Evidence map›Paper›PMID 20189825›Full record

ArticleJournal of the American Society for Mass Spectrometry2010

Confident assignment of intact mass tags to human salivary cystatins using top-down Fourier-transform ion cyclotron resonance mass spectrometry.

Christopher M Ryan, Puneet Souda, Frederic Halgand, David T Wong, Joseph A Loo, Kym F Faull, Julian P Whitelegge

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2010. 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
3.8field-weighted citation impact, top 7% of its field
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, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein-species quantitative venomics: looking through a crystal ball.The journal of venomous animals and toxins including tropical diseases · 2017
    Review
  9. Progress in Top-Down Proteomics and the Analysis of Proteoforms.Annual review of analytical chemistry (Palo Alto, Calif.) · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Analysis of intact protein isoforms by mass spectrometry.The Journal of biological chemistry · 2011
    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

7 authors at 2 institutions in 2 countries.

Christopher M RyanThe Pasarow Mass Spectrometry Laboratory, The NPI-Semel Institute for Neuroscience and Human Behavior, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California 90024, USA.
Puneet Souda
Frederic Halgand
David T Wong
Joseph A Loo
Kym F Faull
Julian P Whitelegge
University of California, Los Angeles · USBioénergétique et Ingénierie des Protéines · FR

Funding

UCLA FUNDAMENTAL CLINICAL RESEARCH TRAINING PROGRAMT32DE007296 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WONG, DAVID T · 1996 to 2011
$5.8M
Human Salivary ProteomeU01DE016275 · NIDCR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WONG, DAVID T · 2004 to 2007
$5.5M
High Resolution Hybrid FT-ICR Mass SpectrometerS10RR023045 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2006 to 2006
$1.2M
NCRR NIH HHS S10 RR023045NIDCR NIH HHS T32 DE007296NIDCR NIH HHS T32 DE07296-13NIDCR NIH HHS U01 DE016275NIDCR NIH HHS U01 DE016275-01
6 · The paper itself

Abstract

A hybrid linear ion-trap Fourier-transform ion cyclotron resonance mass spectrometer was used for top-down characterization of the abundant human salivary cystatins, including S, S1, S2, SA, SN, C, and D, using collisionally activated dissociation (CAD) after chromatographic purification of the native, disulfide intact proteins. Post-translational modifications and protein sequence polymorphisms arising from single nucleotide polymorphisms (SNPs) were assigned from precursor and product ion masses at a tolerance of 10 ppm, allowing confident identification of individual intact mass tags. Cystatins S, S1, S2, SA, and SN were cleaved of a N-terminal 20 amino acid signal peptide and cystatin C a 26-residue peptide, to yield a generally conserved N-terminus. In contrast, cystatin D isoforms with 24 and 28 amino acid residue N-terminal truncations were found such that their N-termini were not conserved. Cystatin S1 was phosphorylated at Ser3, while S2 was phosphorylated at Ser1 and Ser3, in agreement with previous work. Both cystatin D isoforms carried the polymorphism C46R (SNP: rs1799841). The 14,328 Da isoform of cystatin SN previously assigned with polymorphism P31L due to a SNP (rs2070856) was found only in whole saliva. Parotid secretions contained no detectable cystatins while whole saliva largely mirrored the contents of submandibular/sublingual (SMSL) secretions. With fully characterized cystatin intact mass tags it will now be possible to examine the correlation between the abundance of these molecules and human health and disease.

Indexed as

Amino Acid SequenceChromatography, Reverse-PhaseFourier AnalysisHumansMass SpectrometryMolecular Sequence DataPolymorphism, Single NucleotideProtein IsoformsProtein Processing, Post-TranslationalSalivaSalivary CystatinsSalivary GlandsSequence AlignmentProtein IsoformsSalivary Cystatins

Identifiers

PMID20189825
PMCPMC2873128
OpenAlexW2084705753

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.