Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae.
about
A novel ubiquitin-binding protein ZNF216 functioning in muscle atrophyUbiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitinationAPOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replicationUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationA novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C proteinAtaxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysisSts1 plays a key role in targeting proteasomes to the nucleus.Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysisYeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.Rad4 regulates protein turnover at a postubiquitylation step.Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domainBudding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasomeCentrin/Cdc31 is a novel regulator of protein degradation.Physical association of ubiquitin ligases and the 26S proteasome.Proteasome assembly influences interaction with ubiquitinated proteins and shuttle factors.Erythropoietic defect associated with reduced cell proliferation in mice lacking the 26S proteasome shuttling factor Rad23b.A genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2Genetic analyses of the Arabidopsis 26S proteasome regulatory particle reveal its importance during light stress and a specific role for the N-terminus of RPT2 in developmentProteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A.Rad23 stabilizes Rad4 from degradation by the Ub/proteasome pathwayRad23 escapes degradation because it lacks a proteasome initiation regionArabidopsis HEMERA/pTAC12 initiates photomorphogenesis by phytochromes.Rad23 promotes the targeting of proteolytic substrates to the proteasome.Saccharomyces cerevisiae Ub-conjugating enzyme Ubc4 binds the proteasome in the presence of translationally damaged proteinsNew insight into the role of the Cdc34 ubiquitin-conjugating enzyme in cell cycle regulation via Ace2 and Sic1.The cellular level of PR500, a protein complex related to the 19S regulatory particle of the proteasome, is regulated in response to stresses in plants.The Cdc48 ATPase modulates the interaction between two proteolytic factors Ufd2 and Rad23.A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome.Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasomeA large-scale RNAi screen identifies functional classes of genes shaping synaptic development and maintenanceThe Png1-Rad23 complex regulates glycoprotein turnover.Rpn10-mediated degradation of ubiquitinated proteins is essential for mouse developmentLoss of RAD-23 Protects Against Models of Motor Neuron Disease by Enhancing Mutant Protein ClearanceProtein targeting to ATP-dependent proteases.Synthetic lethality of rpn11-1 rpn10Δ is linked to altered proteasome assembly and activityExtraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome.The ubiquitin-proteasome system in cancer, a major player in DNA repair. Part 1: post-translational regulation.Cdc48: a swiss army knife of cell biology.Rad7 E3 Ubiquitin Ligase Attenuates Polyubiquitylation of Rpn10 and Dsk2 Following DNA Damage in Saccharomyces cerevisiae.
P2860
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P2860
Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@ast
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@en
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@nl
type
label
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@ast
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@en
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@nl
prefLabel
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@ast
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@en
Pleiotropic defects caused by ...... 0 of Saccharomyces cerevisiae.
@nl
P2093
P2860
P1433
P1476
Pleiotropic defects caused by ...... 10 of Saccharomyces cerevisiae
@en
P2093
P2860
P407
P577
1999-09-01T00:00:00Z