Evidence map›Paper›PMID 26481499›Full record

ReviewTrends in biochemical sciences2015

Dynamics-Driven Allostery in Protein Kinases.

Alexandr P Kornev, Susan S Taylor

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing 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

145 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Local and distal changes in dynamics are caused by an L205R Cushing's syndrome mutant in PRKACA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

85 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

2 authors.

Alexandr P KornevDepartment of Pharmacology, University of California at San Diego, La Jolla, CA, 92093, USA. Electronic address: akornev@ucsd.edu.
Susan S TaylorDepartment of Pharmacology, University of California at San Diego, La Jolla, CA, 92093, USA; Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, CA, 92093, USA. Electronic address: staylor@ucsd.edu.

Funding

Mapping Allosteric Cooperativity in Protein KinasesR01GM100310 · NIGMS · UNIVERSITY OF MINNESOTA · PI VEGLIA, GIANLUIGI · 2012 to 2019
$4.3M
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
Howard Hughes Medical InstituteNIGMS NIH HHS GM100310NIGMS NIH HHS GM19301NIGMS NIH HHS R01 GM019301NIGMS NIH HHS R01 GM100310NIGMS NIH HHS R37 GM019301
6 · The paper itself

Abstract

Protein kinases have very dynamic structures and their functionality strongly depends on their dynamic state. Active kinases reveal a dynamic pattern with residues clustering into semirigid communities that move in μs-ms timescale. Previously detected hydrophobic spines serve as connectors between communities. Communities do not follow the traditional subdomain structure of the kinase core or its secondary structure elements. Instead they are organized around main functional units. Integration of the communities depends on the assembly of the hydrophobic spine and phosphorylation of the activation loop. Single mutations can significantly disrupt the dynamic infrastructure and thereby interfere with long-distance allosteric signaling that propagates throughout the whole molecule. Dynamics is proposed to be the underlying mechanism for allosteric regulation in protein kinases.

Indexed as

Allosteric RegulationHydrophobic and Hydrophilic InteractionsPhosphorylationProtein KinasesProtein Kinasesallosterycommunity analysisprotein dynamicsprotein kinases

Identifiers

PMID26481499
PMCPMC4630092

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.