ArticleThe Journal of biological chemistry2014
Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 18 citations in OpenAlex.
- Effects of homozygous PARK7 gene mutations L166P and M26I on BNIP3/BNIP3L interactions and ER-mitochondria proximity.Biology direct · 2026Article
- Membrane Lipid Composition Influences the Hydration of Proton Half-Channels in FLife (Basel, Switzerland) · 2023Article
- Structural Basis for Chaperone-Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP.Angewandte Chemie (International ed. in English) · 2022Article
- Semisynthetic Modification of Tau Protein with Di-Ubiquitin Chains for Aggregation Studies.International journal of molecular sciences · 2020Article
- Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.Science advances · 2017Article
- Buckling Under Pressure: Curvature-Based Lipid Segregation and Stability Modulation in Cardiolipin-Containing Bilayers.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Journal of bioenergetics and biomembranes · 2017Review
- Cardiolipin puts the seal on ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.3 Biotech · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tim23 mediates protein translocation into mitochondria. Although inserted into the inner membrane, the dynamic association of its intermembrane space (IMS) domain with the outer membrane promotes protein import. However, little is known about the molecular basis of this interaction. Here, we demonstrate that the IMS domain of Tim23 tightly associates with both inner and outer mitochondrial membrane-like membranes through a hydrophobic anchor at its N terminus. The structure of membrane-bound Tim23(IMS) is highly dynamic, allowing recognition of both the incoming presequence and other translocase components at the translocation contact. Cardiolipin enhances Tim23 membrane attachment, suggesting that cardiolipin can influence preprotein import.
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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.