Evidence map›Paper›PMID 37763671›Full record

ReviewMedicina (Kaunas, Lithuania)2023

Protein Phosphatase 2A as a Therapeutic Target in Pulmonary Diseases.

Howard Yu, Sahil Zaveri, Zeeshan Sattar, Michael Schaible, Brais Perez Gandara, Anwar Uddin, Lucas R McGarvey, Michael Ohlmeyer, Patrick Geraghty

Open access · goldAbstract readReview
In one paragraph

Review in Medicina (Kaunas, Lithuania), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. 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

9 authors at 2 institutions in 1 country.

Howard YuDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.
Sahil ZaveriDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.ORCID 0000-0003-0116-8297
Zeeshan SattarDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.
Michael SchaibleDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.
Brais Perez GandaraDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.
Anwar UddinDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.
Lucas R McGarveyDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.
Michael OhlmeyerAtux Iskay LLC, Plainsboro, NJ 08536, USA.
Patrick GeraghtyDepartment of Medicine, State University of New York Downstate Health Sciences University, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.ORCID 0000-0003-1647-5505
State University of New York · USPrinceton Satellite Systems (United States) · US

Funding

United States Department of Defense W81XWH-20-1-0494
6 · The paper itself

Abstract

New disease targets and medicinal chemistry approaches are urgently needed to develop novel therapeutic strategies for treating pulmonary diseases. Emerging evidence suggests that reduced activity of protein phosphatase 2A (PP2A), a complex heterotrimeric enzyme that regulates dephosphorylation of serine and threonine residues from many proteins, is observed in multiple pulmonary diseases, including lung cancer, smoke-induced chronic obstructive pulmonary disease, alpha-1 antitrypsin deficiency, asthma, and idiopathic pulmonary fibrosis. Loss of PP2A responses is linked to many mechanisms associated with disease progressions, such as senescence, proliferation, inflammation, corticosteroid resistance, enhanced protease responses, and mRNA stability. Therefore, chemical restoration of PP2A may represent a novel treatment for these diseases. This review outlines the potential impact of reduced PP2A activity in pulmonary diseases, endogenous and exogenous inhibitors of PP2A, details the possible PP2A-dependent mechanisms observed in these conditions, and outlines potential therapeutic strategies for treatment. Substantial medicinal chemistry efforts are underway to develop therapeutics targeting PP2A activity. The development of specific activators of PP2A that selectively target PP2A holoenzymes could improve our understanding of the function of PP2A in pulmonary diseases. This may lead to the development of therapeutics for restoring normal PP2A responses within the lung.

Indexed as

AsthmaLung NeoplasmsPulmonary Disease, Chronic ObstructiveDisease ProgressionHumansProtein Phosphatase 2Protein Phosphatase 2future therapyinflammationlung diseasesPP2A

Identifiers

PMID37763671
PMCPMC10535831
OpenAlexW4386222570

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.