Evidence map›Paper›PMID 31063633›Full record

ReviewIUBMB life2019

Tuning the "violin" of protein kinases: The role of dynamics-based allostery.

Lalima G Ahuja, Susan S Taylor, Alexandr P Kornev

Abstract readReview
In one paragraph

Review in IUBMB life, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Allostery in Protein Tyrosine Phosphatases is Enabled by Divergent Dynamics.Journal of chemical information and modeling · 2024
    Article
  13. Protein Kinase Structure and Dynamics: Role of the αC-β4 Loop.bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. The discovery of hidden guanylate cyclases (GCs) in theComputational and structural biotechnology journal · 2023
    Article
  19. Characterisation of sequence-structure-function space in sensor-effector integrators of phytochrome-regulated diguanylate cyclases.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    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

3 authors.

Lalima G AhujaDepartment of Pharmacology, University of California San Diego, La Jolla, CA, USA.ORCID 0000-0002-3839-4936
Susan S TaylorDepartment of Pharmacology, University of California San Diego, La Jolla, CA, USA.
Alexandr P KornevDepartment of Pharmacology, University of California San Diego, La Jolla, CA, USA.ORCID 0000-0002-1543-3795

Funding

Protein Kinase Regulatory Subunit I Directed MutagenesisR01GM034921 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2018
$7.2M
Lessons Learned from PKA: Assembly of Dynamic Macromolecular SwitchesR35GM130389 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SUSAN S. TAYLOR · 2019 to 2026
$5.7M
Protein Kinase: Primary Structure and cAMP InteractionsR01GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2013
$3.4M
PROTEIN KINASE: PRIMARY STRUCTURE AND CAMP INTERACTIONR37GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI TAYLOR, SUSAN S · 1995 to 2004
$2.0M
NIGMS NIH HHS R01 GM019301NIGMS NIH HHS R01 GM034921NIGMS NIH HHS R35 GM130389NIGMS NIH HHS R37 GM019301
6 · The paper itself

Abstract

The intricacies of allosteric regulation of protein kinases continue to engage the research community. Allostery, or control from a distance, is seen as a fundamental biomolecular mechanism for proteins. From the traditional methods of conformational selection and induced fit, the field has grown to include the role of protein motions in defining a dynamics-based allosteric approach. Harnessing of these continuous motions in the protein to exert allosteric effects can be defined by a "violin" model that focuses on distributions of protein vibrations as opposed to concerted pathways. According to this model, binding of an allosteric modifier causes global redistribution of dynamics in the protein kinase domain that leads to changes in its catalytic properties. This model is consistent with the "entropy-driven allostery" mechanism proposed by Cooper and Dryden in 1984 and does not require, but does not exclude, any major structural changes. We provide an overview of practical implementation of the violin model and how it stands amidst the other known models of protein allostery. Protein kinases have been described as the biomolecules of interest. © 2019 IUBMB Life, 71(6):685-696, 2019.

Indexed as

Allosteric RegulationBinding SitesEntropyMolecular Dynamics SimulationProtein BindingProtein ConformationProtein KinasesProteinsSignal TransductionProtein KinasesProteinscommunity mapsconformationentropyMD simulationprotein allosteryprotein dynamicsprotein kinases

Identifiers

PMID31063633
PMCPMC6690483

What OpenQuestion holds

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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.