Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment].
about
Characterization of rat TOM40, a central component of the preprotein translocase of the mitochondrial outer membraneTransport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complexHuman mitochondrial complex I in health and diseaseTom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteinsTom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondriaA novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeastFrom evolution to pathogenesis: the link between β-barrel assembly machineries in the outer membrane of mitochondria and gram-negative bacteriaStructure of the human voltage-dependent anion channelAn essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane.Mim1, a protein required for the assembly of the TOM complex of mitochondriaSam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability.Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membraneTwo novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly.Rpm2, the protein subunit of mitochondrial RNase P in Saccharomyces cerevisiae, also has a role in the translation of mitochondrially encoded subunits of cytochrome c oxidase.Assembly of the mitochondrial protein import channel: role of Tom5 in two-stage interaction of Tom40 with the SAM complexNucleoside diphosphate kinase of Saccharomyces cerevisiae, Ynk1p: localization to the mitochondrial intermembrane space.Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteinsProteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteinsLateral release of proteins from the TOM complex into the outer membrane of mitochondria.Biogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.Assembly of Tim9 and Tim10 into a functional chaperone.Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathwayImport of yeast mitochondrial transcription factor (Mtf1p) via a nonconventional pathway.The Import of Proteins into the Mitochondrion of Toxoplasma gondiiResidues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tetheringTIM29 is a subunit of the human carrier translocase required for protein transportFunctional staging of ADP/ATP carrier translocation across the outer mitochondrial membraneThe three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondriaApocytochrome c requires the TOM complex for translocation across the mitochondrial outer membraneSelf-association and precursor protein binding of Saccharomyces cerevisiae Tom40p, the core component of the protein translocation channel of the mitochondrial outer membraneMembrane-embedded C-terminal segment of rat mitochondrial TOM40 constitutes protein-conducting pore with enriched beta-structureGranzyme B enters the mitochondria in a Sam50-, Tim22- and mtHsp70-dependent manner to induce apoptosis.Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA.Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10Evidence of Distinct Channel Conformations and Substrate Binding Affinities for the Mitochondrial Outer Membrane Protein Translocase Pore Tom40.A novel Mitosomal β-barrel Outer Membrane Protein in EntamoebaPresequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrixEvidence supporting the 19 β-strand model for Tom40 from cysteine scanning and protease site accessibility studies.Weakly stable regions and protein-protein interactions in beta-barrel membrane proteinsThe Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals
P2860
Q24290217-0B1A7CAB-AEBB-4B79-A11B-74DD2FBC2C61Q24534161-A6785D14-BDAA-423A-BA07-BD2E16E76538Q24540036-AEF4237B-C32F-4142-AF7F-705306673036Q24677698-B599FC7E-0DC5-406C-9CF8-369D7E760586Q24679359-B0427983-B41B-49E1-883E-02F3916F67B9Q24685400-B4BEF5E3-0217-4561-AD6C-ABF5226EC3BEQ26829991-97D31FD7-604E-47A2-ADAC-8542E175BD61Q27652383-6138A13B-C276-459C-BF9E-50B30269AF59Q27930688-EAF099BF-13CC-40B8-9619-1733AC6A79ACQ27931080-F905874D-D620-4442-8AB6-AC7D37A55281Q27931312-16E61ED2-E063-4D82-BEA5-6D9B5D7AE48EQ27933650-88911FD5-A8EB-4C40-8F09-081BE5251225Q27933766-4B45D505-4126-4E81-8F2F-FA1683266838Q27934867-ACC63801-7648-4A2C-B17B-167D6605C9BFQ27935538-B5DA612D-8BC6-4759-A5FA-2DAE713CB42DQ27935840-8D1A011A-9372-47C1-92C3-1746968F0FC5Q27936064-9D1D731D-E4BF-4E0A-98B9-43B8C819B038Q27937249-FBA8AE84-32CE-4283-9665-5FBD0DDFAFAEQ27937520-28846C49-7438-43DC-B0EE-FC8F2CED844AQ27937853-3827CF1B-BE37-4544-BD1D-73C2AF2A258BQ27938777-590AC415-A7F3-4AB9-A503-7E0B738009B3Q27939312-392730CB-F982-4D06-A92D-0C8200EDAB98Q27939604-3D9290FB-29DD-4679-B392-92508015FF3AQ27972732-6421AD8E-023F-416E-80D4-6649150B9ADBQ28114318-01EB9A92-6F82-4D64-A87C-2329287527B7Q28118577-2819E87B-E7FA-4842-B935-9C90A5078C7DQ28139290-465558BC-1A0A-4419-B25F-B6818B18463CQ28354447-F9E62CC8-F269-4AB9-B341-B3737AEF5E23Q28361325-D11879A4-C0B9-47EA-92AB-962C88A07725Q28364286-E449BD58-6034-474A-AE0E-8F879F64F078Q28578464-CE663617-8530-4813-8149-D23D35CF34DBQ30152650-BB7DE0FC-1032-41DC-BB61-13A2FD952AB2Q30152682-A3A2EEFE-B502-46BC-A43D-8FD2CB02C202Q30152716-FAD13F56-C50E-4786-9D3F-03FDD36A679FQ30152835-27496777-B5A9-405E-B5AC-D4227C9424AAQ30152977-EF1149E1-85E0-4D14-8B19-6C2EA1285281Q30153367-5EC4EF13-5D24-4F3D-93C4-6210A35DFCBEQ30153385-5F4CDFC7-434A-4305-AB15-F16D34F0619FQ30155086-5943FB5B-32EC-4743-ACF0-415C51173A19Q30155245-D7A547BE-09F2-4611-B144-6BFBBD63CB2D
P2860
Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins [see comment].
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@ast
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@en
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@nl
type
label
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@ast
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@en
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@nl
prefLabel
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@ast
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@en
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@nl
P2093
P2860
P356
P1433
P1476
Tom40 forms the hydrophilic ch ...... for preproteins [see comment].
@en
P2093
K Dietmeier
P2860
P2888
P304
P356
10.1038/26780
P407
P577
1998-10-01T00:00:00Z
P6179
1042308665