A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress. - Wikidata - wikimedia - TriplyDB

A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress.

A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress.

http://www.wikidata.org/entity/Q37148352

about

Near-atomic resolution structural model of the yeast 26S proteasome.Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast Metabolome and proteome changes with aging in Caenorhabditis elegans.Base-CP proteasome can serve as a platform for stepwise lid formation Rice stripe tenuivirus nonstructural protein 3 hijacks the 26S proteasome of the small brown planthopper via direct interaction with regulatory particle non-ATPase subunit 3.Proteasomes associated with the Blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein Dnm1.Moonlighting and pleiotropy within two regulators of the degradation machinery: the proteasome lid and the CSN.Irisflorentin improves α-synuclein accumulation and attenuates 6-OHDA-induced dopaminergic neuron degeneration, implication for Parkinson's disease therapy.

P2860

Q30524942-6BA6A8A2-DFC9-4663-B883-F860F3C8C86E Q30584192-D88FA77F-304D-4000-AA6F-A29565D65C65 Q33807271-E4E04EBD-1A64-4EED-A626-4333317F40D3 Q35626302-085AE9D9-9198-459A-A192-28EE571F397A Q35640930-82B2B37F-32E9-4447-9A55-669B2F30C24A Q37727657-D3F4DAB5-0789-4175-A09E-C18CC88EA8A5 Q38268491-7D39CC7C-E593-40D7-BEBF-E191CC4FAC21 Q41369321-A077A534-718A-47D3-A1FA-806F2EA36A0F

P2860

A proteasome assembly defect in rpn3 mutants is associated with Rpn11 instability and increased sensitivity to stress.

http://www.wikidata.org/entity/Q37148352

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 18 May 2011

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

A proteasome assembly defect i ...... creased sensitivity to stress.

@en

A proteasome assembly defect i ...... creased sensitivity to stress.

@nl

type

label

A proteasome assembly defect i ...... creased sensitivity to stress.

@en

A proteasome assembly defect i ...... creased sensitivity to stress.

@nl

prefLabel

A proteasome assembly defect i ...... creased sensitivity to stress.

@en

A proteasome assembly defect i ...... creased sensitivity to stress.

@nl

P1433

Q37148352-0AAE538D-0A38-4120-986B-49346C9AECB3

P1476

Q37148352-16CE89E7-351A-4181-8480-84051B170F5E

P2093

Q37148352-05A33722-48E3-41EC-A5FF-9EC9F490F022

Q37148352-885888AA-97B6-4BB0-9356-3E0EDCEFB44F

Q37148352-90514776-F82F-4FAC-9324-A47DE5E024E2

Q37148352-CCD2FF6C-8F0C-4506-9440-64F5B228CC6E

Q37148352-F5319089-30D6-4DF7-A6D0-993C47B8D252

P2860

Q37148352-00C9C529-3BA8-4706-8C74-30AA12D5EC64

Q37148352-0F2859DB-0FC5-438E-A1E8-A82E5EFA1A30

Q37148352-1A742C95-4C76-4002-85B3-59B5462D1DFA

Q37148352-1AFA7623-7C1E-4B2A-BA7E-156BEE0015D5

Q37148352-1DEA4DDB-92DF-4C83-9546-0BF28BC721E5

Q37148352-25F14F24-0E12-4DC0-B102-2E596ABAF71F

Q37148352-27836CE7-C501-4BDE-9AAE-99C640BA4EE3

Q37148352-2D24D7CC-EA93-4E8B-8DD7-642E7EE28965

Q37148352-2F749F24-D12D-4098-BC78-933BDDAF4590

Q37148352-39550CCD-8964-42D6-BEE8-CA72012358A3

P304

Q37148352-4F7D9611-2F78-45EF-B7A9-22C8C20C0210

P31

Q37148352-8B93AAD8-3E06-4669-ABF1-A9887EF20F77

P356

Q37148352-048730C4-6E36-4BB0-A566-2D7E2C25F6E0

P407

Q37148352-F6D2FD16-A533-428E-A41A-8957B8B33C18

P433

Q37148352-32403E24-931A-4600-B7EC-620700FEA6B2

P478

Q37148352-02DEC040-5903-404A-8A66-5E693BABE462

P577

Q37148352-31E18C2E-26F5-4238-A0C7-B0EE104861E0

P5875

Q37148352-F75D5020-BAF5-4D52-8E66-E5AD491CB8DD

P698

Q37148352-A18CB9A3-1D7C-4220-8E62-597833CAD002

P932

Q37148352-5736328D-0B88-44F0-AC17-5E4F19E089D4

P356

J.JMB.2011.05.005

P1433

Journal of Molecular Biology

P1476

A proteasome assembly defect i ...... creased sensitivity to stress.

@en

P2093

Kiran Madura

http://www.w3.org/2001/XMLSchema#string

Kishore Kumar Joshi

http://www.w3.org/2001/XMLSchema#string

Li Chen

http://www.w3.org/2001/XMLSchema#string

Nidza Torres

http://www.w3.org/2001/XMLSchema#string

Vincent Tournier

http://www.w3.org/2001/XMLSchema#string

P2860

A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes

Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.

Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1

Proteasome subunit Rpn1 binds ubiquitin-like protein domains.

Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion.

Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis.

A proteolytic pathway that recognizes ubiquitin as a degradation signal.

Functional characterization of rpn3 uncovers a distinct 19S proteasomal subunit requirement for ubiquitin-dependent proteolysis of cell cycle regulatory proteins in budding yeast.

Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome.

A cryptic protease couples deubiquitination and degradation by the proteasome.

P304

383-399

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.JMB.2011.05.005

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

410

http://www.w3.org/2001/XMLSchema#string

P577

2011-05-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51172195

http://www.w3.org/2001/XMLSchema#string

P698

21619884

http://www.w3.org/2001/XMLSchema#string

P932

3763486

http://www.w3.org/2001/XMLSchema#string