Evidence map›Paper›PMID 24115095›Full record

ReviewProtein science : a publication of the Protein Society2013

Molecular basis of MAP kinase regulation.

Wolfgang Peti, Rebecca Page

Open access · hybridAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed
9.0field-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

157 citing papers in PubMed, 319 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Variable thresholds for phosphorylation targets of the ERK signaling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Atypical MAPKs in cancer.The FEBS journal · 2025
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Special Issue: MAPK Signaling Cascades in Human Health and Diseases.International journal of molecular sciences · 2024
    Article
  19. Article
  20. Pharmacological Significance ofFoods (Basel, Switzerland) · 2024
    Review

97 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 at 1 institution in 1 country.

Wolfgang PetiDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, 02912; Department of Chemistry, Brown University, Providence, Rhode Island, 02912.
Rebecca Page
Brown University · US

Funding

The Regulation of PP1 in the NucleusR01GM098482 · NIGMS · UNIVERSITY OF ARIZONA · PI PAGE, REBECCA · 2011 to 2019
$2.8M
Dynamics & energetics of p38a kinase regulation by ligandsR01GM100910 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI PETI, WOLFGANG, WAND, A. JOSHUA · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM098482NIGMS NIH HHS R01GM098482NIGMS NIH HHS R01 GM100910NIGMS NIH HHS R01GM100910
6 · The paper itself

Abstract

Mitogen-activated protein kinases (MAPKs; ERK1/2, p38, JNK, and ERK5) have evolved to transduce environmental and developmental signals (growth factors, stress) into adaptive and programmed responses (differentiation, inflammation, apoptosis). Almost 20 years ago, it was discovered that MAPKs contain a docking site in the C-terminal lobe that binds a conserved 13-16 amino acid sequence known as the D- or KIM-motif (kinase interaction motif). Recent crystal structures of MAPK:KIM-peptide complexes are leading to a precise understanding of how KIM sequences contribute to MAPK selectivity. In addition, new crystal and especially NMR studies are revealing how residues outside the canonical KIM motif interact with specific MAPKs and contribute further to MAPK selectivity and signaling pathway fidelity. In this review, we focus on these recent studies, with an emphasis on the use of NMR spectroscopy, isothermal titration calorimetry and small angle X-ray scattering to investigate these processes.

Indexed as

Amino Acid MotifsAnimalsBinding SitesConsensus SequenceGene Expression RegulationHumansMitogen-Activated Protein Kinase KinasesNuclear Magnetic Resonance, BiomolecularScattering, Small AngleSequence Analysis, ProteinSignal TransductionSubstrate SpecificityX-Ray DiffractionMitogen-Activated Protein Kinase KinasesD-motifDUSPERKJNKKIMkinase interaction motifMAP kinaseNMRp38PTPSAXSstructure

Identifiers

PMID24115095
PMCPMC3843625
OpenAlexW1483925515

What OpenQuestion holds

Textmetadata
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.