ArticleLife science alliance2020
MIC26 and MIC27 cooperate to regulate cardiolipin levels and the landscape of OXPHOS complexes.
Article in Life science alliance, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- Pathogenic variants of the mitochondrial copper chaperones SCO1 and SCO2 reshape their respective interactomes and disrupt cellular phospholipid metabolism.bioRxiv : the preprint server for biology · 2026Article
- The molecular basis of mitochondrial crista formation by the MIC10 complex.Science advances · 2026Article
- Integrative structure determination of a human mitochondrial contact site and cristae organizing system (MICOS) sub-assembly.bioRxiv : the preprint server for biology · 2026Article
- Compositional recalibrations of cardiolipin integrate loss of stearoyl-CoA desaturase 1 activity with mitochondrial decay in lipid-laden pancreatic β-cells.Cell communication and signaling : CCS · 2026Article
- MICOS and MIMAS, multifunctional assemblies linking mitochondrial biogenesis, architecture, and function.Protein science : a publication of the Protein Society · 2026Review
- Global mitochondrial connectivity map reveals the landscape of yeast functional assemblies and conserved protein communities.Nature communications · 2026Article
- Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025Review
- Structures and functions of the MICOS: Pathogenesis and therapeutic implications in Alzheimer's disease.Acta pharmaceutica Sinica. B · 2025Review
- A New Perspective on the Role of Alterations in Mitochondrial Proteins Involved in ATP Synthesis and Mobilization in Cardiomyopathies.International journal of molecular sciences · 2025Review
- SLP2 and MIC13 synergistically coordinate MICOS assembly and crista junction formation.iScience · 2024Article
- Mitochondrial apolipoprotein MIC26 is a metabolic rheostat regulating central cellular fuel pathways.Life science alliance · 2024Article
- Mitochondrial Structure and Function in Human Heart Failure.Circulation research · 2024Review
- A dynamin superfamily-like pseudoenzyme coordinates with MICOS to promote cristae architecture.Current biology : CB · 2024Article
- Review
- Mic19 depletion impairs endoplasmic reticulum-mitochondrial contacts and mitochondrial lipid metabolism and triggers liver disease.Nature communications · 2024Article
- Article
- Navigating the landscape of mitochondrial-ER communication in health and disease.Frontiers in molecular biosciences · 2024Review
- A DRP-like pseudoenzyme coordinates with MICOS to promote cristae architecture.bioRxiv : the preprint server for biology · 2023Article
- Mitochondrial Cristae Morphology Reflecting Metabolism, Superoxide Formation, Redox Homeostasis, and Pathology.Antioxidants & redox signaling · 2023Review
- Unraveling the mechanisms of cardiolipin function: The role of oxidative polymerization of unsaturated acyl chains.Redox biology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homologous apolipoproteins of MICOS complex, MIC26 and MIC27, show an antagonistic regulation of their protein levels, making it difficult to deduce their individual functions using a single gene deletion. We obtained single and double knockout (DKO) human cells of
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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.