Evidence map›Paper›PMID 28224476›Full record

ReviewMolecular neurobiology2018

Protein Phosphatase 2A: a Double-Faced Phosphatase of Cellular System and Its Role in Neurodegenerative Disorders.

Md Nematullah, M N Hoda, Farah Khan

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
  3. Glycyrrhizic Acid Alleviates Semen Strychni-Induced Neurotoxicity Through the Inhibition of HMGB1 Phosphorylation and Inflammatory Responses.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Protein phosphatases in TLR signaling.Cell communication and signaling : CCS · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Proteomic View of the Crosstalk betweenFrontiers in microbiology · 2017
    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

3 authors at 2 institutions in 2 countries.

Md NematullahDepartment of Biochemistry, Faculty of Science, Jamia Hamdard, New Delhi, 110062, India.
M N HodaDepartment of Medical Laboratory, Imaging and Radiological Sciences College of Allied Health Sciences, Georgia Regents University, Augusta, GA, 30912, USA.
Farah KhanDepartment of Biochemistry, Faculty of Science, Jamia Hamdard, New Delhi, 110062, India. fkhan@jamiahamdard.ac.in.
Jamia Hamdard · INAugusta University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphatase 2A (PP2A), a ubiquitously expressed serine/threonine phosphatase, is a vitally important phosphatase for the cellular system. Structurally, it is constituted of three different subunits, namely catalytic subunit (PP2Ac), structural scaffold subunit (PP2A-A), and regulatory subunit (PP2A-B). All subunits have various isoforms, and catalytic and scaffold subunits are ubiquitously expressed, whereas regulatory subunits are more specific to tissue and cell type. It is the numerous possibilities of PP2A holoenzyme assembly with varying isoform components that make it possess a dual nature of activator or the inhibitory character in different signaling pathways, namely neural developmental pathways, Akt/protein kinase B pathway, NF-kB pathway, MAPK pathway, apoptosis pathway, and cell cycle progression to name a few. Importantly, the expression of PP2A in the brain is highest among the serine phosphatases and is known to actively participate in the neural development process. However, the exact mechanism of action of PP2A is still debated and enunciating the holoenzyme components, especially the regulatory subunit of PP2A involved in regulating neural developmental process is still poorly understood. In this review, we try to throw some light on the involvement of various PP2A holoenzyme forms in the process of neurogenesis and progression of neurodegenerative diseases.

Indexed as

AnimalsApoptosisHumansNeurodegenerative DiseasesNeurogenesisProtein Phosphatase 2ProteolysisSignal TransductionProtein Phosphatase 2Neurodegenerative diseaseNeurogenesisPP2AProtein phosphatase

Identifiers

PMID28224476
OpenAlexW2589981026

What Socratic 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 Socratic graph.