Evidence map›Paper›PMID 9685474›Full record

ReviewNucleic acids research1998

Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome.

C C Zhang, L Gonzalez, V Phalip

Open access · bronzeAbstract readComparative StudyReview
In one paragraph

Review in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Article
  3. Revisiting cyanobacterial state transitions.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Eukaryotic-like protein kinases in the prokaryotes and the myxobacterial kinome.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  18. Article
  19. 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.

C C ZhangUnité d'Immunotechnologie et Microbiologie Moléculaires, Ecole Supérieure de Biotechnologie de Strasbourg, Université Louis Pasteur de Strasbourg, Boulevard Sébastien Brandt, F-67400 Illkirch, France. cheng-cai.zhang@esbs.u-strasbg.fr
L Gonzalez
V Phalip
École Supérieure de Biotechnologie de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria usually use two-component systems for signal transduction, while eukaryotic organisms employ Ser/Thr and Tyr kinases and phosphatases for the same purpose. Many prokaryotes turn out to harbor Ser/Thr and Tyr kinases, Ser/Thr and Tyr phosphatases, and their accessory components as well. The sequence determination of the genome of the cyanobacterium Synechocystis sp. strain PCC 6803 offers the possibility to survey the extent of such molecules in a prokaryotic organism. This cyanobacterium possesses seven Ser/Thr kinases, seven Ser/Thr and Tyr phosphatases, one protein kinase interacting protein, one protein kinase regulatory subunit and several WD40-repeat-containing proteins. The majority of the protein phosphatases presented in this study were previously reported as hypothetical proteins. We analyze here the structure and genetic organization of these ORFs in the hope of providing a guidance for their functional analysis. Unlike their eukaryotic counterparts, many of these genes are clustered on the chromosome, and this genetic organization offers the opportunity to study their possible interaction. In several cases, genes of two-component transducers are found within the same cluster as those encoding a Ser/Thr kinase or a Ser/Thr phosphatase; the implication for signal transduction mechanism will be discussed.

Indexed as

Genes, BacterialGenome, BacterialAmino Acid SequenceBacterial ProteinsBase SequenceCyanobacteriaDNA PrimersEukaryotic CellsMolecular Sequence DataMultigene FamilyPhosphoprotein PhosphatasesPolymerase Chain ReactionProkaryotic CellsProtein Serine-Threonine KinasesProtein Sorting SignalsProtein-Tyrosine KinasesBacterial ProteinsDNA PrimersPhosphoprotein PhosphatasesProtein Serine-Threonine KinasesProtein Sorting SignalsProtein-Tyrosine KinasesProtein Tyrosine Phosphatases

Identifiers

PMID9685474
PMCPMC147778
OpenAlexW2133118583

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.