Role of the heat shock protein DnaJ in the lon-dependent degradation of naturally unstable proteins.
about
The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging systemA unifying theory for general multigenic heterosis: energy efficiency, protein metabolism, and implications for molecular breedingEcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli.Evidence that two ATP-dependent (Lon) proteases in Borrelia burgdorferi serve different functionsThe molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli.Stabilizing C-terminal tails on AraC.Analysis of the Escherichia coli Alp phenotype: heat shock induction in ssrA mutantsAntisense downregulation of sigma(32) as a transient metabolic controller in Escherichia coli: effects on yield of active organophosphorus hydrolase.Escherichia coli RcsA, a positive activator of colanic acid capsular polysaccharide synthesis, functions To activate its own expression.The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coliRedundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) protease.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Side effects of chaperone gene co-expression in recombinant protein production.Identification of a small-molecule inhibitor of bacterial AraC family activators.Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid systemATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions.Proteotoxic stress induces a cell-cycle arrest by stimulating Lon to degrade the replication initiator DnaASubstrate sequestration by a proteolytically inactive Lon mutant.ATP-dependent proteases differ substantially in their ability to unfold globular proteinsSmall-molecule inhibitor of the Shigella flexneri master virulence regulator VirF.Two outer membrane proteins contribute to cellular fitness in Caulobacter crescentus by preventing intracellular S-layer protein accumulation.Relaxase DNA binding and cleavage are two distinguishable steps in conjugative DNA processing that involve different sequence elements of the nic siteEvidence for an active role of the DnaK chaperone system in the degradation of sigma(32).Molecular basis for the temperature sensitivity of Escherichia coli pth(Ts).A membrane-bound archaeal Lon protease displays ATP-independent proteolytic activity towards unfolded proteins and ATP-dependent activity for folded proteinsPotential use of toxic thermolabile proteins to study protein quality control systems.Conserved region 2.1 of Escherichia coli heat shock transcription factor sigma32 is required for modulating both metabolic stability and transcriptional activity.Rehosting of bacterial chaperones for high-quality protein production.Cross-system excision of chaperone-mediated proteolysis in chaperone-assisted recombinant protein productionStochastic kinetic analysis of the Escherichia coli stress circuit using sigma(32)-targeted antisense.On the mechanism of FtsH-dependent degradation of the sigma 32 transcriptional regulator of Escherichia coli and the role of the Dnak chaperone machine.ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system.Role of molecular chaperones in inclusion body formation.
P2860
Q24603386-FA78F0C8-D480-4FC5-B6E5-3E2E1F2B6536Q26809996-5790CD99-808E-47FD-99A1-7D05C22538B2Q28363070-215502D5-F6BC-4A87-8FE4-DB0D6A18CA0DQ28472063-1D7125D1-1705-42D8-8628-35026209BF8EQ31523861-4F67B6CC-AF69-4D48-9F0D-6B4A4106B78BQ31709878-E8D53852-595E-4D73-8761-A9AE1B2DA8B9Q33885728-9BE62C5B-3059-4196-A001-F8EE454998C5Q33987812-082BE3D7-A0A3-47DD-A206-58533DD00B06Q33991039-BD423768-173F-4918-A00A-F82B34CF2D0DQ33992303-D72101A7-2C48-4234-A168-662E3AC990BBQ33992310-B6338840-F345-472A-9A9E-E6651EC99F41Q34004070-B8602CDD-9A3E-447B-92A9-EEFBAFA2DDC1Q34148952-D77AA193-DDE9-455B-B967-C69F0425255EQ34567886-E08D25E0-9627-4DFD-B10E-56F4C830B24CQ34891158-7B1CF265-6C12-4560-BD9B-A4AF7C65CB60Q36831491-F01C205E-9539-4970-B5FD-1BCCD048DF76Q37110188-E4BD117B-E780-4159-9726-9C941F2D4250Q37195892-A3B34687-9C32-4A1C-AC5D-DFF081A976DCQ37254059-747A7318-2764-41C7-987D-68F9EC9B8FA8Q37264871-1EAD19B6-3E1B-4123-97A7-9246EA58F669Q37405377-21ECD2B7-EF65-4B25-B0F6-F376F08FE8F1Q38347343-37B9FF8B-8BB9-466F-8F7D-0E5C65CA918BQ38496040-D83D673B-3EA8-4EB3-A116-CE4443A828D4Q39499457-702188DC-6AFA-4664-8EAF-3250AAB342D0Q39679563-7C52D004-C079-4859-BE01-116B452B65F2Q40003136-2685B7C9-86EE-45B4-A46A-35A60E7B86AEQ40270839-8622446E-E276-4698-B8D9-E20BE8D9B521Q41857772-E849EA69-5C1A-4073-9BBA-5B0A759F275AQ42579547-910FB24F-2CE1-4F57-9005-98197AE94BFAQ43728249-168AB049-E9E9-4F08-B11F-860C3EBEB95DQ47271506-6CF65A3C-815F-4845-B9EB-6F40DD9FEA23Q47761036-44E29F43-2994-4387-A5F3-77BCA6CB1060Q54529590-AA2F1D95-1886-4956-A276-EEA03D56847C
P2860
Role of the heat shock protein DnaJ in the lon-dependent degradation of naturally unstable proteins.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Role of the heat shock protein ...... f naturally unstable proteins.
@en
Role of the heat shock protein ...... f naturally unstable proteins.
@nl
type
label
Role of the heat shock protein ...... f naturally unstable proteins.
@en
Role of the heat shock protein ...... f naturally unstable proteins.
@nl
prefLabel
Role of the heat shock protein ...... f naturally unstable proteins.
@en
Role of the heat shock protein ...... f naturally unstable proteins.
@nl
P2093
P2860
P356
P1476
Role of the heat shock protein ...... f naturally unstable proteins.
@en
P2093
P2860
P304
30798-30803
P356
10.1074/JBC.271.48.30798
P407
P577
1996-11-01T00:00:00Z