Evidence map›Paper›PMID 33500497›Full record

ArticleScientific reports2021

Proteome-wide profiling and mapping of post translational modifications in human hearts.

Navratan Bagwan, Henrik H El Ali, Alicia Lundby

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Review
  3. Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome.Journal of cardiovascular development and disease · 2026
    Review
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  5. Article
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  20. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 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

3 authors at 2 institutions in 1 country.

Navratan BagwanDepartment of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, 2200, Copenhagen, Denmark.
Henrik H El AliDepartment of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, 2200, Copenhagen, Denmark.
Alicia LundbyDepartment of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, 2200, Copenhagen, Denmark. alicia.lundby@sund.ku.dk.
University of Copenhagen · DKNovo Nordisk Foundation · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post translational modifications (PTMs) are covalent modifications of proteins that can range from small chemical modifications to addition of entire proteins. PTMs contribute to regulation of protein function and thereby greatly increase the functional diversity of the proteome. In the heart, a few well-studied PTMs, such as phosphorylation and glycosylation, are known to play essential roles for cardiac function. Yet, only a fraction of the ~ 300 known PTMs have been studied in a cardiac context. Here we investigated the proteome-wide map of PTMs present in human hearts by utilizing high-resolution mass spectrometry measurements and a suite of PTM identification algorithms. Our approach led to identification of more than 150 different PTMs across three of the chambers in human hearts. This finding underscores that decoration of cardiac proteins by PTMs is much more diverse than hitherto appreciated and provides insights in cardiac protein PTMs not yet studied. The results presented serve as a catalogue of which PTMs are present in human hearts and outlines the particular protein and the specific amino acid modified, and thereby provides a detail-rich resource for exploring protein modifications in human hearts beyond the most studied PTMs.

Indexed as

Protein Processing, Post-TranslationalProteomicsAmino AcidsAmino Acid SequenceHumansMyocardiumOxidation-ReductionPeptidesPhosphorylationProteomeAmino AcidsPeptidesProteome

Identifiers

PMID33500497
PMCPMC7838296
OpenAlexW3121349694

What OpenQuestion holds

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Registered trials

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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.