ArticleBiophysical journal2003
Comparison of the TIM and TOM channel activities of the mitochondrial protein import complexes.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 55 citations in OpenAlex.
- CALHM2 is a mitochondrial protein import channel that regulates fatty acid metabolism.Research square · 2024Article
- Article
- Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Journal of bioenergetics and biomembranes · 2017Review
- A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import.The Journal of cell biology · 2016Article
- Crosstalk between mitogen-activated protein kinases and mitochondria in cardiac diseases: therapeutic perspectives.Pharmacology & therapeutics · 2014Review
- Watching single proteins using engineered nanopores.Protein and peptide letters · 2014Review
- Protein translocation through Tom40: kinetics of peptide release.Biophysical journal · 2012Article
- The therapeutic potential of mitochondrial channels in cancer, ischemia-reperfusion injury, and neurodegeneration.Mitochondrion · 2012Review
- Measuring mitochondrial function in intact cardiac myocytes.Journal of molecular and cellular cardiology · 2012Review
- Single channel characterization of the mitochondrial ryanodine receptor in heart mitoplasts.The Journal of biological chemistry · 2011Article
- Amphipathic tail-anchoring peptide and Bcl-2 homology domain-3 (BH3) peptides from Bcl-2 family proteins induce apoptosis through different mechanisms.The Journal of biological chemistry · 2011Article
- Interactions of mitochondrial presequence peptides with the mitochondrial outer membrane preprotein translocase TOM.Biophysical journal · 2010Article
- Potential therapeutic benefits of strategies directed to mitochondria.Antioxidants & redox signaling · 2010Review
- Applications of biological pores in nanomedicine, sensing, and nanoelectronics.Current opinion in biotechnology · 2010Review
- Factors governing helix formation in peptides confined to carbon nanotubes.Nano letters · 2008Article
- Dynamics of the preprotein translocation channel of the outer membrane of mitochondria.Biophysical journal · 2008Article
- Excursion of a single polypeptide into a protein pore: simple physics, but complicated biology.European biophysics journal : EBJ · 2008Article
- Reflections on VDAC as a voltage-gated channel and a mitochondrial regulator.Journal of bioenergetics and biomembranes · 2008Review
- A fluorescence assay for peptide translocation into mitochondria.Analytical biochemistry · 2007Article
- Mitochondrial ion channels: gatekeepers of life and death.Physiology (Bethesda, Md.) · 2005Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Water-filled channels are central to the process of translocating proteins since they provide aqueous pathways through the hydrophobic environment of membranes. The Tom and Tim complexes translocate precursors across the mitochondrial outer and inner membranes, respectively, and contain channels referred to as TOM and TIM (previously called PSC and MCC). In this study, little differences were revealed from a direct comparison of the single channel properties of the TOM and TIM channels of yeast mitochondria. As they perform similar functions in translocating proteins across membranes, it is not surprising that both channels are high conductance, voltage-dependent channels that are slightly cation selective. Reconstituted TIM and TOM channel activities are not modified by deletion of the outer membrane channel VDAC, but are similarly affected by signal sequence peptides.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.