Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
about
A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons.The N-end rule pathwayThe life cycle of the 26S proteasome: from birth, through regulation and function, and onto its deathInhibition of proteasomal degradation of rpn4 impairs nonhomologous end-joining repair of DNA double-strand breaks.Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.Genome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1Tmc1 Is a Dynamically Regulated Effector of the Rpn4 Proteotoxic Stress Response.Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cellsIdentification of the preferential ubiquitination site and ubiquitin-dependent degradation signal of Rpn4Regulation of proteasome activity in health and diseaseBiochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systemsGenomewide screen reveals a wide regulatory network for di/tripeptide utilization in Saccharomyces cerevisiae.GONOME: measuring correlations between GO terms and genomic positions.Proteasomal degradation of Rpn4 in Saccharomyces cerevisiae is critical for cell viability under stressed conditions.Non-repair pathways for minimizing protein isoaspartyl damage in the yeast Saccharomyces cerevisiae.Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiaeThe N-end rule pathway and regulation by proteolysisThe ribonucleotide reductase inhibitor, Sml1, is sequentially phosphorylated, ubiquitylated and degraded in response to DNA damageThe Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein.A proteasome for all occasions.A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.The ubiquitin-proteasome system of Saccharomyces cerevisiae.Two proteolytic pathways regulate DNA repair by cotargeting the Mgt1 alkylguanine transferaseNuclear import factor Srp1 and its associated protein Sts1 couple ribosome-bound nascent polypeptides to proteasomes for cotranslational degradation.The Mechanistic Links Between Proteasome Activity, Aging and Age-related Diseases.The ends and means of artificially induced targeted protein degradation.UPS Activation in the Battle Against Aging and Aggregation-Related Diseases: An Extended Review.Opposing roles of Ubp3-dependent deubiquitination regulate replicative life span and heat resistance.Q2N and S65D substitutions of ubiquitin unravel functional significance of the invariant residues Gln2 and Ser65.The sole introduction of two single-point mutations establishes glycerol utilization in Saccharomyces cerevisiae CEN.PK derivatives.A role for the proteasome in the turnover of Sup35p and in [PSI(+) ] prion propagation.Cold Temperature Induces the Reprogramming of Proteolytic Pathways in Yeast.N-Glycosylation deficiency enhanced heterologous production of a Bacillus licheniformis thermostable α-amylase in Saccharomyces cerevisiae.Essential role of Ubr11, but not Ubr1, as an N-end rule ubiquitin ligase in Schizosaccharomyces pombe.Yeast phospholipase C is required for stability of casein kinase I Yck2p and expression of hexose transporters.The armadillo repeats of the Ufd4 ubiquitin ligase recognize ubiquitin-fusion proteins.
P2860
220ebe2cb333fbd6fed44f0e465e590db2d6d2657cfb5f91b3f6fa0f74f358a772a0b1ef017c061580e249273d393a969b6eedc12cddc7764037f5188da09648cf64e7ef4bb89086fcf0fc3bd3af1341e11c561f7367b7a1d764460559f2653415243624f92af699be12c782d6a55bcbdc5516c191399486f9f67b5697f1d031a91d958175ec984c0b12526cfdcde5aa2be31bb8afc9daa46c2733a9db1d8977
P248
Q24529893-6C109BD5-9558-481B-A15A-ADB46A82A72FQ24598290-81B033E0-D6AB-4734-8C09-D57B22263AFBQ26738549-398C4CA7-F91E-44FE-BF10-EEABB3E4C167Q27929905-4C203EC6-4E04-4155-8629-9B466342F0BEQ27930363-64323F74-CF16-42CE-8D17-BFE6F0F83536Q27930957-295A67F0-D36A-494C-B3C8-994AF3D8984EQ27932129-4DEBD93B-8ABC-4EC2-B927-6A8FEB4C292EQ27939530-EC4EB8D7-6577-4571-BEA5-733797883277Q28279454-63B320D7-F3C5-4B31-98FC-B300E8786111Q28298559-D3F02F08-AFF6-45B4-B0FC-5002C7536FF1Q28392708-89AC569B-1E93-4BEC-84F1-4AD4A180BB52Q28594626-802983F8-7C97-4C2E-B356-FC0237077352Q33229782-3BB42684-D2F9-4AF2-A589-6CA5ABD25D13Q33234910-C88643EA-49DD-46A6-9042-DB061694B70AQ33688804-00C2EF73-9D36-4EC1-AA0A-C320A030E4DEQ33761245-9CE3A267-B27F-42D8-A6F0-BEA9B81065C0Q34023025-913B35E2-2EB4-4508-977B-C6EA95E6D6B4Q34189152-CED4A8D4-CEAE-4713-8682-91ECAFCF4E64Q34246788-86CD740B-2BC2-4950-BFE1-59A3E7FC57A0Q34585694-DD98AE65-F528-44F9-9CD3-7AEE7853DFEAQ35973516-BA71FE26-6C55-40B1-8AA8-DC9659A06011Q36078874-74C56EDF-0AF5-4869-94D3-90E8DF10C473Q36268060-34D4172C-BD20-423D-B2EB-B8B974DBD036Q37114760-AA95ACC2-E15F-47D5-8F4D-971598DCFDC8Q37536502-6BFC5111-0056-4153-B214-8DB27EB56DEFQ37645630-254DBA4F-E102-4083-80A5-6A2792ABC9A8Q38052466-E2272596-21B0-4BBB-8C7A-CE4290954790Q38950512-D5BD06D3-94D5-4127-A217-B8815BC73510Q38972887-8E430D26-852A-4F7B-8438-BAA7D6B42B37Q39493680-E6FBDF30-D404-4427-B9B9-8274D168D903Q42159764-3397741F-D74C-41BA-B781-357A54A4CB65Q42225997-5E7971E4-AA01-42D8-8B25-6EA12E7F50EFQ42781900-C653B82F-8376-4FD0-AFBA-C3BF80610B25Q44082404-0F107062-BBAC-45E0-A237-2122E3A06A99Q44208449-472F062D-FF16-4690-B42D-5C21A21CBC7BQ47583377-30EA1C5A-B502-41A8-BD69-A76D84C0F6DEQ52576026-AFD0A1B0-4731-4B06-9071-B6B01D47905A
P2860
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@ast
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@en
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@nl
type
label
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@ast
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@en
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@nl
prefLabel
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@ast
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@en
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@nl
P2093
P2860
P3181
P356
P1476
Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase.
@en
P2093
Donghong Ju
Xicheng Mao
Youming Xie
P2860
P304
P3181
P356
10.1074/JBC.M410085200
P407
P577
2004-12-31T00:00:00Z