Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
about
The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complexTom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondriaFunctional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complexThe Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane.Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membraneTom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment].Assembly of the mitochondrial protein import channel: role of Tom5 in two-stage interaction of Tom40 with the SAM complexIntermembrane space proteome of yeast mitochondria.Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteinsTim9, a new component of the TIM22.54 translocase in mitochondriaTaz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth SyndromePreprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex.Tim9p, an essential partner subunit of Tim10p for the import of mitochondrial carrier proteins.Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes.Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathwayCarrier protein import into mitochondria mediated by the intermembrane proteins Tim10/Mrs11 and Tim12/Mrs5.Import of yeast mitochondrial transcription factor (Mtf1p) via a nonconventional pathway.Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and diseaseFunctional staging of ADP/ATP carrier translocation across the outer mitochondrial membraneThe three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondriaSelf-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membraneImporting mitochondrial proteins: machineries and mechanismsEvidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40.Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrixGenetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37.Mitochondrial protein sorting: differentiation of beta-barrel assembly by Tom7-mediated segregation of Mdm10.VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways.Mitochondrial lysyl-tRNA synthetase independent import of tRNA lysine into yeast mitochondria.Biogenesis of mitochondrial inner membrane proteins.Import of carrier proteins into mitochondria.Targeting and insertion of nuclear-encoded preproteins into the mitochondrial outer membrane.Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis.Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane.Regulation of base excision repair: Ntg1 nuclear and mitochondrial dynamic localization in response to genotoxic stressThe protein import machinery of the mitochondrial membranes.ATP transport through a single mitochondrial channel, VDAC, studied by current fluctuation analysis.Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.Genome-wide screen for genes with effects on distinct iron uptake activities in Saccharomyces cerevisiaeMitochondrial protein import and the genesis of steroidogenic mitochondria
P2860
Q24532734-91C37DEF-7986-4227-8D3B-F1B657F9E851Q24534161-1D50B40F-CDC0-45DA-86F6-B32403776332Q24679359-572D953D-5FE4-4A48-8905-9AFD9673CF59Q27930731-47DEC5C3-FCA9-42FD-995B-881A4F7CE6AAQ27931625-387C84D6-D129-4FDA-90E3-54CEBF5F3CA7Q27933650-E2FA8772-9135-4B7E-B8D2-6FBEFF50C59DQ27934927-A2DE7D9A-63E5-466E-918A-AC15A8DC5E7EQ27935538-85E5D0B2-30ED-4AA9-9983-DC318E422BA9Q27935768-E3962FF6-632A-430A-A698-53D080A4868AQ27936064-2862CFA7-1397-4776-B692-B62888799E8FQ27936311-AEBAC9FC-6FB7-44C8-8B84-EF3454658F82Q27936928-8331D5D1-31A1-482C-858C-E491605EB5EAQ27937503-0BFD96BB-B0D8-4150-8348-A67F8628B3E8Q27937864-5B5DA3F7-E08D-4A83-9705-EED9EC2679D7Q27939155-EE4870DB-3949-4F30-AD65-DEBE37D2C9C4Q27939312-3F02402F-E61C-481A-868F-79FDF060706FQ27939464-4FB7DF09-C3B4-4067-A901-0A0241BBE4FEQ27939604-7B2DE851-A33E-4A9F-8974-36B63B37C36FQ28076268-6278AA91-8F1B-482C-845B-CC307729F7B6Q28139290-8FEFF215-A70A-42B2-9E2C-288EA99B48A9Q28354447-518597F5-6327-4E07-B611-01676D605A1BQ28364286-1D04EE28-2EEB-491B-8DD4-9A6B8A81DD24Q29616477-9D24C6F6-6E69-474D-ACDB-4A00CAAD96FFQ30152835-211940E6-FE04-4657-9EF1-DB9622974AF2Q30153367-1D274780-A5B2-4E5F-A7D8-856EE51760C0Q30157100-EDAA1AC0-19C0-4615-9DFA-D9D8767B1E1EQ30159775-499F281B-F95D-414F-B744-B3F7DA71A242Q30165487-D5BA2A45-02FA-4C55-9B2B-907D4FBA9424Q31059637-A806E3CE-FC7F-4EB6-85DA-D8D7FAE875BBQ33786902-EBE6BA4B-DE1F-4DBD-A131-24A1B6866394Q33793004-CDF4156A-3A2E-4719-8CBB-FE7286FF38AEQ33866727-FC0FF442-1FF3-4F3F-9F67-C919C815B20DQ33889115-A0CE1B37-75B2-4B09-9690-CB63F95F60D8Q33910065-0EB8222E-C08E-4251-B304-8C71F33CD154Q33959367-0DF44230-ED19-4E4D-89CA-ECB79B83CC98Q34156674-34948850-721D-4B2D-BEE0-3B387D748B5EQ34167822-A6EE6419-CC24-4462-8349-EEB610071C5FQ34540380-32498C50-197E-4D5F-AB0A-E1C950169A26Q34570090-F6440778-100D-49B8-A0F4-9A9100079C21Q34672406-287821CA-9FA3-4873-85DC-83DB247F6FB8
P2860
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@ast
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@en
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@nl
type
label
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@ast
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@en
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@nl
altLabel
Tom5 functionally links mitochondrial preprotein receptors to the general import pore
@en
prefLabel
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@ast
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@en
Tom5 functionally links mitochondrial preprotein receptors to the general import pore.
@nl
P2093
P2860
P356
P1433
P1476
Tom5 functionally links mitochondrial preprotein receptors to the general import pore
@en
P2093
Dietmeier K
Eckerskorn C
Hönlinger A
Lottspeich F
P2860
P2888
P304
P356
10.1038/40663
P407
P50
P577
1997-07-01T00:00:00Z
P6179
1022738815