Evidence map›Paper›PMID 27252361›Full record

ReviewCold Spring Harbor perspectives in biology2016

Protein Regulation in Signal Transduction.

Michael J Lee, Michael B Yaffe

Abstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Article
  2. Bacterial stress responses lower mRNA-protein level correlations.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Protein Dynamics in Plant Immunity: Insights into Plant-Pest Interactions.International journal of molecular sciences · 2024
    Review
  15. Review
  16. Review
  17. Interaction of Soybean (Plants (Basel, Switzerland) · 2024
    Article
  18. Review
  19. Article
  20. Article

10 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.

Michael J LeeDavid H. Koch Institute for Integrative Cancer Research at MIT, Department of Biology and Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
Michael B YaffeDavid H. Koch Institute for Integrative Cancer Research at MIT, Department of Biology and Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMMARYCells must respond to a diverse, complex, and ever-changing mix of signals, using a fairly limited set of parts. Changes in protein level, protein localization, protein activity, and protein-protein interactions are critical aspects of signal transduction, allowing cells to respond highly specifically to a nearly limitless set of cues and also to vary the sensitivity, duration, and dynamics of the response. Signal-dependent changes in levels of gene expression and protein synthesis play an important role in regulation of protein levels, whereas posttranslational modifications of proteins regulate their degradation, localization, and functional interactions. Protein ubiquitylation, for example, can direct proteins to the proteasome for degradation or provide a signal that regulates their interactions and/or location within the cell. Similarly, protein phosphorylation by specific kinases is a key mechanism for augmenting protein activity and relaying signals to other proteins that possess domains that recognize the phosphorylated residues.

Indexed as

PhosphorylationProtein BindingProtein Processing, Post-TranslationalAllosteric SiteAmino Acid MotifsAnimalsCell MembraneGene Expression RegulationGTP PhosphohydrolasesHumansLipidsModels, TheoreticalProteasome Endopeptidase ComplexProtein DomainsProtein Interaction MappingSignal TransductionGTP PhosphohydrolasesLipidsProteasome Endopeptidase ComplexTranscription Factors

Identifiers

PMID27252361
PMCPMC4888820

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.