Evidence map›Paper›PMID 19911840›Full record

ArticleBiochemistry2009

Peptidomics of prolyl endopeptidase in the central nervous system.

Whitney M Nolte, Debarati M Tagore, William S Lane, Alan Saghatelian

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Screening Trimethoprim Primary Metabolites for Covalent Binding to Albumin.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2020
    Article
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  7. Review
  8. Article
  9. Article
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  11. Article
  12. Recent advances in quantitative neuroproteomics.Methods (San Diego, Calif.) · 2013
    Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
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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 2 institutions in 1 country.

Whitney M NolteDepartment of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.
Debarati M Tagore
William S Lane
Alan Saghatelian
Harvard University · USCenter for Systems Biology · US

Funding

Training in Molecular, Cellular, and Chemical BiologyT32GM007598 · NIGMS · HARVARD UNIVERSITY · PI DULAC, CATHERINE · 1985 to 2019
$16.2M
Discovery metabolite profiling of the prolyl peptidasesDP2OD002374 · OD · HARVARD UNIVERSITY · PI SAGHATELIAN, ALAN · 2007 to 2009
$2.6M
NIGMS NIH HHS T32 GM007598NIGMS NIH HHS T32GM07598NIH HHS 1DP2OD002374NIH HHS DP2 OD002374
6 · The paper itself

Abstract

Prolyl endopeptidase (Prep) is a member of the prolyl peptidase family and is of interest because of its unique biochemistry and connections to cognitive function. Using an unbiased mass spectrometry (MS)-based peptidomics platform, we identified Prep-regulated peptides in the central nervous system (CNS) of mice by measuring changes in the peptidome as a function of Prep activity. This approach was validated by the identification of known Prep substrates, such as the neuropeptide substance P and thymosin-beta4, the precursor to the bioactive peptide Ac-SDKP. In addition to these known substrates, we also discovered that Prep regulates many additional peptides, including additional bioactive peptides and proline rich peptides (PRPs). Biochemical experiments confirmed that some of these Prep-regulated peptides are indeed substrates of the enzyme. Moreover, these experiments also supported the known preference of Prep for shorter peptides while revealing a previously unknown cleavage site specificity of Prep when processing certain multi-proline-containing peptides, including PRPs. The discovery of Prep-regulated peptides implicates Prep in new biological pathways and provides insights into the biochemistry of this enzyme.

Indexed as

Amino Acid SequenceAnimalsAzabicyclo CompoundsCalcitonin Gene-Related PeptideChlorocebus aethiopsChromatography, LiquidCOS CellsMiceMice, Inbred C57BLMolecular Sequence DataPeptidesProlyl OligopeptidasesProteomicsSerine EndopeptidasesSerine Proteinase InhibitorsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAzabicyclo CompoundsCalcitonin Gene-Related PeptidePeptidesProlyl OligopeptidasesSerine EndopeptidasesSerine Proteinase Inhibitors

Identifiers

PMID19911840
PMCPMC2813186
OpenAlexW2017525042

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.