Evidence map›Paper›PMID 20428524›Full record

ReviewMolecular bioSystems2010

Analysis of mouse brain peptides using mass spectrometry-based peptidomics: implications for novel functions ranging from non-classical neuropeptides to microproteins.

Lloyd D Fricker

Open access · greenAbstract readReview
In one paragraph

Review in Molecular bioSystems, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 4% 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

77 citing papers in PubMed, 1 synthesis or guideline pooled it, 152 citations in OpenAlex.

  1. Limitations of Mass Spectrometry-Based Peptidomic Approaches.Journal of the American Society for Mass Spectrometry · 2015
    Pooled it
  2. Trial
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Quantitative Peptidomics: General Considerations.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  11. Neuropeptidomics of Genetically Defined Cell Types in Mouse Brain.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  12. Current Challenges and Future Directions in Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  13. Peptidomics of Zebrafish Brain in a 6-OHDA-Induced Neurodegeneration Model.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  14. Origins, Technological Advancement, and Applications of Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

17 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Lloyd D FrickerDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA. lloyd.fricker@einstein.yu.edu
Albert Einstein College of Medicine · US

Funding

REGULATION OF ENKEPHALIN CONVERTASE--CARBOXYPEPTIDASE ER01DA004494 · NIDA · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1987 to 2015
$5.9M
NIDA NIH HHS DA-04494NIDA NIH HHS R01 DA004494
6 · The paper itself

Abstract

Peptides are known to play many important physiological roles in signaling. A large number of peptides have been detected in mouse brain extracts using mass spectrometry-based peptidomics studies, and 850 peptides have been identified. Half of these peptides are derived from secretory pathway proteins and many are known bioactive neuropeptides which activate G protein-coupled receptors; these are termed "classical neuropeptides". In addition, 427 peptides were identified that are derived from non-secretory pathway proteins; the majority are cystosolic, and the remainder are mitochondrial, nuclear, lysosomal, or membrane proteins. Many of these peptides represent the N- or C-terminus of the protein, rather than internal fragments, raising the possibility that they are formed by selective processing rather than protein degradation. In addition to consideration of the cleavage site required to generate the intracellular peptides, their potential functions are discussed. Several of the cytosolic peptides were previously found to interact with receptors and/or otherwise influence cellular activity; examples include hemorphins, hemopressins, diazepam binding inhibitor, and hippocampal cholinergic neurostimulating peptide. The possibility that these peptides are secreted from cells and function in cell-cell signaling is discussed. If these intracellular peptides can be shown to be secreted in levels sufficient to produce a biological effect, they would appropriately be called "non-classical neuropeptides" by analogy with non-classical neurotransmitters such as nitric oxide and anandamide. It is also possible that intracellular peptides function as "microproteins" and modulate protein-protein interactions; evidence for this function is discussed, along with future directions that are needed to establish this and other possible functions for peptides.

Indexed as

AnimalsMass SpectrometryMiceModels, BiologicalMolecular WeightNeuropeptidesProteinsProteomicsSecretory PathwayNeuropeptidesProteins

Identifiers

PMID20428524
PMCPMC2902593
OpenAlexW2117039580

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.