Molecular cloning and characterization of a mouse homolog of bacterial ClpX, a novel mammalian class II member of the Hsp100/Clp chaperone family
about
Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXPHuman mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpXCross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and DiseaseIdentification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana.Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases.N-terminal RAG1 frameshift mutations in Omenn's syndrome: internal methionine usage leads to partial V(D)J recombination activity and reveals a fundamental role in vivo for the N-terminal domains.Mitochondrial ClpP activity is required for cisplatin resistance in human cells.Quality control of mitochondrial proteostasis.Analysis of steroid-induced genes in the rat preoptic area-anterior hypothalamus using a differential-display reverse transcriptase-polymerase chain reaction.Frataxin deficiency causes upregulation of mitochondrial Lon and ClpP proteases and severe loss of mitochondrial Fe-S proteins.Mutations conferring amino acid residue substitutions in the carboxy-terminal domain of RNA polymerase alpha can suppress clpX and clpP with respect to developmentally regulated transcription in Bacillus subtilis.
P2860
Q24292867-3DC8FBA0-8A04-412F-B3D9-B10A617EFAA3Q24317060-D150EAF0-B0EC-4DE8-A4C5-3347AC71F6F6Q26765684-C2D002D8-5860-46DD-934F-CA92D2E99890Q30984811-53B78F93-3E76-4FC1-82F1-D3E77B55BE10Q34357337-86805577-7365-4E86-BA1C-F59DA0CF3A25Q34636507-9842792A-B956-4BFD-A35C-C74A92920395Q35850311-37416C9D-B7B7-4964-A028-3BD7CD161A41Q36677047-DC94B11F-85DC-41B8-8F85-D607EF5DC924Q37882863-E4052296-F187-4FA6-82FF-D083CFB33CB3Q43644927-F27D63B1-F28C-4BFB-9133-849A22B236FDQ46156695-276E347D-0BCC-420C-ACB3-2E9EA83D5834Q52165537-21B50257-7406-4034-B975-1317A2117F40
P2860
Molecular cloning and characterization of a mouse homolog of bacterial ClpX, a novel mammalian class II member of the Hsp100/Clp chaperone family
description
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 1999
@ast
im Juni 1999 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1999/06/04)
@sk
vědecký článek publikovaný v roce 1999
@cs
wetenschappelijk artikel (gepubliceerd op 1999/06/04)
@nl
наукова стаття, опублікована в червні 1999
@uk
name
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@ast
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@en
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@nl
type
label
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@ast
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@en
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@nl
prefLabel
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@ast
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@en
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@nl
P2093
P2860
P921
P356
P1476
Molecular cloning and characte ...... he Hsp100/Clp chaperone family
@en
P2093
A. Hodtsev
D. Bhattacharyya
E. Spanopoulou
F. H. Wang
S. Santagata
P2860
P304
16311–16319
P356
10.1074/JBC.274.23.16311
P407
P577
1999-06-04T00:00:00Z