Evidence map›Paper›PMID 19222238›Full record

ArticleJournal of proteome research2009

Expanding the Crustacean neuropeptidome using a multifaceted mass spectrometric approach.

Mingming Ma, Junhua Wang, Ruibing Chen, Lingjun Li

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
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  6. Article
  7. PRESnovo: Prescreening Prior toJournal of the American Society for Mass Spectrometry · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Exploring the Sea Urchin Neuropeptide Landscape by Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018
    Article
  13. Identification, Quantitation, and Imaging of the Crustacean Peptidome.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  14. The State of "Frontiers in genetics · 2018
    Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Trypsin isozymes in the lobster Panulirus argus (Latreille, 1804): from molecules to physiology.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2015
    Review
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

4 authors at 1 institution in 1 country.

Mingming MaSchool of Pharmacy and Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53705-2222, USA.
Junhua Wang
Ruibing Chen
Lingjun Li
University of Wisconsin–Madison · US

Funding

Mass Spectrometric Studies of Neuropeptides in FeedingR01DK071801 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI LINGJUN LI · 2006 to 2026
$6.7M
NIDDK NIH HHS 1R01DK071801NIDDK NIH HHS R01 DK071801
6 · The paper itself

Abstract

Jonah crab Cancer borealis is an excellent, long-served model organism for many areas of physiology, including the study of endocrinology and neurobiology. Characterizing the neuropeptides present in its nervous system provides the first critical step toward understanding the physiological roles of these complex molecules. Multiple mass spectral techniques were used to comprehensively characterize the neuropeptidome in C. borealis, including matrix-assisted laser desorption/ionization Fourier transform mass spectrometry (MALDI-FTMS), MALDI time-of-flight (TOF)/TOF MS and nanoflow liquid chromatography coupled with electrospray ionization quadrupole time-of-flight tandem mass spectrometry (nanoLC-ESI-Q-TOF MS/MS). To enhance the detection signals and expand the dynamic range, direct tissue analysis, tissue extraction, capillary electrophoresis (CE) and off-line HPLC separation have also been employed. In total, 142 peptides were identified, including 85 previously known C. borealis peptides, 22 peptides characterized previously from other decapods, but new to this species, and 35 new peptides de novo sequenced for the first time in this study. Seventeen neuropeptide families were revealed including FMRFamide-related peptide (FaRP), allatostatin (A and B type), RYamide, orcokinin, orcomyotropin, proctolin, crustacean cardioactive peptide (CCAP), crustacean hyperglycemic hormone precursor-related peptide (CPRP), crustacean hyperglycemic hormone (CHH), corazonin, pigment-dispersing hormone (PDH), tachykinin, pyrokinin, SIFamide, red pigment concentrating hormone (RPCH) and HISGLYRamide. Collectively, our results greatly increase the number and expand the coverage of known C. borealis neuropeptides, and thus provide a stronger framework for future studies on the physiological roles played by these molecules in this important model organism.

Indexed as

AnimalsBrachyuraChromatography, High Pressure LiquidMass SpectrometryNeuropeptidesProtein IsoformsProteomicsSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationNeuropeptidesProtein Isoforms

Identifiers

PMID19222238
PMCPMC2692460
OpenAlexW2023029465

What OpenQuestion holds

Textmetadata
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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.