Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC.
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Oligomeric Bax is a component of the putative cytochrome c release channel MAC, mitochondrial apoptosis-induced channelA novel, high conductance channel of mitochondria linked to apoptosis in mammalian cells and Bax expression in yeastTim18p 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 Tim9 and Tim10 into a functional chaperone.Conserved N-terminal negative charges in the Tim17 subunit of the TIM23 translocase play a critical role in the import of preproteins into mitochondria.Mitochondrial ion channels as therapeutic targets.The envelope anion channel involved in chloroplast protein import is associated with Tic110.Pathophysiological and protective roles of mitochondrial ion channels.The protein import machinery of the mitochondrial membranes.The mechanism of inactivation of a 50-pS envelope anion channel during chloroplast protein importComparison of the TIM and TOM channel activities of the mitochondrial protein import complexes.Effects of cytochrome c on the mitochondrial apoptosis-induced channel MAC.Molecular insights revealing interaction of Tim23 and channel subunits of presequence translocaseIs mPTP the gatekeeper for necrosis, apoptosis, or both?Single channel characterization of the mitochondrial ryanodine receptor in heart mitoplasts.Mitochondrial Ion Channels in Cancer TransformationThe therapeutic potential of mitochondrial channels in cancer, ischemia-reperfusion injury, and neurodegeneration.Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria.Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits.Tim23p contains separate and distinct signals for targeting to mitochondria and insertion into the inner membrane.Assembly of the mitochondrial apoptosis-induced channel, MAC.Electrophysiology clarifies the megariddles of the mitochondrial permeability transition pore.Mitochondrial channels: ion fluxes and more.Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p moleculesThe preprotein conducting channel at the inner envelope membrane of plastidsSome amphiphilic cations block the mitochondrial apoptosis-induced channel, MAC.Two high conductance channels of the mitochondrial inner membrane are independent of the human mitochondrial genome.Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import.A fluorescence assay for peptide translocation into mitochondria.Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins.Effects of dexpramipexole on brain mitochondrial conductances and cellular bioenergetic efficiency.Chemical cleavage of the overexpressed mitochondrial F1beta precursor with CNBr: a new strategy to construct an import-competent preprotein.Role of Tim17 Transmembrane Regions in Regulating the Architecture of Presequence Translocase and Mitochondrial DNA Stability.The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.Structural changes in the mitochondrial Tim23 channel are coupled to the proton-motive force.A transcriptomic and proteomic characterization of the Arabidopsis mitochondrial protein import apparatus and its response to mitochondrial dysfunction.
P2860
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P2860
Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
Tim23, a protein import compon ...... iple conductance channel, MCC.
@ast
Tim23, a protein import compon ...... iple conductance channel, MCC.
@en
type
label
Tim23, a protein import compon ...... iple conductance channel, MCC.
@ast
Tim23, a protein import compon ...... iple conductance channel, MCC.
@en
prefLabel
Tim23, a protein import compon ...... iple conductance channel, MCC.
@ast
Tim23, a protein import compon ...... iple conductance channel, MCC.
@en
P2093
P2860
P356
P1476
Tim23, a protein import compon ...... iple conductance channel, MCC.
@en
P2093
K W Kinnally
R E Jensen
T A Lohret
P2860
P304
P356
10.1083/JCB.137.2.377
P407
P577
1997-04-01T00:00:00Z