Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex.
about
The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c releaseConserved roles of Sam50 and metaxins in VDAC biogenesisTom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteinsAn 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.The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria.Multispan mitochondrial outer membrane protein Ugo1 follows a unique Mim1-dependent import pathway.Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly.Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formationThe mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins.The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology.Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth SyndromeBiogenesis of the mitochondrial TOM complex: Mim1 promotes insertion and assembly of signal-anchored receptors.Assembly of the TOB complex of mitochondria.Granzyme B enters the mitochondria in a Sam50-, Tim22- and mtHsp70-dependent manner to induce apoptosis.Characterization 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.Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteinsChloroplast β-barrel proteins are assembled into the mitochondrial outer membrane in a process that depends on the TOM and TOB complexes.Biogenesis of mitochondrial β-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex.Mitochondria can recognize and assemble fragments of a beta-barrel structure.Helicobacter pylori VacA toxin/subunit p34: targeting of an anion channel to the inner mitochondrial membrane.Roles of the Mdm10, Tom7, Mdm12, and Mmm1 proteins in the assembly of mitochondrial outer membrane proteins in Neurospora crassaBacterial porin disrupts mitochondrial membrane potential and sensitizes host cells to apoptosis.Genetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37.Downregulation of mitochondrial porin inhibits cell growth and alters respiratory phenotype in Trypanosoma brucei.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.Alternative splicing gives rise to different isoforms of the Neurospora crassa Tob55 protein that vary in their ability to insert beta-barrel proteins into the outer mitochondrial membrane.The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins.Mitochondrial protein sorting: differentiation of beta-barrel assembly by Tom7-mediated segregation of Mdm10.Effect of mutations in Tom40 on stability of the translocase of the outer mitochondrial membrane (TOM) complex, assembly of Tom40, and import of mitochondrial preproteins.Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria.A 3D model of the voltage-dependent anion channel (VDAC).VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways.Mitochondrial protein import: recognition of internal import signals of BCS1 by the TOM complexCharacterization of a human import component of the mitochondrial outer membrane, TOMM70A.Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum.
P2860
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P2860
Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Biogenesis of porin of the out ...... mport pore of the TOM complex.
@en
type
label
Biogenesis of porin of the out ...... mport pore of the TOM complex.
@en
prefLabel
Biogenesis of porin of the out ...... mport pore of the TOM complex.
@en
P2093
P2860
P921
P356
P1476
Biogenesis of porin of the out ...... mport pore of the TOM complex.
@en
P2093
C K Kassenbrock
E Blachly-Dyson
F E Nargang
M G Douglas
P2860
P304
P356
10.1083/JCB.152.2.289
P407
P577
2001-01-01T00:00:00Z