Evidence map›Paper›PMID 36834832›Full record

ReviewInternational journal of molecular sciences2023

Structure, Substrate Specificity and Role of Lon Protease in Bacterial Pathogenesis and Survival.

Perumalraja Kirthika, Khristine Kaith Sison Lloren, Vijayakumar Jawalagatti, John Hwa Lee

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Involvement ofApplied and environmental microbiology · 2026
    Article
  7. Article
  8. Lon protease reprograms cellular physiology ofFrontiers in microbiology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The protein degradation system encoded byInfection and immunity · 2025
    Article
  14. Article
  15. microLife · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

4 authors at 2 institutions in 2 countries.

Perumalraja KirthikaDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55902, USA.
Khristine Kaith Sison LlorenCollege of Veterinary Medicine, Jeonbuk National University, Iksan 54596, Republic of Korea.ORCID 0000-0002-9858-9452
Vijayakumar JawalagattiDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55902, USA.
John Hwa LeeCollege of Veterinary Medicine, Jeonbuk National University, Iksan 54596, Republic of Korea.
Jeonbuk National University · KRMayo Clinic · US

Funding

National Research Foundation of Korea 2019R1A6A1A03033084
6 · The paper itself

Abstract

Proteases are the group of enzymes that carry out proteolysis in all forms of life and play an essential role in cell survival. By acting on specific functional proteins, proteases affect the transcriptional and post-translational pathways in a cell. Lon, FtsH, HslVU and the Clp family are among the ATP-dependent proteases responsible for intracellular proteolysis in bacteria. In bacteria, Lon protease acts as a global regulator, governs an array of important functions such as DNA replication and repair, virulence factors, stress response and biofilm formation, among others. Moreover, Lon is involved in the regulation of bacterial metabolism and toxin-antitoxin systems. Hence, understanding the contribution and mechanisms of Lon as a global regulator in bacterial pathogenesis is crucial. In this review, we discuss the structure and substrate specificity of the bacterial Lon protease, as well as its ability to regulate bacterial pathogenesis.

Indexed as

Protease LaATP-Dependent ProteasesBacteriaBacterial ProteinsEndopeptidasesPeptide HydrolasesSubstrate SpecificityATP-Dependent ProteasesBacterial ProteinsEndopeptidasesPeptide HydrolasesProtease LabacteriaLon proteasepathogenesisstress responsevirulence

Identifiers

PMID36834832
PMCPMC9961632
OpenAlexW4319763409

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.