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Proteasomal interference prevents zona pellucida penetration and fertilization in mammalsFbx7 functions in the SCF complex regulating Cdk1-cyclin B-phosphorylated hepatoma up-regulated protein (HURP) proteolysis by a proline-rich regionHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumRNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signallingStructural basis of selective ubiquitination of TRF1 by SCFFbx4Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligasesMultiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised.Diversity of degradation signals in the ubiquitin-proteasome systemOne step at a time: endoplasmic reticulum-associated degradationTargeted disruption of p185/Cul7 gene results in abnormal vascular morphogenesisReplication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin-proteasome pathwayBuilding and remodelling Cullin-RING E3 ubiquitin ligasesGenetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligasesStructural basis for the selection of glycosylated substrates by SCFFbs1 ubiquitin ligaseGenome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.Function and regulation of cullin-RING ubiquitin ligasesThe F-box protein TIR1 is an auxin receptorGlcNAcylation of histone H2B facilitates its monoubiquitinationERAD: the long road to destructionUbiquitination and degradation of the inhibitors of NF-kappaBThe SCF ubiquitin ligase: insights into a molecular machineFbx15 is a novel target of Oct3/4 but is dispensable for embryonic stem cell self-renewal and mouse developmentGlycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substratesActivity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitinationFbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chainsDopamine 5 receptor mediates Ang II type 1 receptor degradation via a ubiquitin-proteasome pathway in mice and human cells.Sugar-binding properties of VIP36, an intracellular animal lectin operating as a cargo receptor.N-linked glycosylation does not impair proteasomal degradation but affects class I major histocompatibility complex presentation.A CULLINary ride across the secretory pathway: more than just secretion.Applications of proteomic technologies for understanding the premature proteolysis of CFTR.A role for N-glycanase in the cytosolic turnover of glycoproteins.The Arabidopsis SLEEPY1 gene encodes a putative F-box subunit of an SCF E3 ubiquitin ligase.Cellular refractoriness to the heat-stable enterotoxin peptide is associated with alterations in levels of the differentially glycosylated forms of guanylyl cyclase C.The cytoplasmic peptide:N-glycanase (Ngly1)-basic science encounters a human genetic disorder.Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding moduleFBXO15 regulates P-glycoprotein/ABCB1 expression through the ubiquitin--proteasome pathway in cancer cells.Cullin E3 ligases and their rewiring by viral factorsRoles of F-box proteins in cancerThe ubiquitin E3 ligase SCF-FBXO24 recognizes deacetylated nucleoside diphosphate kinase A to enhance its degradation.
P2860
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P248
Q23919487-17F08621-7691-42BC-B181-29491A742026Q24293185-A2A94C31-8CE8-489F-98AC-3BC53BAFFDFBQ24298901-B457A830-8DB3-459E-A1B4-98796FC5D384Q24299327-8A0EA066-D57D-4492-9461-41C93F361C90Q24299395-A2940FDA-9AA4-4929-8885-B8D9314AAB8AQ24306888-94E8A019-64DE-4A43-B6A5-70C28D079A4FQ24530318-17133B2E-D14C-478A-ACAD-222332EEBC0CQ24535941-CA351193-2C82-4FBA-B4AF-69BD1B27DF04Q24642979-4484C369-32FB-499D-B30A-13900738ADEBQ24658302-E26FBBFD-86E5-4ECB-93EE-269BC190429CQ24680360-8BBAE12C-B93F-4834-9817-151464477C00Q24680651-0CF19ECF-6ADD-44FC-8678-DD5E3926B9B0Q27027816-56E8EDD4-385A-4E1F-B979-26F3BF8D9665Q27027897-B92F8912-9572-43FF-871F-71D862874F40Q27644251-A788578D-D64A-4F95-8187-7029E8E2E558Q27930957-3C92E5B1-BB49-4D0C-B6F3-6048002942CDQ28131707-696AB3DF-A8F2-49B1-AA59-0A3F4A28DE03Q28253006-3855F7AB-D6C2-4CC9-B6FB-86FF71383D5CQ28254074-928A33E4-8277-4B22-B65B-4C3ECBB44A93Q28264823-219F95DD-AD62-44E8-9DED-0D4622607040Q28274205-E1EA8940-5933-4ABE-ACDB-699C381DDE6CQ28279993-FDF2493C-2215-459F-9970-302014FA80FDQ28506535-6F760A5B-50DB-4136-9C1D-2527D3ADB2D4Q28508835-0549F0F9-0214-40F5-B85B-A4E4F0853C27Q28510206-A0F5A939-DFAB-4707-8F6F-FAE42EED5D52Q28590989-07311D33-A3F5-4EA4-8872-65C799BF572DQ30441613-67C97A11-47D0-413B-9085-5EB8C82D1C66Q33222548-E3CF9B79-102E-4546-943A-D9350FAFE9A0Q33303325-DFC6CE2B-4698-45FF-91DF-3D43676B0F78Q33819289-B6EAF463-8EDF-4059-8F9F-33629444D4E0Q34076025-A4431C8C-445A-499A-B1B0-DBEF96E62021Q34179944-B1FD5FD7-6A64-4586-BD59-4A6F115983B6Q34194020-C1D87782-7FBB-486F-8119-FDC6F8C44771Q34226965-98FF3A71-D497-4C64-8272-71AEF0436DE3Q34448040-BD76FF81-66A0-4328-9774-57376871657DQ34579798-E52F3EB2-C5C1-411D-A97A-E18454EB4EECQ34610210-02EA54BD-9AD5-40F4-AB30-C43D88EBF5B8Q34785767-CC3207F9-BF33-44F3-9E9E-CFAAF149C3A3Q35012352-F76EF2FB-2C48-44D4-95E8-E42EF1E80076Q35097070-FC6144DC-5847-41C8-BF85-3D253FC7A11B
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
E3 ubiquitin ligase that recognizes sugar chains
@ast
E3 ubiquitin ligase that recognizes sugar chains
@en
E3 ubiquitin ligase that recognizes sugar chains
@nl
type
label
E3 ubiquitin ligase that recognizes sugar chains
@ast
E3 ubiquitin ligase that recognizes sugar chains
@en
E3 ubiquitin ligase that recognizes sugar chains
@nl
prefLabel
E3 ubiquitin ligase that recognizes sugar chains
@ast
E3 ubiquitin ligase that recognizes sugar chains
@en
E3 ubiquitin ligase that recognizes sugar chains
@nl
P2093
P2860
P50
P921
P356
P1433
P1476
E3 ubiquitin ligase that recognizes sugar chains
@en
P2093
Fuminori Tokunaga
Kazuhiro Iwai
Keiji Tanaka
Tadashi Tai
Tomoki Chiba
Toshiaki Suzuki
Yukiko Yoshida
P2860
P2888
P304
P356
10.1038/NATURE00890
P407
P577
2002-07-25T00:00:00Z
P6179
1033057716