Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.
about
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle.Protein quality control in the nucleusStructure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysisRad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.Complementary roles for Rpn11 and Ubp6 in deubiquitination and proteolysis by the proteasome.Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopyMolecular architecture of the 26S proteasome holocomplex determined by an integrative approachRpn1 and Rpn2 coordinate ubiquitin processing factors at proteasomeRegulation of proteasome activity in health and diseaseRecognition and processing of ubiquitin-protein conjugates by the proteasomeUbiquitin and ubiquitin-like proteins as multifunctional signalsUbiquitin domain proteins in disease.Toward an integrated structural model of the 26S proteasomeThe F-box protein FBXO7 positively regulates bone morphogenetic protein-mediated signaling through Lys-63-specific ubiquitination of neurotrophin receptor-interacting MAGE (NRAGE).Getting into position: the catalytic mechanisms of protein ubiquitylation.The regulation of proteasome degradation by multi-ubiquitin chain binding proteins.Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse developmentProteasome-associated proteins: regulation of a proteolytic machine.Mapping the structural topology of the yeast 19S proteasomal regulatory particle using chemical cross-linking and probabilistic modeling.Proteomics of proteasome complexes and ubiquitinated proteins.Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Rad7 E3 Ubiquitin Ligase Attenuates Polyubiquitylation of Rpn10 and Dsk2 Following DNA Damage in Saccharomyces cerevisiae.The central unit within the 19S regulatory particle of the proteasomeUBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.The ubiquitin-associated (UBA) 1 domain of Schizosaccharomyces pombe Rhp23 is essential for the recognition of ubiquitin-proteasome system substrates both in vitro and in vivoTogether, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor.Dss1 is a 26S proteasome ubiquitin receptor.Cysteine-protease involved in male chromatin remodeling after fertilization co-localizes with alpha-tubulin at mitosis.
P2860
Q21245310-27459A86-98D3-43A9-ADFA-3AF90ADAF38BQ24534914-75D8992E-24E8-4FDE-97F3-DC0B77FC87B9Q27023202-27D0312D-49EA-43D5-A655-E56E88BAC527Q27664179-46CD705E-35F1-47B9-87A2-B9453DE86740Q27931879-8FE10385-413C-4314-A5AC-0744D6DAED60Q27933278-B7B25C2E-8401-4116-BA99-8411D7987510Q27939996-0DFB0DD6-CC5D-451F-9FBC-69B3E5B03AB9Q28256624-682C63B8-BF86-4049-8E30-69FFCB0DB340Q28259014-CC8F6EBB-A586-42C2-9043-2FEC4A91CBECQ28259286-092AC297-5BB2-4584-AE29-1D43B5F6D236Q28392708-E8D72974-6EA7-4CFA-9662-D24C1A449C44Q29547616-BBF9DFD9-EAC3-447E-8363-3A1ABD00DC91Q30014838-3068A0DF-D471-40E3-929A-2B7BDE6E5A63Q33307870-8E187EEC-10D3-4B03-9082-F2A17542EDC8Q34121912-12911E35-8A6A-4BF7-BAB6-66A77CAC9FBEQ35191687-B3BFB16D-666A-474C-93AB-9664EF79850AQ35681247-9268C758-4E6B-4171-9766-BDFFCAF7A12CQ36155975-CD5011A9-CC68-4071-AE4A-16A50F6B3FE9Q36176652-586CF5D6-C287-4563-9CFE-5167B628BA5AQ36275413-636E9970-9559-4A86-B9CF-BCBDFC7993AAQ36455723-C4D973EB-BD8D-4E72-8569-B3F8B964D2BDQ36973779-1615F913-9197-4CA7-BD6E-F996F0FB3643Q37098025-A0300661-28A4-43C5-9E09-94BEB85D0DEEQ37267119-C67E87F4-D3B5-43EA-A981-2581F4E98394Q39840445-07955C36-5840-4C77-AC18-F3D1C96E829AQ40817421-CF443966-707B-479E-A50C-CC245586B7F1Q41176558-90D9BA6E-2898-46C4-A013-20F0887ACAFBQ41890812-7CFB9E3F-28B4-4585-8FA6-32372A9CFDFEQ42936102-D562AF47-0AE0-48CC-B034-26D3F66AF057Q43006495-E364CA8C-3B06-4FA8-ADF8-434DB1FC12A8Q45076241-5BC792B8-F98A-4259-B8B5-ED8C866CF772
P2860
Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@en
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@nl
type
label
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@en
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@nl
prefLabel
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@en
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@nl
P2093
P2860
P356
P1476
Interaction of the anaphase-pr ...... quitin chain-binding proteins.
@en
P2093
Caroline R M Wilkinson
Colin Gordon
Itaru Samejima
Mairi Wallace
Michael Seeger
P2860
P304
16791-16796
P356
10.1074/JBC.M208281200
P407
P577
2003-03-03T00:00:00Z