Evidence map›Paper›PMID 42496275›Full record

ArticleProteomes2026

Lyophilization Prior to Homogenisation and Extraction Increases Membrane Protein Detection in Gram-Negative Bacterial Proteomic Analyses.

Breyer Woodland, Luke A Farrell, Matthew B O'Rourke, Matthew P Padula

Abstract read
In one paragraph

Article in Proteomes, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Breyer WoodlandSchool of Life Sciences and Proteomics and Metabolomics Core Facility, Faculty of Science, University of Technology Sydney, Ultimo, NSW 2007, Australia.ORCID 0009-0004-7390-0189
Luke A FarrellSchool of Life Sciences and Proteomics and Metabolomics Core Facility, Faculty of Science, University of Technology Sydney, Ultimo, NSW 2007, Australia.ORCID 0009-0004-6953-8877
Matthew B O'RourkeSchool of Life Sciences and Proteomics and Metabolomics Core Facility, Faculty of Science, University of Technology Sydney, Ultimo, NSW 2007, Australia.
Matthew P PadulaSchool of Life Sciences and Proteomics and Metabolomics Core Facility, Faculty of Science, University of Technology Sydney, Ultimo, NSW 2007, Australia.ORCID 0000-0002-8283-0643

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMulti-drug resistant Gram-negative bacteria (GNB) are major contributors to the antimicrobial resistance (AMR) burden. AMR mechanisms are primarily mediated by proteoforms; therefore, proteomic analyses of GNB offers a significant advantage in understanding the mechanisms of AMR. A large portion of these mechanisms are mediated by membrane proteins; however, they are often difficult to extract due to their hydrophobic nature and complex interactions with other components of the cell membrane. To extract the greatest number of proteoforms, an efficient homogenisation protocol is required to effectively disrupt the rigid cell wall and membrane.

methodsUsing

resultsWe demonstrate that lyophilization improves bead-beating extraction methods by increasing the detection of membrane proteins. We detected numerous unique membrane proteins in each bacterial isolate, including ABC transporters and proteins involved in lipopolysaccharide synthesis, when lyophilizing prior to bead-beating, compared to only flash-freezing.

conclusionsAs membrane proteins play a central role in AMR mechanisms, this improvement in their isolation and identification will aid in understanding the resistance and molecular mechanisms associated with multi-drug resistant GNB.

Indexed as

antimicrobial resistancebacterial protein extractionmembrane proteinsmulti-drug resistance bacteriaproteomics

Identifiers

PMID42496275
PMCPMC13398305

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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.