ReviewThe AAPS journal2010
Peptidomics of the prolyl peptidases.
Review in The AAPS journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Limitations of Mass Spectrometry-Based Peptidomic Approaches.Journal of the American Society for Mass Spectrometry · 2015Pooled it
- Fibroblast activation protein: Pivoting cancer/chemotherapeutic insight towards heart failure.Biochemical pharmacology · 2024Review
- Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.Protein science : a publication of the Protein Society · 2024Article
- Article
- An Efficient Peptidomics Screening for Exogenous Substrates and Inhibitory Peptides of the Dipeptidase ACE from Milk Hydrolysate.Pharmaceutics · 2023Article
- Dipeptidyl Peptidase 4 (DPP4) as A Novel Adipokine: Role in Metabolism and Fat Homeostasis.Biomedicines · 2022Review
- Distinctive Metabolomics Patterns Associated With Insulin Resistance and Type 2 Diabetes Mellitus.Frontiers in molecular biosciences · 2020Article
- What doesn't kill you makes you stranger: Dipeptidyl peptidase-4 (CD26) proteolysis differentially modulates the activity of many peptide hormones and cytokines generating novel cryptic bioactive ligands.Pharmacology & therapeutics · 2019Review
- Role of dipeptidyl peptidase-4 as a potentiator of activin/nodal signaling pathway.BMB reports · 2018Article
- The Neuromuscular Junction and Wide Heterogeneity of Congenital Myasthenic Syndromes.International journal of molecular sciences · 2018Review
- Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.Nature communications · 2017Article
- Mechanism of Action of Prolyl Oligopeptidase (PREP) in Degenerative Brain Diseases: Has Peptidase Activity Only a Modulatory Role on the Interactions of PREP with Proteins?Frontiers in aging neuroscience · 2017Article
- Article
- The Role of Dipeptidyl Peptidase - 4 Inhibitors in Diabetic Kidney Disease.Frontiers in immunology · 2015Review
- Inherited disorders of the neuromuscular junction: an update.Journal of neurology · 2014Review
- Ortleppascaris sp. and your host Rhinella marina: A proteomic view into a nematode-amphibian relationship.International journal for parasitology. Parasites and wildlife · 2014Article
- A monoclonal antibody (MCPR3-7) interfering with the activity of proteinase 3 by an allosteric mechanism.The Journal of biological chemistry · 2013Article
- Article
- Fishing for the hidden peptidome in health and disease (drug abuse).The AAPS journal · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prolyl peptidases are a family of enzymes characterized by a biochemical preference for cleaving proline-containing peptides. The members of this enzyme family include prolyl endopeptidase, prolyl endopeptidase-like, dipeptidyl peptidase 4 (DPP4), DPP7, DPP8, DPP9, and fibroblast activation protein. DPP4 is the best studied member of the family, due to its role in physiological glucose tolerance, exerted through the regulation of the insulinotropic peptide glucagon-like peptide-1. While other members of the prolyl peptidase family have also been implicated in various (patho)physiological processes, the underlying peptides and pathways regulated by these enzymes are less clear. The identification of endogenous substrates of the prolyl peptidases is an important step in elucidating the molecular mechanisms of these enzymes. Here, we highlight the utility of liquid chromatography-mass spectrometry-based peptidomics to enable the discovery of endogenous prolyl peptidase substrates directly from tissues, and demonstrate the utility of this information in understanding the biochemical and physiological functions of the prolyl peptidases.
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What OpenQuestion holds
Registered trials
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.