ArticleMolecular & cellular proteomics : MCP2017
Neprosin, a Selective Prolyl Endoprotease for Bottom-up Proteomics and Histone Mapping.
Article in Molecular & cellular proteomics : MCP, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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.
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.
Who cites it
20 citing papers in PubMed, 49 citations in OpenAlex.
- Targeted enzymatic therapy for coeliac disease.EMBO molecular medicine · 2026Article
- A Native Nepenthesin Reactor for Improved Proteolytic Digestion of Intrinsically Disordered Proteins in Proteomics Workflows.Chembiochem : a European journal of chemical biology · 2026Article
- Jasmonate signaling and prey nutrient availability trigger distinct biochemical responses in the Drosera capensis feeding cycle.Plant physiology · 2026Article
- Postproline Cleaving Enzymes also Show Specificity to Reduced Cysteine.Analytical chemistry · 2024Article
- Leveraging yeast sequestration to study and engineer posttranslational modification enzymes.Biotechnology and bioengineering · 2024Review
- The Arabidopsis DUF239 gene family encodes Neprosin-like proteins that are widely expressed in seed endosperm.The plant genome · 2023Article
- Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy.Nature communications · 2022Article
- Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications.Plants (Basel, Switzerland) · 2022Review
- Article
- Mass spectrometry-based proteomics in basic and translational research of SARS-CoV-2 coronavirus and its emerging mutants.Clinical proteomics · 2021Review
- Dual protease type XIII/pepsin digestion offers superior resolution and overlap for the analysis of histone tails by HX-MS.Methods (San Diego, Calif.) · 2020Article
- Targeting proline in (phospho)proteomics.The FEBS journal · 2020Article
- ExteNDing Proteome Coverage with Legumain as a Highly Specific Digestion Protease.Analytical chemistry · 2020Article
- Unusual genome expansion and transcription suppression in ectomycorrhizal Tricholoma matsutake by insertions of transposable elements.PloS one · 2020Article
- Chasing Tails: Cathepsin-L Improves Structural Analysis of Histones by HX-MS.Molecular & cellular proteomics : MCP · 2019Article
- Assessing Carnivorous Plants for the Production of Recombinant Proteins.Frontiers in plant science · 2019Article
- Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.The Journal of biological chemistry · 2018Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Article
- Aspergillus niger Prolyl Endoprotease for Hydrogen-Deuterium Exchange Mass Spectrometry and Protein Structural Studies.Analytical chemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trypsin dominates bottom-up proteomics, but there are reasons to consider alternative enzymes. Improving sequence coverage, exposing proteomic "dark matter," and clustering post-translational modifications in different ways and with higher-order drive the pursuit of reagents complementary to trypsin. Additionally, enzymes that are easy to use and generate larger peptides that capitalize upon newer fragmentation technologies should have a place in proteomics. We expressed and characterized recombinant neprosin, a novel prolyl endoprotease of the DUF239 family, which preferentially cleaves C-terminal to proline residues under highly acidic conditions. Cleavage also occurs C-terminal to alanine with some frequency, but with an intriguingly high "skipping rate." Digestion proceeds to a stable end point, resulting in an average peptide mass of 2521 units and a higher dependence upon electron-transfer dissociation for peptide-spectrum matches. In contrast to most proline-cleaving enzymes, neprosin effectively degrades proteins of any size. For 1251 HeLa cell proteins identified in common using trypsin, Lys-C, and neprosin, almost 50% of the neprosin sequence contribution is unique. The high average peptide mass coupled with cleavage at residues not usually modified provide new opportunities for profiling clusters of post-translational modifications. We show that neprosin is a useful reagent for reading epigenetic marks on histones. It generates peptide 1-38 of histone H3 and peptide 1-32 of histone H4 in a single digest, permitting the analysis of co-occurring post-translational modifications in these important N-terminal tails.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.