Evidence map›Paper›PMID 30611608›Full record

ReviewTrends in biochemical sciences2019

Disordered Protein Kinase Regions in Regulation of Kinase Domain Cores.

Gergő Gógl, Alexandr P Kornev, Attila Reményi, Susan S Taylor

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

45 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. ERK autoinhibition mechanism informs a drug combination strategy.Protein science : a publication of the Protein Society · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. RiSKs in Computational Modeling of Isoform-Selective RSK Inhibitors.Journal of chemical information and modeling · 2025
    Review
  13. Fuzziness in enzymatic catalysis.Current opinion in structural biology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. A conserved juxtamembrane motif in plant NFR5 receptors is essential for root nodule symbiosis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Exploring the conformational landscape of protein kinases.Current opinion in structural biology · 2024
    Review
  19. 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

4 authors at 2 institutions in 2 countries.

Gergő GóglInstitute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Alexandr P KornevDepartment of Pharmacology, University of California San Diego, 9500 Gilman Drive, La Jolla, San Diego, CA 92093-0654, USA.
Attila ReményiInstitute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary. Electronic address: remenyi.attila@ttk.mta.hu.
Susan S TaylorDepartment of Pharmacology, University of California San Diego, 9500 Gilman Drive, La Jolla, San Diego, CA 92093-0654, USA; Department of Chemistry and Biochemistry, University of California San Diego, 9500 Gilman Drive, La Jolla, San Diego, CA 92093-0654, USA. Electronic address: staylor@ucsd.edu.
Hungarian Academy of Sciences · HUUniversity of California, San Diego · US

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
Lessons Learned from PKA: Assembly of Dynamic Macromolecular SwitchesR35GM130389 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SUSAN S. TAYLOR · 2019 to 2026
$5.7M
NIDDK NIH HHS P01 DK054441NIGMS NIH HHS R35 GM130389
6 · The paper itself

Abstract

Since publication of the crystal structure of protein kinase (PK)A three decades ago, a structural portrait of the conserved kinase core has been drawn. The next challenge is to elucidate structures of full-length kinases and to address the intrinsically disordered regions (IDRs) that typically flank the core as well as the small linear motifs (SLiMs) that are embedded within the IDRs. It is increasingly apparent that unstructured regions integrate the kinase catalytic chassis into multienzyme-based regulatory networks. The extracellular signal-regulated kinase-ribosomal S6 PK-phosphoinositide-dependent kinase (ERK-RSK-PDK) complex is an excellent example to demonstrate how IDRs and SLiMs govern communication between four different kinase catalytic cores to mediate activation and how in molecular terms these promote the formation of kinase heterodimers in a context dependent fashion.

Indexed as

HumansIntrinsically Disordered ProteinsModels, MolecularProtein DomainsProtein KinasesIntrinsically Disordered ProteinsProtein Kinasescell signalingdisorderlinear motifprotein kinaseprotein–protein interaction

Identifiers

PMID30611608
PMCPMC6592696
OpenAlexW2908089242

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.