Evidence map›Paper›PMID 32034150›Full record

ArticleNature communications2020

Minimally disruptive optical control of protein tyrosine phosphatase 1B.

Akarawin Hongdusit, Peter H Zwart, Banumathi Sankaran, Jerome M Fox

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Allosteric regulation of the tyrosine phosphatase PTP1B by a protein-protein interaction.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Analysis of neutral mutational drift in an allosteric enzyme.Protein science : a publication of the Protein Society · 2023
    Article
  10. Article
  11. Allosteric Inhibition of PTP1B by a Nonpolar Terpenoid.The journal of physical chemistry. B · 2022
    Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Engineering an Allosteric Control of Protein Function.The journal of physical chemistry. B · 2021
    Review
  20. Review
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

4 authors at 2 institutions in 1 country.

Akarawin HongdusitDepartment of Chemical and Biological Engineering, University of Colorado - Boulder, 3415 Colorado Avenue, Boulder, CO, 80303, USA.
Peter H ZwartMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA, 94720, USA.
Banumathi SankaranMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA, 94720, USA.
Jerome M FoxDepartment of Chemical and Biological Engineering, University of Colorado - Boulder, 3415 Colorado Avenue, Boulder, CO, 80303, USA. jerome.fox@colorado.edu.ORCID http://orcid.org/0000-0002-3739-1899
Lawrence Berkeley National Laboratory · USUniversity of Colorado Boulder · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
NIGMS NIH HHS P30 GM124169
6 · The paper itself

Abstract

Protein tyrosine phosphatases regulate a myriad of essential subcellular signaling events, yet they remain difficult to study in their native biophysical context. Here we develop a minimally disruptive optical approach to control protein tyrosine phosphatase 1B (PTP1B)-an important regulator of receptor tyrosine kinases and a therapeutic target for the treatment of diabetes, obesity, and cancer-and we use that approach to probe the intracellular function of this enzyme. Our conservative architecture for photocontrol, which consists of a protein-based light switch fused to an allosteric regulatory element, preserves the native structure, activity, and subcellular localization of PTP1B, affords changes in activity that match those elicited by post-translational modifications inside the cell, and permits experimental analyses of the molecular basis of optical modulation. Findings indicate, most strikingly, that small changes in the activity of PTP1B can cause large shifts in the phosphorylation states of its regulatory targets.

Indexed as

Allosteric RegulationAnimalsBiosensing TechniquesChlorocebus aethiopsCOS CellsCrystallography, X-RayFluorescence Resonance Energy TransferHEK293 CellsHumansOptogeneticsPhosphorylationPhototropinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Receptor, InsulinRecombinant ProteinsPhototropinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Receptor, InsulinRecombinant Proteins

Identifiers

PMID32034150
PMCPMC7005756
OpenAlexW3004946484

What OpenQuestion holds

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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.