Evidence map›Paper›PMID 36289728›Full record

ArticleBiomedicines2022

Study on Tissue Homogenization Buffer Composition for Brain Mass Spectrometry-Based Proteomics.

Adam Aleksander Karpiński, Julio Cesar Torres Elguera, Anne Sanner, Witold Konopka, Leszek Kaczmarek, Dominic Winter, Anna Konopka, Ewa Bulska

Open access · goldAbstract read
In one paragraph

Article in Biomedicines, 2022. 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
0.7field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  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

8 authors at 4 institutions in 2 countries.

Adam Aleksander KarpińskiFaculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.ORCID 0000-0002-1798-4021
Julio Cesar Torres ElgueraBiological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw, Żwirki i Wigury 101, 02-089 Warsaw, Poland.
Anne SannerInstitute for Biochemistry and Molecular Biology (IBMB), Medical Faculty, University of Bonn, Nußallee 11, 53115 Bonn, Germany.ORCID 0000-0002-6662-7039
Witold KonopkaLukasiewicz Research Network-PORT Polish Center for Technology Development, Stablowicka 147, 54-066 Wroclaw, Poland.
Leszek KaczmarekNencki-EMBL Center of Excellence for Neural Plasticity and Brain Disorders: BRAINCITY, Nencki Institute of Experimental Biology of the Polish Academy of Sciences, Pasteura 3, 02-093 Warsaw, Poland.
Dominic WinterInstitute for Biochemistry and Molecular Biology (IBMB), Medical Faculty, University of Bonn, Nußallee 11, 53115 Bonn, Germany.ORCID 0000-0001-6788-6641
Anna KonopkaBiological and Chemical Research Centre, Faculty of Chemistry, University of Warsaw, Żwirki i Wigury 101, 02-089 Warsaw, Poland.
Ewa BulskaFaculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw, Poland.
Instytut Biologii Doświadczalnej im. Marcelego Nenckiego · PLŁukasiewicz Research Network · PLUniversity of Bonn · DEUniversity of Warsaw · PL

Funding

National Science Center 2019/35/B/NZ4/02831Operational Programme Knowledge Education Development 2014-2020 co-financed by European Social Fund POWR.03.02.00-00-I007/16-00
6 · The paper itself

Abstract

Mass spectrometry-based proteomics aims to study the proteome both qualitatively and quantitatively. A key step in proteomic analysis is sample preparation, which is crucial for reliable results. We investigated the effect of the composition of the homogenization buffer used to extract proteins from brain tissue on the yield of protein extraction and the number and type of extracted proteins. Three different types of buffers were compared-detergent-based buffer (DB), chaotropic agent-based buffer (CAB) and buffer without detergent and chaotropic agent (DFB). Based on label-free quantitative protein analysis, detergent buffer was identified as the most suitable for global proteomic profiling of brain tissue. It allows the most efficient extraction of membrane proteins, synaptic and synaptic membrane proteins along with ribosomal, mitochondrial and myelin sheath proteins, which are of particular interest in the field of neurodegenerative disorders research.

Indexed as

brain proteomicsproteomic analysissample preparation

Identifiers

PMID36289728
PMCPMC9598821
OpenAlexW4303614147

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.