MassIVE MSV000099803

Partial Public PXD070503

Global profiling of post-translationally modified crustacean neuropeptidome trends affiliated with feeding activity

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Description

Neuropeptides modulate a diverse range of physiological functions, such as those associated with feeding. Post-translational modifications (PTMs) are responsible for much of the dynamic nature of neuropeptide isoforms for varied influence on these functions. Mass spectrometry is the gold standard analytical technique for peptidomic analyses, followed by computational methods for peptide identification. However, the computational search space quickly becomes difficult to manage as more modifications are considered. With innovative approaches to endless combinations of potential modifications, such as the PEAKS PTM, we globally profiled the Cancer borealis (Jonah crab) neuropeptidome to investigate the role of PTMs in feeding and appetite related processes across time. Through deep examination of several notable modifications, we were able to propose PTM-associated motifs for neuropeptides, which can bolster future identification abilities. Furthermore, this work revealed neuropeptides which were characteristically modified depending on the crab feeding status and the time post-feeding, pointing to potential biological significance. This is the first large-scale investigation of the modified crustacean neuropeptidome, revealing new insights on the implications of modifications in biological regulation. [doi:10.25345/C59W09C2W] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Neuropeptides ; Post translational modifications ; DatasetType:Proteomics

Contact

Principal Investigators:
(in alphabetical order) 		Lingjun Li, University of Wisconsin-Madison, United States
Submitting User: lfields
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Number of distinct biological replicates across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct technical replicates across all analyses (original submission and reanalyses) associated with this dataset.

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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Number of distinct protein accessions reported across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct unmodified peptide sequences reported across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct peptide sequences (including modified variants or peptidoforms) reported across all analyses (original submission and reanalyses) associated with this dataset.

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Total number of peptide-spectrum matches (i.e. spectrum identifications) reported across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct proteins quantified across all analyses (original submission and reanalyses) associated with this dataset.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

A protein is differentially abundant if its change in abundance across conditions is found to be statistically significant with an adjusted p-value <= 0.05 and lists no issues associated with statistical tests for differential abundance.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

"N/A" means no results of this type were submitted.
This dataset may not contain all raw spectra data as originally deposited in PRIDE. It has been imported to MassIVE for reanalysis purposes, so its spectra data here may consist solely of processed peak lists suitable for reanalysis with most software.