Evidence map›Paper›PMID 23202904›Full record

ReviewInternational journal of molecular sciences2012

Protein Arginine Methyltransferases (PRMTs): promising targets for the treatment of pulmonary disorders.

Dariusz Zakrzewicz, Anna Zakrzewicz, Klaus T Preissner, Philipp Markart, Malgorzata Wygrecka

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 21% 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, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Histone methyltransferase and drug resistance in cancers.Journal of experimental & clinical cancer research : CR · 2020
    Review
  11. Article
  12. Article
  13. Mechanisms and Inhibitors of Histone Arginine Methylation.Chemical record (New York, N.Y.) · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Small Molecule Inhibitors of Protein Arginine Methyltransferases.Expert opinion on investigational drugs · 2016
    Review
  19. Review
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

5 authors at 3 institutions in 1 country.

Dariusz ZakrzewiczDepartment of Biochemistry, Faculty of Medicine, University of Giessen Lung Center, Friedrichstrasse 24, 35392 Giessen, Germany. dariusz.zakrzewicz@innere.med.uni-giessen.de.
Anna Zakrzewicz
Klaus T Preissner
Philipp Markart
Malgorzata Wygrecka
Universities of Giessen and Marburg Lung Center · DEGerman Center for Lung Research · DEJustus-Liebig-Universität Gießen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein arginine methylation is a novel posttranslational modification that plays a pivotal role in a variety of intracellular events, such as signal transduction, protein-protein interaction and transcriptional regulation, either by the direct regulation of protein function or by metabolic products originating from protein arginine methylation that influence nitric oxide (NO)-dependent processes. A growing body of evidence suggests that both mechanisms are implicated in cardiovascular and pulmonary diseases. This review will present and discuss recent research on PRMTs and the methylation of non-histone proteins and its consequences for the pathogenesis of various lung disorders, including lung cancer, pulmonary fibrosis, pulmonary hypertension, chronic obstructive pulmonary disease and asthma. This article will also highlight novel directions for possible future investigations to evaluate the functional contribution of arginine methylation in lung homeostasis and disease.

Indexed as

AnimalsAsthmaHumansHypertension, PulmonaryLung DiseasesLung NeoplasmsProtein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalPulmonary Disease, Chronic ObstructivePulmonary FibrosisProtein-Arginine N-Methyltransferases

Identifiers

PMID23202904
PMCPMC3497278
OpenAlexW1991630298

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.