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              <creatorName>Petzold, Axel</creatorName>
              <givenName>Axel</givenName>
              <familyName>Petzold</familyName>
              <nameIdentifier nameIdentifierScheme="ORCID" schemeURI="http://orcid.org">0000-0002-0344-9749</nameIdentifier>
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          <titles>
            <title><![CDATA[<b>Visinin-like protein 1 Degradome Foundation Atlas</b>]]></title>
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          <subjects>
            <subject>Applications in health</subject>
            <subject>Other chemical sciences not elsewhere classified</subject>
            <subject>Analytical biochemistry</subject>
            <subject>Computational neuroscience (incl. mathematical neuroscience and theoretical neuroscience)</subject>
            <subject>VILIP</subject>
            <subject>vilip1</subject>
            <subject>vilip-1-expression</subject>
            <subject>visinin-like protein-1</subject>
            <subject>VISININ-LIKE PROTEIN-1</subject>
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          <dates>
            <date dateType="Created">2026-04-20</date>
            <date dateType="Updated">2026-04-21</date>
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          <resourceType resourceTypeGeneral="Dataset">Dataset</resourceType>
          <publicationYear>2026</publicationYear>
          <publisher>University College London</publisher>
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            <description descriptionType="Abstract"><![CDATA[<p dir="ltr">The VILIP-1 Degradome Foundation Atlas (Version 1) is an open-access, fully reproducible reference dataset that provides the first comprehensive <i>in silico</i> reconstruction of the proteolytic degradome of Visinin-like protein-1 (VILIP-1), a neuronal calcium-sensor protein encoded by <i>VSNL1</i>. VILIP-1 participates in intracellular calcium signalling and contributes to neuronal survival, synaptic plasticity, and intracellular signalling pathways. Elevated concentrations of VILIP-1 have been reported in neurodegenerative disorders, where the protein has been investigated as a biomarker of neuronal injury and synaptic dysfunction.</p><p dir="ltr">Proteins undergoing physiological turnover and stress-related modification generate complex populations of proteolytic fragments. The potential repertoire of VILIP-1-derived peptides has not previously been systematically characterized. The VILIP-1 Degradome Foundation Atlas addresses this gap by enumerating the theoretical peptide landscape that can arise from proteolytic and chemical cleavage of the VILIP-1 primary sequence.</p><p dir="ltr">Each predicted fragment is annotated with a rich panel of physicochemical and biochemical properties relevant to proteomics, biomarker discovery, and computational peptide analysis.</p><p><br></p><p><br></p>Scope and Content<p dir="ltr">The dataset comprises every predicted proteolytic fragment derived from the human VILIP-1 primary sequence based on defined cleavage boundaries. The resulting fragment space includes overlapping peptides spanning the entire protein sequence.</p><p dir="ltr">For each peptide, the dataset provides:</p><ul><li>Peptide identifier and coordinates (start and stop positions)</li><li>Amino acid sequence</li><li>Calculated mass-to-charge ratio (m/z)</li><li>Molecular weight (Da)</li><li>Boman index</li><li>Net charge</li><li>Isoelectric point (pI)</li><li>Hydrophobicity</li><li>Instability index</li><li>Aliphatic index</li></ul><p dir="ltr">These features provide a unified, feature-rich representation suitable for mass-spectrometry analysis, biomarker discovery, and computational proteomics workflows.</p><p><br></p><p><br></p>Methods Summary<p dir="ltr">The Degradome Atlas was generated using a reproducible Python workflow:</p><ol><li>Definition of cleavage sites<br>Experimentally reported and computationally defined cleavage positions were specified along the full-length VILIP-1 amino-acid sequence.</li><li>Fragment enumeration<br>All pairwise subsequences between cleavage boundaries were generated, producing the complete theoretical fragment space of the protein.</li><li>Peptide property calculation<br>Physicochemical properties were calculated using the <i>peptides</i> Python library.</li><li>Structured data export<br>All peptide information was exported as structured CSV files.</li><li>Dataset consolidation<br>Output files were merged and compressed into a single FAIR-compliant archive (TAR.XZ format) to facilitate efficient distribution and reproducibility.</li></ol><p dir="ltr">The complete Python workflow is included in the repository to enable transparent re-execution and extension to additional proteins or sequence variants.</p><p><br></p><p><br></p>Data Format and Access<p dir="ltr">Primary file:<br>VILIP1_Degradome_Foundation_Atlas_v1.tar.xz</p><p dir="ltr">Contents</p><ul><li>CSV tables containing all predicted peptide fragments and calculated properties</li><li>Python scripts used to generate the degradome dataset</li><li>Documentation describing the workflow and dataset structure</li></ul><p dir="ltr">File Type:<br>ASCII comma-separated values (CSV)</p><p dir="ltr">Compression:<br><code>xz -9 -T0</code> (maximum parallel compression for efficient distribution)</p><p dir="ltr">Compatibility</p><p dir="ltr">The dataset can be used directly in:</p><ul><li>Python (pandas, NumPy)</li><li>R</li><li>MATLAB</li><li>SAS</li><li>Excel / LibreOffice</li></ul><p dir="ltr">It can also be integrated into proteomics workflows, including:</p><ul><li>Skyline</li><li>MaxQuant preprocessing</li><li>MS/MS spectral library construction</li><li>computational peptide modelling pipelines</li></ul><p dir="ltr"><br></p>FAIR Principles<p dir="ltr">This dataset follows FAIR data principles:</p><p dir="ltr"><b>Findable</b><br>Rich metadata, persistent DOI, and search-optimized dataset description.</p><p dir="ltr"><b>Accessible</b><br>Publicly available through present open-access Figshare repository.</p><p dir="ltr"><b>Interoperable</b><br>Standard CSV format and widely used physicochemical descriptors.</p><p dir="ltr"><b>Reusable</b><br>Fully reproducible Python workflow and transparent data generation pipeline.</p><p><br></p><p><br></p>Applications<p dir="ltr">The VILIP-1 Degradome Foundation Atlas enables research across several biomedical and computational domains:</p><ul><li>Biomarker discovery in neurodegenerative disease</li><li>Mass-spectrometry assay development</li><li>Computational proteomics and peptide modelling</li><li>Neo-epitope discovery and immunological studies</li><li>Proteolytic pathway analysis</li><li>Systems-level degradomics</li></ul><p dir="ltr">The dataset may also serve as a reference framework for interpreting peptide-level signals detected in cerebrospinal fluid or blood proteomic studies.</p><p><br></p><p><br></p>Versioning and Future Work<p dir="ltr">This release represents Version 1 of the VILIP-1 Degradome Foundation Atlas.</p><p dir="ltr">Future updates will incorporate:</p><ul><li>additional experimentally validated cleavage sites</li><li>disease-associated sequence variants of VILIP-1</li><li>experimentally detected peptide fragments</li><li>integration with other degradome atlases to support systems-level biomarker research</li></ul><p dir="ltr">These developments will progressively refine modelling of VILIP-1 proteolysis in health and neurodegenerative disease.</p><p><br></p><p><br></p>Citation<p dir="ltr">If you use this dataset, please cite the associated Figshare <b><u>DOI:10.5522/04/32054535</u></b></p><p dir="ltr"><br></p><p dir="ltr">and:</p><p dir="ltr">Petzold A. Proteolysis-Based Biomarker Repertoires in Protein Degradomics.<br><i>Journal of Neurochemistry.</i> 2025;169(3):e70023.<br>doi:10.1111/jnc.70023</p>]]></description>
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