Evidence map›Paper›PMID 22119779›Full record

ReviewBiochimica et biophysica acta2012

Multitasking in the mitochondrion by the ATP-dependent Lon protease.

Sundararajan Venkatesh, Jae Lee, Kamalendra Singh, Irene Lee, Carolyn K Suzuki

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
5.7field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

89 citing papers in PubMed, 165 citations in OpenAlex.

  1. Article
  2. Review
  3. Beyond the genome: clinical challenges in diagnosingFrontiers in cell and developmental biology · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. AMPK Suppression Due to Obesity Drives Oocyte mtDNA Heteroplasmy via ATF5-POLG Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Pharmacological Progress of Mitophagy Regulation.Current neuropharmacology · 2023
    Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

29 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Sundararajan VenkateshDepartment of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, 185 South Orange Avenue, MSB E-633, Newark, New Jersey 07103 USA.
Jae Lee
Kamalendra Singh
Irene Lee
Carolyn K Suzuki
Rutgers, The State University of New Jersey · USCase Western Reserve University · USUniversity of Missouri · US

Funding

STRUCTURE AND FUNCTION OF THE MITOCHONDRIAL LON PROTEASER01GM061095 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI SUZUKI, CAROLYN K · 2000 to 2004
$1.3M
High throughput screens for modulators of mitochondrial ATP-dependent proteolysisR01GM084039 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI SUZUKI, CAROLYN K · 2009 to 2010
$734k
High throughput screening assays to identify small molecules that target the ClpXR21NS067668 · NINDS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI SUZUKI, CAROLYN K · 2010 to 2010
$171k
NIGMS NIH HHS R01 GM061095NIGMS NIH HHS R01 GM084039NIGMS NIH HHS R01GM084039NINDS NIH HHS R21 NS067668NINDS NIH HHS R21NS067668
6 · The paper itself

Abstract

The AAA(+) Lon protease is a soluble single-ringed homo-oligomer, which represents the most streamlined operational unit mediating ATP-dependent proteolysis. Despite its simplicity, the architecture of Lon proteases exhibits a species-specific diversity. Homology modeling provides insights into the structural features that distinguish bacterial and human Lon proteases as hexameric complexes from yeast Lon, which is uniquely heptameric. The best-understood functions of mitochondrial Lon are linked to maintaining proteostasis under normal metabolic conditions, and preventing proteotoxicity during environmental and cellular stress. An intriguing property of human Lon is its specific binding to G-quadruplex DNA, and its association with the mitochondrial genome in cultured cells. A fraction of Lon preferentially binds to the control region of mitochondrial DNA where transcription and replication are initiated. Here, we present an overview of the diverse functions of mitochondrial Lon, as well as speculative perspectives on its role in protein and mtDNA quality control.

Indexed as

AnimalsConserved SequenceDNA-Binding ProteinsDNA, MitochondrialHumansMembrane ProteinsMitochondriaMolecular Sequence DataProtease LaProtein Structure, QuaternaryProtein Structure, TertiaryProteolysisSaccharomyces cerevisiae ProteinsASI1 protein, S cerevisiaeDNA-Binding ProteinsDNA, MitochondrialMembrane ProteinsProtease LaSaccharomyces cerevisiae Proteins

Identifiers

PMID22119779
PMCPMC3263341
OpenAlexW1968698003

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.