ArticleThe EMBO journal1997
Active unfolding of precursor proteins during mitochondrial protein import.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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
53 citing papers in PubMed, 159 citations in OpenAlex.
- Elevated mitochondrial protein import in acute myeloid leukemia increases reliance on mitochondrial protease LONP1.The Journal of clinical investigation · 2026Article
- A protein-specific priority code in presequences determines the efficiency of mitochondrial protein import.PLoS biology · 2025Article
- Structural determinants of mitochondrial STAT3 targeting and function.Mitochondrial communications · 2024Article
- Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes.eLife · 2022Article
- Role of the membrane potential in mitochondrial protein unfolding and import.Scientific reports · 2019Article
- Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Hsp70 chaperones use ATP to remodel native protein oligomers and stable aggregates by entropic pulling.Nature structural & molecular biology · 2016Article
- Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore.ACS nano · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation stabilizes ISCU protein: implications for iron metabolism.The Journal of biological chemistry · 2013Article
- Spatial association with PTEX complexes defines regions for effector export into Plasmodium falciparum-infected erythrocytes.Nature communications · 2013Article
- Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I.BioMed research international · 2013Review
- Evidence of evolutionary constraints that influences the sequence composition and diversity of mitochondrial matrix targeting signals.PloS one · 2013Article
- A model system for mitochondrial biogenesis reveals evolutionary rewiring of protein import and membrane assembly pathways.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The molten globule state is unusually deformable under mechanical force.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Protein sensing with engineered protein nanopores.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Charge requirements for proton gradient-driven translocation of anthrax toxin.The Journal of biological chemistry · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Precursor proteins made in the cytoplasm must be in an unfolded conformation during import into mitochondria. Some precursor proteins have tightly folded domains but are imported faster than they unfold spontaneously, implying that mitochondria can unfold proteins. We measured the import rates of artificial precursors containing presequences of varying length fused to either mouse dihydrofolate reductase or bacterial barnase, and found that unfolding of a precursor at the mitochondrial surface is dramatically accelerated when its presequence is long enough to span both membranes and to interact with mhsp70 in the mitochondrial matrix. If the presequence is too short, import is slow but can be strongly accelerated by urea-induced unfolding, suggesting that import of these 'short' precursors is limited by spontaneous unfolding at the mitochondrial surface. With precursors that have sufficiently long presequences, unfolding by the inner membrane import machinery can be orders of magnitude faster than spontaneous unfolding, suggesting that mhsp70 can act as an ATP-driven force-generating motor during protein import.
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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.