Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
about
The complete plastid genome sequence of the parasitic green alga Helicosporidium sp. is highly reduced and structuredNucleotide-dependent substrate recognition by the AAA+ HslUV protease.Membrane proteases in the bacterial protein secretion and quality control pathway.Phage shock protein C (PspC) of Yersinia enterocolitica is a polytopic membrane protein with implications for regulation of the Psp stress responseATP-dependent proteases differ substantially in their ability to unfold globular proteinsQuality control of cytoplasmic membrane proteins in Escherichia coli.Evolutionary Dynamics of Cryptophyte Plastid GenomesTesting the Role of the N-Terminal Tail of D1 in the Maintenance of Photosystem II in Tobacco ChloroplastsMembrane protein degradation by FtsH can be initiated from either end.Conditional Proteolysis of the Membrane Protein YfgM by the FtsH Protease Depends on a Novel N-terminal Degron.Reconstitution of membrane proteolysis by FtsH.Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli.The C-terminal end of LpxC is required for degradation by the FtsH protease.Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.Stable membrane orientations of small dual-topology membrane proteins.In vivo trapping of FtsH substrates by label-free quantitative proteomics.The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site.The Escherichia coli plasma membrane contains two PHB (prohibitin homology) domain protein complexes of opposite orientations.Subunit organization of a synechocystis hetero-oligomeric thylakoid FtsH complex involved in photosystem II repair.Folding-Degradation Relationship of a Membrane Protein Mediated by the Universally Conserved ATP-Dependent Protease FtsH.FtsH Protease in the Thylakoid Membrane: Physiological Functions and the Regulation of Protease Activity.
P2860
Q22065296-183D9319-BEC1-457A-9E6B-9E5CBE789D7FQ34391837-0C7F32BD-82AC-4DFC-8D64-4E05A3329838Q36023269-6B0FDB21-D817-42A0-A712-10463ACA3E71Q36397093-10E27D34-AB20-4FF5-A5A1-550119B78E8AQ37254059-6FA27968-AA1A-43E1-A58F-5B5EC54A9827Q37489256-6789855B-03C1-4336-8F67-C96BB0D84A2DQ38602005-0BD85EFD-9818-4ECF-86E0-81B5302BAF0BQ39572410-71727663-E74B-4043-96EA-7AB41D82EBBFQ39680104-8D666285-9698-48C1-873A-B0990BB6C2B4Q40818234-0AB10539-8BD2-4EB8-A593-254803DC03E8Q44365527-3994453A-C788-400F-AD83-D0210C60F775Q46632169-A2D28802-7B11-4C88-9166-ACB3CFDFED16Q46899391-17930306-468C-498D-A163-EAF5ED84A0F2Q47611950-76F9B98B-8289-46EB-BD19-80EDE8C09E0BQ48143169-BD3B2477-65C6-48AC-8001-7EAAB7457294Q51371510-C23A0CF4-25BC-4E7C-A5BB-1A96E57E0ACDQ52546489-22E20D18-66BB-4AF4-884E-FA4B081F315DQ52569631-1C684D89-C6FB-4411-8151-AFB792915D36Q53144458-186865BE-E53E-4094-8018-51391C9DC1A2Q54975593-F250C8ED-5064-4CBF-BCAB-AED1F30311E1Q55433939-4851B08B-7F48-4D0B-AB2B-A77302EBB97C
P2860
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@en
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@nl
type
label
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@en
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@nl
prefLabel
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@en
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@nl
P2093
P2860
P356
P1433
P1476
Length recognition at the N-terminal tail for the initiation of FtsH-mediated proteolysis
@en
P2093
P2860
P356
10.1093/EMBO-REPORTS/KVD005
P577
2000-07-01T00:00:00Z