The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
about
Function and evolution of a minimal plastid genome from a nonphotosynthetic parasitic plantProteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon proteaseCDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3pHuman ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the geneNin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiaeA human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon proteaseNewly identified pair of proteasomal subunits regulated reciprocally by interferon gammaMapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradationYeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritimaThe crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coliThe catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active siteStructural Insights into the Regulatory Particle of the Proteasome from Methanocaldococcus jannaschiiStructural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon proteaseArginine phosphorylation marks proteins for degradation by a Clp proteaseCrystal structure of a ubiquitin-dependent degradation substrate: a three-disulfide form of lysozymeCrystal structure of heat shock locus V (HslV) from Escherichia coliHSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases.Sue1p is required for degradation of labile forms of altered cytochromes C in yeast mitochondria.An essential yeast gene encoding a homolog of ubiquitin-activating enzyme.Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70The Ubc3 (Cdc34) ubiquitin-conjugating enzyme is ubiquitinated and phosphorylated in vivoRegulation of SulA cleavage by Lon protease by the C-terminal amino acid of SulA, histidineThe ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine proteasePolyphosphate--an ancient energy source and active metabolic regulatorThe proteolytic fragments generated by vertebrate proteasomes: structural relationships to major histocompatibility complex class I binding peptides.The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli.Intrinsic thermal sensing controls proteolysis of Yersinia virulence regulator RovA.Molecular determinants of MecA as a degradation tag for the ClpCP protease.Proteolysis and class I major histocompatibility complex antigen presentation.An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 S proteasome, activates protein breakdown by 20 S proteasomes.A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity.Expression of listeriolysin O and ActA by intracellular and extracellular Listeria monocytogenes.Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomesDetermination of the cleavage sites in SulA, a cell division inhibitor, by the ATP-dependent HslVU protease from Escherichia coli.Biological roles of the Podospora anserina mitochondrial Lon protease and the importance of its N-domain.Heat shock proteins: molecular chaperones of protein biogenesis.Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli.Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli.Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene.
P2860
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P2860
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@ast
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@en
type
label
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@ast
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@en
prefLabel
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@ast
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@en
P2860
P1433
P1476
The mechanism and functions of ATP-dependent proteases in bacterial and animal cells.
@en
P2093
A L Goldberg
P2860
P356
10.1111/J.1432-1033.1992.TB19822.X
P407
P577
1992-01-01T00:00:00Z