Bridging Neuropeptidomics and Genomics with Bioinformatics: Prediction of Mammalian Neuropeptide Prohormone Processing
- 13 April 2006
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Proteome Research
- Vol. 5 (5) , 1162-1167
- https://doi.org/10.1021/pr0504541
Abstract
Neuropeptides are an important class of cell to cell signaling molecules that are difficult to predict from genetic information because of their large number of post-translational modifications. The transition from prohormone genetic sequence information to the determination of the biologically active neuropeptides requires the identification of the cleaved basic sites, among the many possible cleavage sites, that exist in the prohormone. We report a binary logistic regression model trained on mammalian prohormones that is more sensitive than existing methods in predicting these processing sites, and demonstrate the application of this method to mammalian neuropeptidomic studies. By comparing the predictive abilities of a binary logistic model trained on molluscan prohormone cleavages with the reported model, we establish the need for phyla-specific models. Keywords: neuropeptide • prohormone processing prediction • binary logistic regression • statistical methods • mammalian prohormonesKeywords
This publication has 27 references indexed in Scilit:
- Discovering new invertebrate neuropeptides using mass spectrometryMass Spectrometry Reviews, 2005
- Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two‐dimensional capillary liquid chromatography quadrupole time‐of‐flight mass spectrometryJournal of Mass Spectrometry, 2005
- Discovery and Neurochemical Screening of Peptides in Brain Extracellular Fluid by Chemical Analysis of in Vivo Microdialysis SamplesAnalytical Chemistry, 2004
- Miniaturized proteomics and peptidomics using capillary liquid separation and high resolution mass spectrometryFEBS Letters, 2004
- Prediction of proprotein convertase cleavage sitesProtein Engineering, Design and Selection, 2004
- Identification and Characterization of a Novel RF-amide Peptide Ligand for Orphan G-protein-coupled Receptor SP9155Journal of Biological Chemistry, 2003
- Role of Amino Acid Sequences Flanking Dibasic Cleavage Sites in Precursor Proteolytic Processing. The Importance of the First Residue C-Terminal of the Cleavage SiteEuropean Journal of Biochemistry, 1995
- Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathwayFEBS Letters, 1993
- Consensus sequence for processing of peptide precursors at monobasic sitesFEBS Letters, 1991
- The processing of peptide precursorsFEBS Letters, 1986