q33307870-AD2EB99E-768D-497C-BAD9-9C9B2F9235FBQ33351326-A604659E-5071-41EE-B514-67B72993C624Q33576532-943A7DC9-3B85-49FC-BD11-B06CA62C51F4Q33852992-74961BC2-7574-4828-B16B-4749BB9BD4EBQ33905811-38572CD3-EDF9-42F2-BD10-E1C887BF8990Q33927244-63C3FB89-BAAB-43FD-9E06-0CA47B647382Q34015771-28F8A1A8-46E1-4042-B64B-58242E30B726Q34335062-9561A131-93C0-46BF-8E70-E35DA2D66E2BQ34347848-0E0BC496-2E0F-4C01-8797-1C727350E066Q34349645-D8F32225-E8E7-4A6B-9C59-F46449D42EDCQ34407193-6E01ED30-ED80-434E-A71F-9B4D7D7D8F07
P2860
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@en
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@nl
type
label
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@en
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@nl
prefLabel
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@en
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@nl
P356
P1476
In vitro assembly and recognition of Lys-63 polyubiquitin chains.
@en
P2093
C M Pickart
R M Hofmann
P304
27936-27943
P356
10.1074/JBC.M103378200
P407
P577
2001-05-21T00:00:00Z