ArticleJournal of mass spectrometry : JMS2013
Mass-biased partitioning to enhance middle down proteomics analysis.
Article in Journal of mass spectrometry : JMS, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
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Who cites it
5 citing papers in PubMed.
- Middle-down approach: a choice to sequence and characterize proteins/proteomes by mass spectrometry.RSC advances · 2018Review
- Toward an Optimized Workflow for Middle-Down Proteomics.Analytical chemistry · 2017Article
- Middle-down mass spectrometry enables characterization of branched ubiquitin chains.Biochemistry · 2014Article
- Ultraviolet photodissociation for characterization of whole proteins on a chromatographic time scale.Analytical chemistry · 2014Article
- Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A strategy is presented for enhancing the middle-down analysis of higher mass peptides recovered from complex protein mixtures. Following a 30-min digestion of multiple myeloma cell lysate by an acid cleavage reaction that is selective for aspartic acid, a 3000 Da membrane filter is used to bifurcate the peptide product mixture, and the heavier fraction is subjected to collisional activation with precursor selection that excludes charge states below +4. Filtration and charge state selection are shown to provide significant increases in the number of peptides identified in the mass range above 3000 Da and in information about protein sequences.
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Registered trials
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