Evidence map›Paper›PMID 33706930›Full record

ReviewAdvances in pharmacology (San Diego, Calif.)2021

Modulation of dendritic spines by protein phosphatase-1.

Jimcy Platholi, Hugh C Hemmings

Open access · greenAbstract readReview
In one paragraph

Review in Advances in pharmacology (San Diego, Calif.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A spatial model of autophosphorylation of CabioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. 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 2 institutions in 1 country.

Jimcy PlatholiDepartment of Anesthesiology, Weill Cornell Medicine, New York, NY, United States; Feil Family Brain and Mind Research Institute, Weill Cornell Medicine, New York, NY, United States.
Hugh C HemmingsDepartment of Anesthesiology, Weill Cornell Medicine, New York, NY, United States; Department of Pharmacology, Weill Cornell Medicine, New York, NY, United States. Electronic address: hchemmi@med.cornell.edu.
MIND Research Institute · USWeill Cornell Medicine · US

Funding

SYNAPTIC MECHANISMS OF GENERAL ANESTHETIC ACTIONR01GM058055 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HEMMINGS, HUGH C · 1998 to 2023
$10.1M
Mechanisms of anesthetic-induced synaptic plasticityR01GM130722 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI PLATHOLI, JIMCY · 2019 to 2023
$1.8M
NIGMS NIH HHS R01 GM058055NIGMS NIH HHS R01 GM130722
6 · The paper itself

Abstract

Protein phosphatase-1 (PP-1), a highly conserved multifunctional serine/threonine phosphatase, is enriched in dendritic spines where it plays a major role in modulating excitatory synaptic activity. In addition to established functions in spine maturation and development, multi-subunit holoenzyme forms of PP-1 modulate higher-order cognitive functions such learning and memory. Mechanisms involved in regulating PP-1 activity and localization in spines include interactions with neurabin and spinophilin, structurally related synaptic scaffolding proteins associated with the actin cytoskeleton. Since PP-1 is a critical element in synaptic development, signaling, and plasticity, alterations in PP-1 signaling in dendritic spines are implicated in various neurological and psychiatric disorders. The effects of PP-1 depend on its isoform-specific association with regulatory proteins and activation of downstream signaling pathways. Here we review the role of PP-1 and its binding proteins neurabin and spinophilin in both developing and established dendritic spines, as well as some of the disorders that result from its dysregulation.

Indexed as

Actin CytoskeletonAnimalsDendritic SpinesHumansModels, BiologicalNervous System DiseasesNeuronal PlasticityProtein Phosphatase 1Protein Phosphatase 1Dendritic spinesNeurabinProtein phosphatase-1SpinophilinSynapse formationSynaptic plasticity

Identifiers

PMID33706930
PMCPMC8973313
OpenAlexW3110339025

What Socratic 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 Socratic graph.