Evidence map›Paper›PMID 11489874›Full record

ArticleJournal of bacteriology2001

Regulation and mechanism of action of the small heat shock protein from the hyperthermophilic archaeon Pyrococcus furiosus.

P Laksanalamai, D L Maeder, F T Robb

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Archaeal-like chaperonins in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  9. Article
  10. Article
  11. Transposon insertion reveals pRM, a plasmid of Rickettsia monacensis.Applied and environmental microbiology · 2007
    Article
  12. Article
  13. Article
  14. Small heat shock proteins from extremophiles: a review.Extremophiles : life under extreme conditions · 2004
    Review
  15. Article
  16. 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

3 authors at 1 institution in 1 country.

P LaksanalamaiCenter of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, Maryland 21202, USA.
D L Maeder
F T Robb
Biotechnology Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small heat shock protein (sHSP) from the hyperthermophile Pyrococcus furiosus was specifically induced at the level of transcription by heat shock at 105 degrees C. The gene encoding this protein was cloned and overexpressed in Escherichia coli. The recombinant sHSP prevented the majority of E. coli proteins from aggregating in vitro for up to 40 min at 105 degrees C. The sHSP also prevented bovine glutamate dehydrogenase from aggregating at 56 degrees C. Survivability of E. coli overexpressing the sHSP was enhanced approximately sixfold during exposure to 50 degrees C for 2 h compared with the control culture, which did not express the sHSP. Apparently, the sHSP confers a survival advantage on mesophilic bacteria by preventing protein aggregation at supraoptimal temperatures.

Indexed as

AnimalsCattleCloning, MolecularEscherichia coliGlutamate DehydrogenaseHeat-Shock ProteinsHot TemperatureMolecular Sequence DataPyrococcus furiosusGlutamate DehydrogenaseHeat-Shock Proteinssmall heat shock protein, Pyrococcus furiosus

Identifiers

PMID11489874
PMCPMC95397
OpenAlexW2106630675

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.