ReviewBiochimica et biophysica acta2008
Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates.
Review in Biochimica et biophysica acta, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
60 citing papers in PubMed, 117 citations in OpenAlex.
- Functional FTSH4 complexes in Arabidopsis mitochondria: a megacomplex with SLP1 and SLP1-free smaller complexes.Plant & cell physiology · 2026Article
- Differential contributions of ClpX and ClpP to pulmonary virulence in classical and hypervirulentInfection and immunity · 2026Article
- Comparative genomics of an Antarctic sea-ice diatom (Frontiers in microbiology · 2026Article
- Lon protease reprograms cellular physiology ofFrontiers in microbiology · 2026Article
- Comparative transcriptomic analysis of perfluoroalkyl substances-induced responses of exponential and stationary phase Escherichia coli.BMC genomics · 2025Article
- Substrate-dependent activation of LONP1 informs on proteolytic regulation and ATPase motor function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The ClpA chaperone and the two adaptor proteins modulate the fate of the model substrate tagged with a SsrA-degron of Leptospira.The Biochemical journal · 2025Article
- Mitochondrial proteases and their roles in mitophagy in plants, animals, and yeast.Plant & cell physiology · 2025Review
- Multitarget mechanism of MYC inhibition by the bacterial lon protease in disease.Scientific reports · 2025Article
- Cellular senescence as a source of chronic microinflammation that promotes the aging process.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025Review
- Global impacts of peroxisome and pexophagy dysfunction revealed through multi-omics analyses of lon2 and atg2 mutants.The Plant journal : for cell and molecular biology · 2024Article
- Allosteric modulation of the Lon protease by effector binding and local charges.bioRxiv : the preprint server for biology · 2024Article
- Proteolytic control of FixT by the Lon protease impacts FixLJ signaling inJournal of bacteriology · 2024Article
- Structural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Mitochondrial metabolism regulation and epigenetics in hypoxia.Frontiers in physiology · 2024Review
- Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.International journal of molecular sciences · 2023Review
- Article
- The diverse arsenal of type III CRISPR-Cas-associated CARF and SAVED effectors.Biochemical Society transactions · 2022Review
- ATP hydrolysis tunes specificity of a AAA+ protease.Cell reports · 2022Article
- Plant peroxisome proteostasis-establishing, renovating, and dismantling the peroxisomal proteome.Essays in biochemistry · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Lon, also known as the protease La, is a homo-oligomeric ATP-dependent protease, which is highly conserved in archaea, eubacteria and eukaryotic mitochondria and peroxisomes. Since its discovery, studies have shown that Lon activity is essential for cellular homeostasis, mediating protein quality control and metabolic regulation. This article highlights the discoveries made over the past decade demonstrating that Lon selectively degrades abnormal as well as certain regulatory proteins and thus plays significant roles in maintaining bacterial and mitochondrial function and integrity. In addition, Lon is required in certain pathogenic bacteria, for rendering pathogenicity and host infectivity. Recent research endeavors have been directed toward elucidating the reaction mechanism of the Lon protease by different biochemical and structural biological techniques. In this mini-review, the authors survey the diverse biological roles of Lon, and also place special emphasis on recent findings that clarify the mechanistic aspects of the Lon reaction cycle.
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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.