ArticleJournal of the American Society for Mass Spectrometry2022
Top-Down Identification and Sequence Analysis of Small Membrane Proteins Using MALDI-MS/MS.
Article in Journal of the American Society for Mass Spectrometry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Bacterial Proteomics and Antibiotic Resistance Identification: Is Single-Cell Analysis a Worthwhile Pursuit?Pathogens (Basel, Switzerland) · 2025Review
- Sample preparation and cleanup methods for clinical top-down proteomics.Expert review of proteomics · 2025Review
- Detection and Quantitation of Small Proteins Using Mass Spectrometry.Molecular & cellular proteomics : MCP · 2025Article
- Functional diversity and molecular interactions of small membrane proteins in bacteria.microLife · 2025Review
- A survey of experimental and computational identification of small proteins.Briefings in bioinformatics · 2024Review
- Small proteins in Gram-positive bacteria.FEMS microbiology reviews · 2023Article
- Toward a MALDI in-source decay (ISD) method for top-down analysis of protein footprinting.European journal of mass spectrometry (Chichester, England) · 2023Article
- Proteoforms expand the world of microproteins and short open reading frame-encoded peptides.iScience · 2023Review
- Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research.Molecules (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Identification and sequence determination by mass spectrometry have become routine analyses for soluble proteins. Membrane proteins, however, remain challenging targets due to their hydrophobicity and poor annotation. In particular small membrane proteins often remain unnoticed as they are largely inaccessible to Bottom-Up proteomics. Recent advances in structural biology, though, have led to multiple membrane protein complex structures being determined at sufficiently high resolution to detect uncharacterized, small subunits. In this work we offer a guide for the mass spectrometric characterization of solvent extraction-based purifications of small membrane proteins isolated from protein complexes and cellular membranes. We first demonstrate our Top-Down MALDI-MS/MS approach on a Photosystem II preparation, analyzing target protein masses between 2.5 and 9 kDa with high accuracy and sensitivity. Then we apply our technique to purify and sequence the mycobacterial ATP synthase
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Registered trials
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