ArticleBiophysical journal2010
Interactions of mitochondrial presequence peptides with the mitochondrial outer membrane preprotein translocase TOM.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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
10 citing papers in PubMed, 20 citations in OpenAlex.
- The TOM Complex in the Outer Membrane of Mitochondria: A Supramolecular Assembly for Protein Import.Advances in experimental medicine and biology · 2026Review
- New insights into the structure and dynamics of the TOM complex in mitochondria.Biochemical Society transactions · 2024Review
- Tracking the Activity and Position of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Review
- Reconstitution of the membrane protein OmpF into biomimetic block copolymer-phospholipid hybrid membranes.Beilstein journal of nanotechnology · 2016Article
- Crosstalk between mitochondria and peroxisomes.World journal of biological chemistry · 2015Review
- Watching single proteins using engineered nanopores.Protein and peptide letters · 2014Review
- Peptide translocation through the mesoscopic channel: binding kinetics at the single molecule level.European biophysics journal : EBJ · 2013Article
- Protein translocation through Tom40: kinetics of peptide release.Biophysical journal · 2012Article
- Functional refolding and characterization of two Tom40 isoforms from human mitochondria.The Journal of membrane biology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TOM protein-conducting channels serve as the main entry sites into mitochondria for virtually all mitochondrial proteins. When incorporated into lipid bilayers, they form large, relatively nonspecific ion channels that are blocked by peptides derived from mitochondrial precursor proteins. Using single-channel electrical recordings, we analyzed the interactions of mitochondrial presequence peptides with single TOM pores. The largest conductance state of the translocon represents the likely protein-conducting conformation of the channel. The frequency (but not the duration) of the polypeptide-induced blockage is strongly modulated by the substrate concentration. Structural differences between substrates are reflected in characteristic blockage frequencies and duration of blockage. To our knowledge, this study provides first quantitative data regarding the kinetics of polypeptide interaction with the mitochondrial TOM machinery.
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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.