Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
about
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1The ubiquilin gene family: evolutionary patterns and functional insightsMPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 functionThe rice HGW gene encodes a ubiquitin-associated (UBA) domain protein that regulates heading date and grain weightCross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysisHuman Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathwayInteraction with a ubiquitin-like protein enhances the ubiquitination and degradation of hepatitis C virus RNA-dependent RNA polymeraseRad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chainsFAT10, a ubiquitin-independent signal for proteasomal degradationA novel ubiquitin-binding protein ZNF216 functioning in muscle atrophyThe ubiquitin-like protein PLIC-2 is a negative regulator of G protein-coupled receptor endocytosis.Structure of the ubiquitin-associated domain of p62 (SQSTM1) and implications for mutations that cause Paget's disease of boneThe UBA domains of NUB1L are required for binding but not for accelerated degradation of the ubiquitin-like modifier FAT10Role of the UBL-UBA protein KPC2 in degradation of p27 at G1 phase of the cell cycle.Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymesInvolvement of the DNA repair protein hHR23 in p53 degradationSolution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUGOrigin and function of ubiquitin-like proteinsUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationThe ubiquitin-associated domain of hPLIC-2 interacts with the proteasomeStructural determinants for the binding of ubiquitin-like domains to the proteasomeThe life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathUbiquitination-induced fluorescence complementation (UiFC) for detection of K48 ubiquitin chains in vitro and in live cellsStructure of the ubiquitin-interacting motif of S5a bound to the ubiquitin-like domain of HR23BStructure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12Molecular architecture and assembly of the eukaryotic proteasomeProteasome subunit Rpn1 binds ubiquitin-like protein domains.Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome.A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradationCentrin/Cdc31 is a novel regulator of protein degradation.A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domainTOR-dependent reduction in the expression level of Rrn3p lowers the activity of the yeast RNA Pol I machinery, but does not account for the strong inhibition of rRNA productionMultiple assembly chaperones govern biogenesis of the proteasome regulatory particle base.Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryomicroscopyRpn1 and Rpn2 coordinate ubiquitin processing factors at proteasomeUbiquitin-binding domainsUbiquitin and ubiquitin-like proteins as multifunctional signalsProteasome assembly influences interaction with ubiquitinated proteins and shuttle factors.A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43.
P2860
Q21245310-DFB2E028-FE55-4E6B-92BD-BBAC292E514FQ21283993-75B20182-4324-492A-A0AB-253B3D9A02FBQ21284393-98EB5E1D-C57E-443E-8AA8-E10756BCD9A0Q21561023-75A180DF-CFAF-4764-AE8E-EA68BBAAF7D4Q24294410-707ECFC8-8823-4905-B32A-8C9C8264F2D4Q24297296-D7ABE2BC-0CBA-40FE-9BFE-0A89395064BEQ24297704-18C35EEF-1FDF-4218-A5DC-C2EDA8CEE634Q24298011-50151168-9958-4EF7-A4F4-B81B0540A0B3Q24300071-EDD846B9-5692-4899-93B8-9C14F8BCA85DQ24301547-E4296FA3-526C-4EF1-87DC-FFE06726715BQ24306610-B6687E02-D804-4D43-BCA8-25E34C4183E6Q24307892-C6D77F22-FBB2-48B6-9DAF-B982499A117EQ24337252-AFB8B3E2-5D5A-4F91-920D-EB1603C724AEQ24534914-87E417B2-19C4-486C-96A7-E0C91D45A71FQ24536045-B7BF4783-56DE-4DD0-A7FE-A0C4DECAF74CQ24633456-84AEC7D0-1335-47E4-88F7-91A7EC5173E1Q24644912-0E11448B-372B-4414-8334-1407E41CC11BQ24651141-DCCE2178-3FB7-452D-9932-4AA2264EB1F3Q24653719-A5256989-23EC-4C3C-BD15-0918B207DDB6Q24669533-CB7C2BBE-FB6B-4691-AF81-1BE30C178D76Q24685639-054A4812-82ED-416D-A89D-678C0DAD9B55Q26738549-AA59D610-275F-49BE-8A96-69257DB49947Q27307830-B34EFF3C-7AA7-4998-AF04-96E86EC809F8Q27642449-FC75EB41-8735-421B-B336-D0163AA0C48AQ27664179-A541707E-84A1-4989-8B69-0921A44EF3C8Q27693890-BC9CA47A-C166-4FEF-8A8B-8D7BF1EF99CCQ27930136-E7F6D108-AAFE-41A8-BF94-4E516E944286Q27932293-41457A50-C4F5-44E4-BB5F-982CFCC15BB2Q27933278-A4D9DACB-811A-4186-97A5-2CA6B1322A8EQ27934931-DE17B652-4925-4BC3-B709-CB7F32608252Q27935207-04AEC196-9F1E-49C3-9E13-ECB446DC4EB3Q27935209-8CE65313-BA3F-42F1-AA3A-BA52A41E104FQ27937453-0EDCD050-C7AC-4ED7-9B7E-0D88AAB5FA41Q27939675-114F4B66-BB24-4645-86D7-C27518D4C893Q28256624-A5128646-6F4F-4BC4-9FA5-D41C1A1A38B7Q28259286-50FEBB24-38F4-4B69-A132-8669A2B46B0DQ29616461-353C05F7-709F-4BC5-9A17-5CE006D5ECD7Q30014838-2E573C4E-2B8F-449F-9B00-6085E533A834Q30493508-0117D0C1-071D-40D0-AF70-F5754DDC4452Q33310245-D3D0EB81-B266-4CBC-AE93-74E023CAE159
P2860
Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունվարին 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
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@ast
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@en
Budding yeast Dsk2p is a polyu ...... interact with the proteasome.
@nl
type
label
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@ast
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@en
Budding yeast Dsk2p is a polyu ...... interact with the proteasome.
@nl
prefLabel
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@ast
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@en
Budding yeast Dsk2p is a polyu ...... interact with the proteasome.
@nl
P2093
P2860
P3181
P356
P1476
Budding yeast Dsk2p is a polyu ...... n interact with the proteasome
@en
P2093
Hideki Kobayashi
Minoru Funakoshi
Takeharu Nishimoto
Toru Sasaki
P2860
P304
P3181
P356
10.1073/PNAS.012585199
P407
P577
2002-01-22T00:00:00Z