Evidence map›Paper›PMID 24687996›Full record

ArticleProteomics2014

Top-down tandem mass spectrometry on RNase A and B using a Qh/FT-ICR hybrid mass spectrometer.

Sandrine Bourgoin-Voillard, Nancy Leymarie, Catherine E Costello

Abstract read
In one paragraph

Article in Proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  3. Article
  4. Review
  5. Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Paucimannose-RichMolecular & cellular proteomics : MCP · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
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

3 authors.

Sandrine Bourgoin-VoillardCenter for Biomedical Mass Spectrometry, Boston University School of Medicine, Boston, MA, USA.
Nancy Leymarie
Catherine E Costello

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
LTQ-FT MS System for On-line Protein and Glycan AnalysisS10RR025082 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2009 to 2009
$1.3M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
NCRR NIH HHS P41 RR010888NCRR NIH HHS S10 RR025082NHLBI NIH HHS HHSN268201000031CNHLBI NIH HHS N01 HV028178NIGMS NIH HHS GM104603NIGMS NIH HHS P41 GM104603
6 · The paper itself

Abstract

Protein characterization using top-down approaches emerged with advances in high-resolution mass spectrometers and increased diversity of available activation modes: collision-induced dissociation (CID), infrared multiphoton dissociation (IRMPD) electron capture dissociation (ECD), and electron transfer dissociation (ETD). Nevertheless, top-down approaches are still rarely used for glycoproteins. Hence, this work summarized the capacity of top-down approaches to improve sequence coverage and glycosylation site assignment on the glycoprotein Ribonuclease B (RNase B). The glycan effect on the protein fragmentation pattern was also investigated by comparing the fragmentation patterns of RNase B and its nonglycosylated analog RNase A. The experiments were performed on a Bruker 12-T Qh/FT-ICR SolariX mass spectrometer using vibrational (CID/IRMPD) and radical activation (ECD/ETD) with/without pre- or post-activation (IRMPD or CID, respectively). The several activation modes yielded complementary sequence information. The radical activation modes yielded the most extensive sequence coverage that was slightly improved after a CID predissociation activation event. The combination of the data made it possible to obtain 90% final sequence coverage for RNase A and 86% for RNase B. Vibrational and radical activation modes showed high retention of the complete glycan moiety (>98% for ETD and ECD) facilitating unambiguous assignment of the high-mannose glycosylation site. Moreover, the presence of the high-mannose glycan enhanced fragmentation around the glycosylation site.

Indexed as

Amino Acid SequenceAnimalsCattleGlycoproteinsMolecular Sequence DataPeptide FragmentsProteomicsRibonuclease, PancreaticRibonucleasesTandem Mass SpectrometryGlycoproteinsPeptide Fragmentsribonuclease BRibonuclease, PancreaticRibonucleasesCollision-induced dissociation (CID)Electron capture dissociation (ECD)Electron transfer dissociation (ETD)GlycoproteomicsInfrared multiphoton dissociation (IRMPD)

Identifiers

PMID24687996
PMCPMC4095805

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.