Cited by 23

The DOI matches its Crossref record, with a small difference in title or year.

High-throughput proteotyping of bacterial isolates by double barrel chromatography-tandem mass spectrometry based on microplate paramagnetic beads and phylopeptidomics

Hayoun, Karim, Gaillard, Jean-Charles, Pible, Olivier, Alpha-Bazin, Béatrice, Armengaud, Jean·2020·Journal of Proteomics

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.jprot.2020.103887

Cites

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 40

  1. Grenga, 2019, Pathogen proteotyping: a rapidly developing application of mass spectrometry to address clinical concerns, Clin. Mass Spectro., 14, 9, 10.1016/j.clinms.2019.04.004 · DOI
  2. Lavigne, 2013, Mass spectrometry: a revolution in clinical microbiology?, Clin. Chem. Lab. Med., 51, 257, 10.1515/cclm-2012-0291 · DOI
  3. Karger, 2016, Current developments to use linear MALDI-TOF spectra for the identification and typing of bacteria and the characterization of other cells/organisms related to infectious diseases, Proteomics Clin. Appl., 10, 982, 10.1002/prca.201600038 · DOI
  4. Durighello, 2014, Proteogenomic biomarkers for identification of Francisella species and subspecies by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry, Anal. Chem., 86, 9394, 10.1021/ac501840g · DOI
  5. Emele, 2019, Proteotyping as alternate typing method to differentiate campylobacter coli clades, Sci. Rep., 9, 4244, 10.1038/s41598-019-40842-w · DOI
  6. Carvalhaes, 2018, Rapid detection of ceftazidime/avibactam resistance by MALDI-TOF MS, J. Antimicrob. Chemother., 73, 2579, 10.1093/jac/dky196 · DOI
  7. Patel, 2019, A moldy application of MALDI: MALDI-ToF mass spectrometry for fungal identification, J. Fungi. (Basel), 5
  8. Karlsson, 2015, Proteotyping: proteomic characterization, classification and identification of microorganisms--a prospectus, Syst. Appl. Microbiol., 38, 246, 10.1016/j.syapm.2015.03.006 · DOI
  9. Boulund, 2017, Typing and characterization of bacteria using bottom-up tandem mass spectrometry proteomics, Mol. Cell. Proteomics, 16, 1052, 10.1074/mcp.M116.061721 · DOI
  10. Karlsson, 2018, Proteotyping bacteria: characterization, differentiation and identification of pneumococcus and other species within the mitis group of the genus Streptococcus by tandem mass spectrometry proteomics, PLoS One, 13, 10.1371/journal.pone.0208804 · DOI
  11. Mappa, 2018, Assessing the ratio of Bacillus spores and vegetative cells by shotgun proteomics, Environ. Sci. Pollut. Res. Int.
  12. Berendsen, 2020, Untargeted accurate identification of highly pathogenic bacteria directly from blood culture flasks, Int. J. Med. Microbiol., 310, 151376, 10.1016/j.ijmm.2019.151376 · DOI
  13. Abbondio, 2019, Fecal metaproteomic analysis reveals unique changes of the gut microbiome functions after consumption of sourdough carasau bread, Front. Microbiol., 10, 1733, 10.3389/fmicb.2019.01733 · DOI
  14. Pible, 2020, Estimating relative biomasses of organisms in microbiota using “phylopeptidomics”, Microbiome, 8, 30, 10.1186/s40168-020-00797-x · DOI
  15. Chen, 2019, Detection of antimicrobial resistance using proteomics and the comprehensive antibiotic resistance database: a case study, Proteomics Clin. Appl.
  16. Armengaud, 2016, Next-generation proteomics faces new challenges in environmental biotechnology, Curr. Opin. Biotechnol., 38, 174, 10.1016/j.copbio.2016.02.025 · DOI
  17. Hartmann, 2014, Taking the shortcut for high-throughput shotgun proteomic analysis of bacteria, Methods Mol. Biol., 1197, 275, 10.1007/978-1-4939-1261-2_16 · DOI
  18. Ludwig, 2018, Comparison of In-Solution, FASP, and S-Trap based digestion methods for bottom-up proteomic studies, J. Proteome Res., 17, 2480, 10.1021/acs.jproteome.8b00235 · DOI
  19. Wisniewski, 2019, Filter aided sample preparation - a tutorial, Anal. Chim. Acta, 1090, 23, 10.1016/j.aca.2019.08.032 · DOI
  20. Zougman, 2014, Suspension trapping (STrap) sample preparation method for bottom-up proteomics analysis, Proteomics, 14, 10.1002/pmic.201300553 · DOI
  21. Hughes, 2014, Ultrasensitive proteome analysis using paramagnetic bead technology, Mol. Syst. Biol., 10, 757, 10.15252/msb.20145625 · DOI
  22. Hughes, 2019, Single-pot, solid-phase-enhanced sample preparation for proteomics experiments, Nat. Protoc., 14, 68, 10.1038/s41596-018-0082-x · DOI
  23. Hayoun, 2019, Evaluation of sample preparation methods for fast proteotyping of microorganisms by tandem mass spectrometry, Front. Microbiol., 10, 1985, 10.3389/fmicb.2019.01985 · DOI
  24. Dayon, 2014, Comprehensive and scalable highly automated MS-based proteomic workflow for clinical biomarker discovery in human plasma, J. Proteome Res., 13, 3837, 10.1021/pr500635f · DOI
  25. Humphrey, 2018, High-throughput and high-sensitivity phosphoproteomics with the EasyPhos platform, Nat. Protoc., 13, 1897, 10.1038/s41596-018-0014-9 · DOI
  26. Potriquet, 2017, A modified FASP protocol for high-throughput preparation of protein samples for mass spectrometry, PLoS One, 12, 10.1371/journal.pone.0175967 · DOI
  27. Yu, 2017, Quick 96FASP for high throughput quantitative proteome analysis, J. Proteome, 166, 1, 10.1016/j.jprot.2017.06.019 · DOI
  28. HaileMariam, 2018, S-trap, an ultrafast sample-preparation approach for shotgun proteomics, J. Proteome Res., 17, 2917, 10.1021/acs.jproteome.8b00505 · DOI
  29. Dagley, 2019, Universal Solid-Phase Protein Preparation (USP(3)) for Bottom-up and Top-down Proteomics, J. Proteome Res., 18, 2915, 10.1021/acs.jproteome.9b00217 · DOI
  30. Gonzalez-Lozano, 2019, A fast and economical sample preparation protocol for interaction proteomics analysis, Proteomics, 19, 10.1002/pmic.201900027 · DOI
  31. Müller, 2020, Automated sample preparation with SP3 for low-input clinical proteomics, Mol. Syst. Biol., 16, 10.15252/msb.20199111 · DOI
  32. Klein, 2016, RNA-binding proteins are a major target of silica nanoparticles in cell extracts, Nanotoxicology, 10, 1555, 10.1080/17435390.2016.1244299 · DOI
  33. Trapp, 2018, Digging deeper into the pyriproxyfen-response of the amphipod gammarus fossarum with a next-generation ultra-high-field orbitrap analyser: new perspectives for environmental toxicoproteomics, Front. Environ. Sci., 6
  34. Hosp, 2015, A double-barrel liquid chromatography-tandem mass spectrometry (LC-MS/MS) system to quantify 96 interactomes per day, Mol. Cell. Proteomics, 14, 2030, 10.1074/mcp.O115.049460 · DOI
  35. Rodriguez-Sanchez, 2019, Review of the impact of MALDI-TOF MS in public health and hospital hygiene, 2018, Euro. Surveill., 24, 10.2807/1560-7917.ES.2019.24.4.1800193 · DOI
  36. Singhal, 2015, MALDI-TOF mass spectrometry: an emerging technology for microbial identification and diagnosis, Front. Microbiol., 6, 791, 10.3389/fmicb.2015.00791 · DOI
  37. Varghese, 2017, Current challenges in the accurate identification of Streptococcus pneumoniae and its serogroups/serotypes in the vaccine era, J. Microbiol. Methods, 141, 48, 10.1016/j.mimet.2017.07.015 · DOI
  38. Dumolin, 2019, Introducing SPeDE: high-Throughput dereplication and accurate determination of microbial diversity from matrix-assisted laser desorption-ionization time of flight mass spectrometry data, mSystems, 4, 10.1128/mSystems.00437-19 · DOI
  39. Sauget, 2017, Can MALDI-TOF mass spectrometry reasonably type Bacteria?, Trends Microbiol., 25, 447, 10.1016/j.tim.2016.12.006 · DOI · Paper page
  40. Kleiner, 2017, Assessing species biomass contributions in microbial communities via metaproteomics, Nat. Commun., 8, 1558, 10.1038/s41467-017-01544-x · DOI · Paper page

Cited by

Sorted by citations

See all 23

Metadata

Authors
Hayoun, K., Gaillard, J.-C., Pible, O., Alpha-Bazin, B., & Armengaud, J.
Venue
Journal of Proteomics
Publisher
Elsevier BV
Published
2020-08
Volume
226
Pages
103887
ISSN
1874-3919
Cited by
23
References
0
Language
en
Funders
Universitat de les Illes Balears

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: High-throughput proteotyping of bacterial isolates by double barrel chromatography-tandem mass spectrometry based on microplate paramagnetic beads and phylopeptidomics. https://app.cochat.ai/papers/10.1016/j.jprot.2020.103887
The paper
Hayoun, K., Gaillard, J.-C., Pible, O., Alpha-Bazin, B., & Armengaud, J. (2020). High-throughput proteotyping of bacterial isolates by double barrel chromatography-tandem mass spectrometry based on microplate paramagnetic beads and phylopeptidomics. Journal of Proteomics. https://doi.org/10.1016/j.jprot.2020.103887