Evidence map›Paper›PMID 23860656›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2013

Protein tyrosine phosphatases: structure, function, and implication in human disease.

Lutz Tautz, David A Critton, Stefan Grotegut

Open access · greenAbstract readReview
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
15.1field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Phosphatase Signaling as a Therapeutic Strategy in Schizophrenia.International journal of molecular sciences · 2026
    Review
  7. Unsaturated Phosphorus Electrophiles to Probe Protein Tyrosine Phosphatases.Angewandte Chemie (International ed. in English) · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

41 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

3 authors at 2 institutions in 1 country.

Lutz TautzInfectious and Inflammatory Disease Center, Sanford-Burnham Medical Research Institute, La Jolla, CA, USA.
David A Critton
Stefan Grotegut
Sanford Burnham Prebys Medical Discovery Institute · USBristol-Myers Squibb (United States) · US

Funding

Novel Delivery Technology for Potential Drugs for Cervical CancerR21CA132121 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2008 to 2009
$473k
STEP inhibitors for intervention in Alzheimer's DiseaseR03MH095532 · NIMH · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2011 to 2012
$97k
Small-Molecule Inhibitors of Vaccinia-H1-Related Phosphatase VHRR03MH084230 · NIMH · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI TAUTZ, LUTZ · 2008 to 2008
$25k
NCI NIH HHS R21 CA132121NCI NIH HHS R21CA132121NIMH NIH HHS R03 MH084230NIMH NIH HHS R03MH084230NIMH NIH HHS R03 MH095532NIMH NIH HHS R03MH095532
6 · The paper itself

Abstract

Protein tyrosine phosphorylation is a key regulatory mechanism in eukaryotic cell physiology. Aberrant expression or function of protein tyrosine kinases and protein tyrosine phosphatases can lead to serious human diseases, including cancer, diabetes, as well as cardiovascular, infectious, autoimmune, and neuropsychiatric disorders. Here, we give an overview of the protein tyrosine phosphatase superfamily with its over 100 members in humans. We review their structure, function, and implications in human diseases, and discuss their potential as novel drug targets, as well as current challenges and possible solutions to developing therapeutics based on these enzymes.

Indexed as

Drug DesignCatalysisCatalytic DomainCrystallography, X-RayHumansNeoplasmsPhosphorylationProtein Tyrosine PhosphatasesSubstrate SpecificityTyrosineProtein Tyrosine PhosphatasesTyrosine

Identifiers

PMID23860656
PMCPMC8158066
OpenAlexW125787089

What OpenQuestion holds

Textmetadata
LicenceTDM
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.