Evidence map›Paper›PMID 7659757›Full record

ArticlePlant physiology1995

The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity.

Y T Loh, G B Martin

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Plant physiology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

22 citing papers in PubMed, 95 citations in OpenAlex.

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  14. AvrPto-dependent Pto-interacting proteins and AvrPto-interacting proteins in tomato.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Genetically engineered broad-spectrum disease resistance in tomato.Proceedings of the National Academy of Sciences of the United States of America · 1998
    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 at 1 institution in 1 country.

Y T LohDepartment of Agronomy, Purdue University, West Lafayette, Indiana 47907-1150, USA.
G B Martin
Purdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The catalytic activity and amino acid specificity of the tomato Pto and Fen kinases were investigated. The Pto and Fen genes were fused to the carboxyl terminus of the maltose-binding protein and expressed in Escherichia coli. Incubation of the purified fusion proteins with [gamma-32P]ATP in an in vitro assay showed that both proteins were capable of autophosphorylation. Mutant fusion proteins in which the conserved lysine residue of subdomain II was changed to a glutamine were unable to autophosphorylate. Phosphoamino analysis of the active fusion proteins indicated that both kinases phosphorylate serine and threonine residues but not tyrosine.

Indexed as

Amino AcidsAmino Acid SequenceBase SequenceConserved SequenceFenthionGenes, PlantImmunity, InnateMolecular Sequence DataPhosphorylationPlant DiseasesPlant ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSequence Homology, Amino AcidSolanum lycopersicumAmino AcidsFen protein, Lycopersicon esculentumFenthionPlant ProteinsProtein Serine-Threonine KinasesPto protein, LycopersiconRecombinant Fusion Proteins

Identifiers

PMID7659757
PMCPMC157555
OpenAlexW1968295940

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.