Evidence map›Paper›PMID 9246757›Full record

ReviewFolia microbiologica1997

Diversity and specificity of protein-phosphorylating systems in bacteria.

A J Cozzone

Abstract readReview
PubMed Publisher
In one paragraph

Review in Folia microbiologica, 1997. 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
0.6field-weighted citation impact, top 34% 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

5 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Bacterial tyrosine kinases: evolution, biological function and structural insights.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  3. Article
  4. Review
  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

1 author at 1 institution in 1 country.

A J CozzoneInstitut de Biologie et Chimie des Protéines, CNRS, Lyon, France.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria harbor three different protein-phosphorylating systems which regulate distinct physiological processes: first, the nucleotide-dependent system which modifies hydroxyl groups of amino acids in protein substrates; second, the two-component system which involves both sensor kinase and response regulator; third, the phosphoenolpyruvate-dependent phosphotransferase system. These systems share a number of structural and functional similarities with the protein-phosphorylating systems of eukaryotes.

Indexed as

Adaptation, BiologicalBacteriaBacterial ProteinsEukaryotic CellsPhosphoenolpyruvate Sugar Phosphotransferase SystemPhosphorylationProkaryotic CellsProtein KinasesProtein-Tyrosine KinasesSignal TransductionBacterial ProteinsPhosphoenolpyruvate Sugar Phosphotransferase SystemProtein KinasesProtein-Tyrosine Kinases

Identifiers

PMID9246757
OpenAlexW2018463246

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.