Evidence map›Paper›PMID 39449499›Full record

ArticleProteomes2024

Protein Extraction Methods Suitable for Muscle Tissue Proteomic Analysis.

Lorenza Vantaggiato, Claudia Landi, Enxhi Shaba, Daniela Rossi, Vincenzo Sorrentino, Luca Bini

Abstract read
In one paragraph

Article in Proteomes, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

6 authors.

Lorenza VantaggiatoFunctional Proteomics Lab., Department Life Sciences, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.ORCID 0000-0003-4078-7250
Claudia LandiFunctional Proteomics Lab., Department Life Sciences, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.ORCID 0000-0003-0410-8038
Enxhi ShabaFunctional Proteomics Lab., Department Life Sciences, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.ORCID 0000-0002-9561-2426
Daniela RossiDepartment of Molecular and Developmental Medicine, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.ORCID 0000-0003-0463-7327
Vincenzo SorrentinoDepartment of Molecular and Developmental Medicine, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.ORCID 0000-0002-8573-8631
Luca BiniFunctional Proteomics Lab., Department Life Sciences, University of Siena, Via Aldo Moro 2, 53100 Siena, Italy.ORCID 0000-0001-8951-2106

Funding

European Union-Next Generation EU in the framework of the mRNA National Center for Gene Therapy and Drugs PNRR-M4C2-1.4 CN00000041-CUP: J33C22001140001Italian Ministry of Education, Universities and Research (MUR) within the Italian NRRP, Tuscany Health Ecosystem SPOKE 7 D.D. n. 1050 23/06/2022
6 · The paper itself

Abstract

Muscle tissue is one of the most dynamic and plastic tissues of the mammalian body and covers different roles, such as force generation and metabolic control. Muscular proteomics provides an important opportunity to reveal the molecular mechanisms behind muscle pathophysiology. To ensure successful proteomic analysis, it is necessary to have an efficient and reproducible protein extraction method. This study aimed to evaluate the efficacy of two different extraction protocols of muscle samples for two-dimensional gel electrophoresis. In particular, mouse muscle proteins were extracted by an SDS-based buffer (Method A) and by a UREA/CHAPS/DTE/TRIS solution (Method B). The efficacies of the methods were assessed by performing an image analysis of the 2DE gels and by statistical and multivariate analyses. The 2DE gels in both preparations showed good resolution and good spot overlapping. Methods A and B produced 2DE gels with different means of total spots, higher for B. Image analysis showed different patterns of protein abundance between the protocols. The results showed that the two methods extract and solubilize proteins with different chemical-physical characteristics and different cellular localizations. These results attest the efficacy and reproducibility of both protein extraction methods, which can be parallelly applied for comprehensive proteomic profiling of muscle tissue.

Indexed as

mass spectrometrymuscle tissuemyopathiesprotein denaturationtwo-dimensional electrophoresis

Identifiers

PMID39449499
PMCPMC11503273

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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.