Evidence map›Paper›PMID 11717299›Full record

ArticleJournal of bacteriology2001

Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus.

M J Eriksson, J Schelin, E Miskiewicz, A K Clarke

Abstract 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 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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.

M J ErikssonUmeå Plant Science Centre, Department of Plant Physiology, Umeå University, S-901 87 Umeå, Sweden.
J Schelin
E Miskiewicz
A K Clarke

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synechococcus sp. strain PCC 7942 has a second clpB gene that encodes a 97-kDa protein with novel features. ClpBII is the first ClpB not induced by heat shock or other stresses; it is instead an essential, constitutive protein. ClpBII is unable to complement ClpBI function for acquired thermotolerance. No truncated ClpBII version is normally produced, unlike other bacterial forms, while ectopic synthesis of a putative truncated ClpBII dramatically decreased cell viability.

Indexed as

Adaptation, BiologicalBacterial ProteinsCloning, MolecularCyanobacteriaEndopeptidase ClpGene Expression Regulation, BacterialGenes, BacterialGenes, EssentialHeat-Shock ProteinsHeat-Shock ResponsePeptide FragmentsSequence Analysis, DNABacterial ProteinsClpBII protein, Synechococcus sp.ClpB protein, SynechococcusEndopeptidase ClpHeat-Shock ProteinsPeptide Fragments

Identifiers

PMID11717299
PMCPMC95589

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.