Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly.
about
Membrane protein insertion: mixing eukaryotic and prokaryotic concepts.Conserved roles of Sam50 and metaxins in VDAC biogenesisMultiple pathways for sorting mitochondrial precursor proteinsSystem-level impact of mitochondria on fungal virulence: to metabolism and beyondMim1, a protein required for the assembly of the TOM complex of mitochondriaThe morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.Multispan mitochondrial outer membrane protein Ugo1 follows a unique Mim1-dependent import pathway.Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria.Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40Mcp3 is a novel mitochondrial outer membrane protein that follows a unique IMP-dependent biogenesis pathwayCharacterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import.The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins.Assembly of the mitochondrial protein import channel: role of Tom5 in two-stage interaction of Tom40 with the SAM complexThe cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology.Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteinsThe role of Djp1 in import of the mitochondrial protein Mim1 demonstrates specificity between a cochaperone and its substrate protein.Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space.Cell wall integrity is linked to mitochondria and phospholipid homeostasis in Candida albicans through the activity of the post-transcriptional regulator Ccr4-Pop2.Biogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.Assembly of the TOB complex of mitochondria.Specific targeting of proteins to outer envelope membranes of endosymbiotic organelles, chloroplasts, and mitochondriaImporting mitochondrial proteins: machineries and mechanismsCharacterization of the targeting signal in mitochondrial β-barrel proteins.Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.In vivo roles of BamA, BamB and BamD in the biogenesis of BamA, a core protein of the β-barrel assembly machine of Escherichia coli.Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteinsCharacterization of the insertase for β-barrel proteins of the outer mitochondrial membraneThe Tom40 assembly process probed using the attachment of different intramitochondrial sorting signalsRole of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane.Assembly of the β-Barrel Outer Membrane Proteins in Gram-Negative Bacteria, Mitochondria, and Chloroplasts.Targeting of Neisserial PorB to the mitochondrial outer membrane: an insight on the evolution of β-barrel protein assembly machines.The Neurospora crassa TOB complex: analysis of the topology and function of Tob38 and Tob37Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex.Neisserial Omp85 protein is selectively recognized and assembled into functional complexes in the outer membrane of human mitochondria.Mitochondria can recognize and assemble fragments of a beta-barrel structure.Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassaGenetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37.Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence.Signals in bacterial beta-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria.
P2860
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P2860
Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly.
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Two novel proteins in the mito ...... beta-barrel protein assembly.
@ast
Two novel proteins in the mito ...... beta-barrel protein assembly.
@en
Two novel proteins in the mito ...... beta-barrel protein assembly.
@nl
type
label
Two novel proteins in the mito ...... beta-barrel protein assembly.
@ast
Two novel proteins in the mito ...... beta-barrel protein assembly.
@en
Two novel proteins in the mito ...... beta-barrel protein assembly.
@nl
prefLabel
Two novel proteins in the mito ...... beta-barrel protein assembly.
@ast
Two novel proteins in the mito ...... beta-barrel protein assembly.
@en
Two novel proteins in the mito ...... beta-barrel protein assembly.
@nl
P2093
P2860
P921
P3181
P356
P1476
Two novel proteins in the mito ...... beta-barrel protein assembly.
@en
P2093
Daigo Ishikawa
Hayashi Yamamoto
Kaori Moritoh
Toshiya Endo
P2860
P3181
P356
10.1083/JCB.200405138
P407
P577
2004-08-30T00:00:00Z