Evidence map›Paper›PMID 9602534›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences1998

The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease.

T Hunter

Open access · greenAbstract readHistorical ArticleLectureReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

103 citing papers in PubMed, 408 citations in OpenAlex.

  1. Unsaturated Phosphorus Electrophiles to Probe Protein Tyrosine Phosphatases.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. The molecular biology of NF2/Merlin on tumorigenesis and development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Review
  9. Review
  10. Advancements in tyrosine kinase-mediated regulation of innate nucleic acid sensing.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2024
    Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

43 more citing papers are in PubMed but not listed here.

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.

T HunterMolecular Biology and Virology Laboratory, Salk Institute, La Jolla, CA 92037, USA.
Salk Institute for Biological Studies · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The reversible phosphorylation of tyrosines in proteins plays a key role in regulating many different processes in eukaryotic organisms, such as growth control, cell cycle control, differentiation cell shape and movement, gene transcription, synaptic transmission, and insulin action. Phosphorylation of proteins is brought about by enzymes called protein-tyrosine kinases that add phosphate to specific tyrosines in target proteins; phosphate is removed from phosphorylated tyrosines by enzymes called protein-tyrosine phosphatases. Phosphorylated tyrosines are recognized by specialized binding domains on other proteins, and such interactions are used to initiate intracellular signaling pathways. Currently, more than 95 protein-tyrosine kinases and more than 55 protein-tyrosine phosphatase genes are known in Homo sapiens. Aberrant tyrosine phosphorylation is a hallmark of many types of cancer and other human diseases. Drugs are being developed that antagonize the responsible protein-tyrosine kinases and phosphatases in order to combat these diseases.

Indexed as

AnimalsCell DivisionDiseaseDrug DesignEnzyme InhibitorsHistory, 20th CenturyHumansMutationPhosphorylationProteinsProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesReceptor Protein-Tyrosine KinasesResearchSignal TransductionTyrosineEnzyme InhibitorsProteinsProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesReceptor Protein-Tyrosine KinasesTyrosine

Identifiers

PMID9602534
PMCPMC1692245
OpenAlexW2097558464

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.