Evidence map›Paper›PMID 28373296›Full record

ArticleMolecular & cellular proteomics : MCP2017

A Proteomic Approach to Identify Alterations in the Small Ubiquitin-like Modifier (SUMO) Network during Controlled Mechanical Ventilation in Rat Diaphragm Muscle.

Arvind Venkat Namuduri, Gabriel Heras, Jia Mi, Nicola Cacciani, Katarina Hörnaeus, Anne Konzer, Sara Bergström Lind, Lars Larsson, Stefano Gastaldello

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The emerging roles of SUMOylation in pulmonary diseases.Molecular medicine (Cambridge, Mass.) · 2023
    Review
  5. Review
  6. Article
  7. Review
  8. MuRF1/TRIM63, Master Regulator of Muscle Mass.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Article
  11. 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 3 institutions in 3 countries.

Arvind Venkat NamuduriFrom the ‡Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, SE-17177, Sweden.
Gabriel HerasFrom the ‡Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, SE-17177, Sweden.
Jia Mi§Department of Chemistry-BMC, Analytical Chemistry and Science for Lab Laboratory, Uppsala University, Box 599, Uppsala, SE-75124, Sweden.
Nicola CaccianiFrom the ‡Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, SE-17177, Sweden.
Katarina Hörnaeus§Department of Chemistry-BMC, Analytical Chemistry and Science for Lab Laboratory, Uppsala University, Box 599, Uppsala, SE-75124, Sweden.
Anne Konzer§Department of Chemistry-BMC, Analytical Chemistry and Science for Lab Laboratory, Uppsala University, Box 599, Uppsala, SE-75124, Sweden.
Sara Bergström Lind§Department of Chemistry-BMC, Analytical Chemistry and Science for Lab Laboratory, Uppsala University, Box 599, Uppsala, SE-75124, Sweden.
Lars LarssonFrom the ‡Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, SE-17177, Sweden.ORCID 0000-0002-6440-1458
Stefano GastaldelloFrom the ‡Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm, SE-17177, Sweden; stefano.gastaldello@ki.se.ORCID 0000-0001-7369-8452
Karolinska Institutet · SEUppsala University · SEPennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small ubiquitin-like modifier (SUMO) is as a regulator of many cellular functions by reversible conjugation to a broad number of substrates. Under endogenous or exogenous perturbations, the SUMO network becomes a fine sensor of stress conditions by alterations in the expression level of SUMO enzymes and consequently changing the status of SUMOylated proteins. The diaphragm is the major inspiratory muscle, which is continuously active under physiological conditions, but its structure and function is severely affected when passively displaced for long extents during mechanical ventilation (MV). An iatrogenic condition called Ventilator-Induced Diaphragm Dysfunction (VIDD) is a major cause of failure to wean patients from ventilator support but the molecular mechanisms underlying this dysfunction are not fully understood. Using a unique experimental Intensive Care Unit (ICU) rat model allowing long-term MV, diaphragm muscles were collected in rats control and exposed to controlled MV (CMV) for durations varying between 1 and 10 days. Endogenous SUMOylated diaphragm proteins were identified by mass spectrometry and validated with

Indexed as

Respiration, ArtificialAnimalsDeep SedationDiaphragmFemaleNeuromuscular BlockadeProteomicsRats, Sprague-DawleySmall Ubiquitin-Related Modifier ProteinsSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID28373296
PMCPMC5461539
OpenAlexW2604129760

What OpenQuestion 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 OpenQuestion graph.