Evidence map›Paper›PMID 22992589›Full record

ReviewNature reviews. Molecular cell biology2012

Assembly of allosteric macromolecular switches: lessons from PKA.

Susan S Taylor, Ronit Ilouz, Ping Zhang, Alexandr P Kornev

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 277 papers.

0numbers the graph read from it
0cells of the map it votes in
277citing papers in PubMed
14.2field-weighted citation impact, top 1% 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

277 citing papers in PubMed, 475 citations in OpenAlex.

  1. A Sesquiterpenoid fromInternational journal of molecular sciences · 2026
    Article
  2. Review
  3. Article
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  5. Review
  6. Article
  7. Article
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  14. Conformational Dynamics and Allostery in the cAMP-Protein Kinase A Signalosome.Advances in experimental medicine and biology · 2026
    Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. N3A motifs in RIβ mediate allosteric crosstalk between cAMP and ATP in PKA activation.Protein science : a publication of the Protein Society · 2025
    Article
  20. Article

217 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

4 authors at 2 institutions in 1 country.

Susan S TaylorDepartment of Pharmacology, University of California, San Diego, La Jolla, 92093-90654, USA. staylor@ucsd.edu
Ronit Ilouz
Ping Zhang
Alexandr P Kornev
University of California, San Diego · USHoward Hughes Medical Institute · 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
Protein Kinase Regulatory Subunit I Directed MutagenesisR01GM034921 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2018
$7.2M
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 InstituteNIDDK NIH HHS DK54441NIDDK NIH HHS P01 DK054441NIGMS NIH HHS GM19301NIGMS NIH HHS GM34921NIGMS NIH HHS R01 GM019301NIGMS NIH HHS R01 GM034921NIGMS NIH HHS R37 GM019301
6 · The paper itself

Abstract

Protein kinases are dynamic molecular switches that have evolved to be only transiently activated. Kinase activity is embedded within a conserved kinase core, which is typically regulated by associated domains, linkers and interacting proteins. Moreover, protein kinases are often tethered to large macromolecular complexes to provide tighter spatiotemporal control. Thus, structural characterization of kinase domains alone is insufficient to explain protein kinase function and regulation in vivo. Recent progress in structural characterization of cyclic AMP-dependent protein kinase (PKA) exemplifies how our knowledge of kinase signalling has evolved by shifting the focus of structural studies from single kinase subunits to macromolecular complexes.

Indexed as

Catalytic DomainCrystallography, X-RayCyclic AMPCyclic AMP-Dependent Protein KinasesMacromolecular SubstancesPhosphorylationProtein IsoformsProtein Structure, TertiarySignal TransductionCyclic AMPCyclic AMP-Dependent Protein KinasesMacromolecular SubstancesProtein Isoforms

Identifiers

PMID22992589
PMCPMC3985763
OpenAlexW2061684132

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.