Evidence map›Paper›PMID 30401536›Full record

ReviewBiochimica et biophysica acta. Molecular cell research2019

cAMP regulation of protein phosphatases PP1 and PP2A in brain.

Shannon N Leslie, Angus C Nairn

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Molecular cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Role of serine/threonine phosphatases 1 and 2A in pancreatic acinar fluid and electrolyte secretion.American journal of physiology. Gastrointestinal and liver physiology · 2026
    Article
  6. Article
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  11. Review
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  14. Compartmentalized cAMP signalling and control of cardiac rhythm.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  15. Article
  16. Article
  17. Article
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  19. Article
  20. Resveratrol Induces the Fasting State and Alters Circadian Metabolism in Hepatocytes.Plant foods for human nutrition (Dordrecht, Netherlands) · 2022
    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

2 authors at 1 institution in 1 country.

Shannon N LeslieInterdepartmental Neuroscience Program, Yale University, New Haven, CT, United States of America.
Angus C NairnDepartment of Psychiatry, Yale University, New Haven, CT, United States of America.
Yale University · US

Funding

Interdepartmental Neuroscience Program (INP)T32NS041228 · NINDS · YALE UNIVERSITY · PI Charles A Greer, Marina R Picciotto · 2001 to 2026
$12.0M
Yale Alzheimer Disease Research CenterP50AG047270 · NIA · YALE UNIVERSITY · PI MAROTTOLI, RICHARD · 2015 to 2019
$8.3M
Supplement for "Serine/Threonine Phosphatases in Neurological Diseases"R01NS091336 · NINDS · UNIVERSITY OF ARIZONA · PI PAGE, REBECCA, PETI, WOLFGANG · 2015 to 2019
$1.8M
NIA NIH HHS P50 AG047270NINDS NIH HHS R01 NS091336NINDS NIH HHS T32 NS041228
6 · The paper itself

Abstract

Normal functioning of the brain is dependent upon a complex web of communication between numerous cell types. Within neuronal networks, the faithful transmission of information between neurons relies on an equally complex organization of inter- and intra-cellular signaling systems that act to modulate protein activity. In particular, post-translational modifications (PTMs) are responsible for regulating protein activity in response to neurochemical signaling. The key second messenger, cyclic adenosine 3',5'-monophosphate (cAMP), regulates one of the most ubiquitous and influential PTMs, phosphorylation. While cAMP is canonically viewed as regulating the addition of phosphate groups through its activation of cAMP-dependent protein kinases, it plays an equally critical role in regulating removal of phosphate through indirect control of protein phosphatase activity. This dichotomy of regulation by cAMP places it as one of the key regulators of protein activity in response to neuronal signal transduction throughout the brain. In this review we focus on the role of cAMP in regulation of the serine/threonine phosphatases protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) and the relevance of control of PP1 and PP2A to regulation of brain function and behavior.

Indexed as

AnimalsBrainCyclic AMPCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsHumansIntracellular Signaling Peptides and ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Phosphatase 2Signal TransductionCyclic AMPCyclic AMP-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinDopamine and cAMP-Regulated Phosphoprotein 32Enzyme InhibitorsIntracellular Signaling Peptides and ProteinsPhosphoprotein PhosphatasesProtein Phosphatase 1Protein Phosphatase 2protein phosphatase inhibitor-1BraincAMPPKAPP1PP2AStriatum

Identifiers

PMID30401536
PMCPMC6433392
OpenAlexW2890294399

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.