Evidence map›Paper›PMID 24874800›Full record

ArticleBioengineered

Polyphosphate, cyclic AMP, guanosine tetraphosphate, and c-di-GMP reduce in vitro Lon activity.

Devon O Osbourne, Valerie W C Soo, Igor Konieczny, Thomas K Wood

Open access · goldAbstract read
In one paragraph

Article in Bioengineered. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. mBio · 2022
    Article
  7. Review
  8. Review
  9. Article
  10. (p)ppGpp and Its Role in Bacterial Persistence: New Challenges.Antimicrobial agents and chemotherapy · 2020
    Review
  11. Article
  12. Review
  13. Iron Limitation inFrontiers in microbiology · 2020
    Article
  14. Article
  15. Review
  16. Power-law tail in lag time distribution underlies bacterial persistence.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Ribosome dependence of persister cell formation and resuscitation.Journal of microbiology (Seoul, Korea) · 2019
    Review
  18. Article
  19. Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018
    Review
  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 3 institutions in 2 countries.

Devon O OsbourneDepartment of Chemical Engineering; Pennsylvania State University; University Park, PA USA.
Valerie W C SooDepartment of Chemical Engineering; Pennsylvania State University; University Park, PA USA.
Igor KoniecznyDepartment of Molecular and Cellular Biology; Intercollegiate Faculty of Biotechnology; University of Gdansk; Gdansk, Poland.
Thomas K WoodDepartment of Chemical Engineering; Pennsylvania State University; University Park, PA USA; Department of Biochemistry and Molecular Biology; Pennsylvania State University; University Park, PA USA.
Pennsylvania State University · USPark University · USUniversity of Gdańsk · PL

Funding

Re-Wiring Cellular Metabolism to Control Biofilm Formation and Virulence BY...R01GM089999 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI WOOD, THOMAS K · 2009 to 2011
$846k
NIGMS NIH HHS R01 GM089999
6 · The paper itself

Abstract

Lon protease is conserved from bacteria to humans and regulates cellular processes by degrading different classes of proteins including antitoxins, transcriptional activators, unfolded proteins, and free ribosomal proteins. Since we found that Lon has several putative cyclic diguanylate (c-di-GMP) binding sites and since Lon binds polyphosphate (polyP) and lipid polysaccharide, we hypothesized that Lon has an affinity for phosphate-based molecules that might regulate its activity. Hence we tested the effect of polyP, cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), guanosine tetraphosphate (ppGpp), c-di-GMP, and GMP on the ability of Lon to degrade α-casein. Inhibition of in vitro Lon activity occurred for polyP, cAMP, ppGpp, and c-di-GMP. We also demonstrated by HPLC that Lon is able to bind c-di-GMP. Therefore, four cell signals were found to regulate the activity of Lon protease.

Indexed as

Amino Acid SequenceBinding SitesCaseinsCyclic AMPCyclic GMPEscherichia coliEscherichia coli ProteinsGuanosine TetraphosphateMolecular Sequence DataPolyphosphatesProtease LaProteolysisbis(3',5')-cyclic diguanylic acidCaseinsCyclic AMPCyclic GMPEscherichia coli ProteinsGuanosine TetraphosphatePolyphosphatesProtease LacAMPc-di-GMPLon proteasepolyphosphateppGpp

Identifiers

PMID24874800
PMCPMC4143397
OpenAlexW2093570970

What OpenQuestion holds

Textmetadata
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.