Evidence map›Paper›PMID 33661624›Full record

ArticleJournal of the American Chemical Society2021

Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases.

Rory M Crean, Michal Biler, Marc W van der Kamp, Alvan C Hengge, Shina C L Kamerlin

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

46 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.Protein science : a publication of the Protein Society · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 3 countries.

Rory M CreanScience for Life Laboratory, Department of Chemistry - BMC, Uppsala University, Box 576, S-751 23 Uppsala, Sweden.
Michal BilerScience for Life Laboratory, Department of Chemistry - BMC, Uppsala University, Box 576, S-751 23 Uppsala, Sweden.
Marc W van der KampSchool of Biochemistry, University of Bristol, Biomedical Sciences Building, University Walk, Bristol BS8 1TD, United Kingdom.ORCID 0000-0002-8060-3359
Alvan C HenggeDepartment of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322-0300, United States.ORCID 0000-0002-5696-2087
Shina C L KamerlinScience for Life Laboratory, Department of Chemistry - BMC, Uppsala University, Box 576, S-751 23 Uppsala, Sweden.ORCID 0000-0002-3190-1173
Uppsala University · SEUniversity of Bristol · GBUtah State University · US

Funding

Biotechnology and Biological Sciences Research Council BB/M026280/1
6 · The paper itself

Abstract

Protein tyrosine phosphatases (PTPs) play an important role in cellular signaling and have been implicated in human cancers, diabetes, and obesity. Despite shared catalytic mechanisms and transition states for the chemical steps of catalysis, catalytic rates within the PTP family vary over several orders of magnitude. These rate differences have been implied to arise from differing conformational dynamics of the closure of a protein loop, the WPD-loop, which carries a catalytically critical residue. The present work reports computational studies of the human protein tyrosine phosphatase 1B (PTP1B) and YopH from

Indexed as

Allosteric RegulationBiocatalysisCatalytic DomainHumansKineticsMolecular Dynamics SimulationProtein StabilityProtein Structure, TertiaryProtein Tyrosine Phosphatase, Non-Receptor Type 1ThermodynamicsProtein Tyrosine Phosphatase, Non-Receptor Type 1PTPN1 protein, human

Identifiers

PMID33661624
PMCPMC8031367
OpenAlexW3111877653

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.