Evidence map›Paper›PMID 8759835›Full record

ReviewJournal of bacteriology1996

Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation.

P J Kennelly, M Potts

Abstract readReview
In one paragraph

Review in Journal of bacteriology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Metabolic Kinases Moonlighting as Protein Kinases.Trends in biochemical sciences · 2018
    Review
  5. Review
  6. Regulation of Escherichia coli RNase III activity.Journal of microbiology (Seoul, Korea) · 2015
    Review
  7. Nucleoside diphosphate kinase as protein histidine kinase.Naunyn-Schmiedeberg's archives of pharmacology · 2015
    Review
  8. Protein Ser/Thr/Tyr phosphorylation in the Archaea.The Journal of biological chemistry · 2014
    Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  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

2 authors.

P J KennellyDepartment of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA. pjkennel@vt.edu
M Potts

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria play host to a wide range of protein phosphorylation-dephosphorylation systems (Fig. 1). As little as five years ago the known systems were thought to be late-emerging and absolutely prokaryote specific. Today we know that most protein kinases and protein phosphatases are descended from a set of common, and possibly quite ancient, prototypes. Prokaryote- and eukaryote-specific protein kinases and protein phosphatases are rare and represent exceptions, not the rule as previously thought. Commonality suggests that a dynamic and versatile regulatory mechanism was first adapted to the modulation of protein function as early if not earlier than more "basic" mechanisms such as allosterism, etc. The existence of common molecular themes confirms that the microbial world offers a unique, largely untapped library and a powerful set of tools for the understanding of a regulatory mechanism which is crucial to all organisms, tools whose diversity and experimental malleability will provide new avenues for exploring and understanding key modes of cellular regulation.

Indexed as

AnimalsBacteriaBacterial ProteinsCyanobacteriaHistidine KinaseModels, BiologicalPhosphoprotein PhosphatasesPhosphorylationPhylogenyProkaryotic CellsProtein KinasesBacterial ProteinsHistidine KinasePhosphoprotein PhosphatasesProtein Kinases

Identifiers

PMID8759835
PMCPMC178254

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.