ReviewInternational journal of molecular sciences2013
Folding and biogenesis of mitochondrial small Tim proteins.
Review in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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
15 citing papers in PubMed, 24 citations in OpenAlex.
- Galactokinase 1 Positively Regulates Mitochondrial Respiration by Phosphorylating TIMM13 as a Protein Kinase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- TIMM9 as a prognostic biomarker in multiple cancers and its associated biological processes.Scientific reports · 2024Article
- Role of Yme1 in mitochondrial protein homeostasis: from regulation of protein import, OXPHOS function to lipid synthesis and mitochondrial dynamics.Biochemical Society transactions · 2024Review
- Unique Interactions of the Small Translocases of the Mitochondrial Inner Membrane (Tims) inInternational journal of molecular sciences · 2024Article
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- Redox characterisation of Erv1, a key component for protein import and folding in yeast mitochondria.The FEBS journal · 2020Article
- Kinetic characterisation of Erv1, a key component for protein import and folding in yeast mitochondria.The FEBS journal · 2020Article
- Santacruzamate A Ameliorates AD-Like Pathology by Enhancing ER Stress Tolerance Through Regulating the Functions of KDELR and Mia40-ALRFrontiers in cellular neuroscience · 2019Article
- Oxeiptosis, a ROS-induced caspase-independent apoptosis-like cell-death pathway.Nature immunology · 2018Article
- The divergent N-terminal domain of Tim17 is critical for its assembly in the TIM complex in Trypanosoma brucei.Molecular and biochemical parasitology · 2017Article
- Identification of a Degradation Signal Sequence within Substrates of the Mitochondrial i-AAA Protease.Journal of molecular biology · 2017Article
- Labile Low-Molecular-Mass Metal Complexes in Mitochondria: Trials and Tribulations of a Burgeoning Field.Biochemistry · 2016Review
- Mitochondrial Tim9 protects Tim10 from degradation by the protease Yme1.Bioscience reports · 2015Article
- Dimeric Structure of the Bacterial Extracellular Foldase PrsA.The Journal of biological chemistry · 2015Article
- Mitochondrial thiol oxidase Erv1: both shuttle cysteine residues are required for its function with distinct roles.The Biochemical journal · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Correct and timely folding is critical to the function of all proteins. The importance of this is illustrated in the biogenesis of the mitochondrial intermembrane space (IMS) "small Tim" proteins. Biogenesis of the small Tim proteins is regulated by dedicated systems or pathways, beginning with synthesis in the cytosol and ending with assembly of individually folded proteins into functional complexes in the mitochondrial IMS. The process is mostly centered on regulating the redox states of the conserved cysteine residues: oxidative folding is crucial for protein function in the IMS, but oxidized (disulfide bonded) proteins cannot be imported into mitochondria. How the redox-sensitive small Tim precursor proteins are maintained in a reduced, import-competent form in the cytosol is not well understood. Recent studies suggest that zinc and the cytosolic thioredoxin system play a role in the biogenesis of these proteins. In the IMS, the mitochondrial import and assembly (MIA) pathway catalyzes both import into the IMS and oxidative folding of the small Tim proteins. Finally, assembly of the small Tim complexes is a multistep process driven by electrostatic and hydrophobic interactions; however, the chaperone function of the complex might require destabilization of these interactions to accommodate the substrate. Here, we review how folding of the small Tim proteins is regulated during their biogenesis, from maintenance of the unfolded precursors in the cytosol, to their import, oxidative folding, complex assembly and function in the IMS.
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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.