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oai:figshare.com:article/34054953 2026-10-02T08:43:55Z category_25270 category_24748 category_24829 portal_549 item_type_3 month_year_10_2026

Lamin-B2 Degradome Foundation Atlas Axel Petzold (7076261) Theoretical and computational chemistry not elsewhere classified Neurosciences not elsewhere classified Ophthalmology and optometry not elsewhere classified progressive myoclonus epilepsy microcephaly with brain malformations acquired partial lipodystrophy Barraquer-Simons syndrome neuronal migration cortical lamination This Figshare repository hosts the Lamin-B2 Degradome Foundation Atlas (Version 1), a comprehensive in silico reconstruction of the theoretical peptide landscape generated through the proteolytic cleavage of human Lamin-B2 (LMNB2).The atlas provides an open-access computational reference for researchers working in proteomics, degradomics, mass spectrometry, nuclear biology, cell biology, developmental biology, and biomarker discovery. By systematically mapping potential peptide fragments arising from Lamin-B2 turnover and enzymatic processing, the dataset provides a degradome-centred perspective on the dynamic peptide populations that may be generated during nuclear protein turnover, cell-cycle progression, cellular differentiation, and disease-associated cellular remodeling.<h2 dir="ltr">Biological Context</h2>Lamin-B2, encoded by LMNB2, is a type V intermediate filament protein and a major component of the nuclear lamina. Together with Lamin-B1 and other nuclear lamins, Lamin-B2 forms part of the structural network underlying the inner nuclear membrane and contributes to the organization, mechanical stability, and functional integrity of the nucleus.Lamin-B2 is expressed broadly across human tissues and has important roles in nuclear architecture, nuclear envelope organization, chromatin interactions, and cell-cycle progression. Its association with the nuclear envelope and its dynamic behavior during mitosis make Lamin-B2 an important component of the cellular machinery governing nuclear disassembly and reassembly.Proteolytic processing and turnover of nuclear lamins can generate peptide fragments that may provide molecular information distinct from measurements of the intact protein. Mapping the theoretical Lamin-B2 fragment landscape therefore provides a foundation for investigating LMNB2-derived peptides as potential indicators of nuclear protein turnover, cellular state, and pathological nuclear remodeling.Alterations in Lamin-B2 biology have been investigated in developmental and neurological contexts, as well as in processes involving cellular proliferation and differentiation. Genetic alterations in LMNB2 have been associated with rare neurological disorders, highlighting the importance of Lamin-B2 in maintaining normal nuclear organization and cellular function.<h3 dir="ltr">Key Features of the Proteomics Dataset</h3>The Lamin-B2 Degradome Foundation Atlas provides a systematic computational representation of the theoretical peptide space associated with LMNB2, including:<ul><li>Predicted enzymatic and chemical cleavage sites across the Lamin-B2 sequence</li><li>Potential contiguous peptide fragments generated through proteolytic cleavage</li><li>Fragment-level physicochemical and biochemical characteristics</li><li>Sequence-derived properties relevant to peptide characterization and mass-spectrometric detection</li></ul>Mass Spectrometry and Peptide Metrics:<ul><li>Molecular weight</li><li>Mass-to-charge ratio (m/z)</li><li>Net charge</li><li>Isoelectric point (pI)</li></ul>Biochemical and Biophysical Features:<ul><li>Hydrophobicity</li><li>Boman index</li><li>Instability index</li><li>Aliphatic index</li></ul>Together, these calculated parameters provide a feature-rich computational reference for evaluating LMNB2-derived peptides and prioritizing candidate fragments for downstream proteomic and mass-spectrometric investigation.<h3 dir="ltr">Applications in Biomarker Discovery and Biomedical Research</h3>The dataset can support a broad range of research applications, including:<ul><li>Targeted Proteomics: Identification and prioritization of LMNB2-derived peptides for targeted mass-spectrometry assays.</li><li>Biomarker Discovery: Exploration of Lamin-B2-derived peptide signatures associated with nuclear protein turnover, cellular remodeling, and disease-associated processes.</li><li>Discovery Proteomics: Generation of candidate peptide lists for untargeted and discovery-based proteomic investigations.</li><li>Degradomics: Investigation of Lamin-B2 proteolytic processing and nuclear protein turnover through a protein-specific degradome framework.</li><li>Clinical Proteomics: Identification of candidate peptide biomarkers associated with nuclear and cellular changes.</li><li>Nuclear Biology: Supporting studies of nuclear lamina organization, nuclear envelope integrity, and chromatin-associated nuclear architecture.</li><li>Cell-Cycle Research: Exploration of LMNB2-derived peptides associated with nuclear envelope disassembly, reassembly, and cell-cycle progression.</li><li>Developmental Biology: Supporting investigations into Lamin-B2 during cellular differentiation and tissue development.</li><li>Neurobiology: Providing a computational resource for studying LMNB2-associated nuclear biology in neural tissues and neurological disease.</li><li>Cell Biology: Investigation of LMNB2-derived peptides in cellular proliferation, differentiation, and stress-associated remodeling.</li><li>Computational Biology: Enabling sequence-based degradome profiling, peptide prioritization, and comparative protein analysis.</li><li>Assay Development: Supporting the selection and characterization of candidate LMNB2 peptides for future experimental validation.</li></ul><h3 dir="ltr">Data Inclusion and Reproducibility</h3>Version 1 focuses on the wild-type human Lamin-B2 protein and provides a systematic theoretical representation of its potential degradome, including contiguous peptide fragments and their calculated physicochemical properties.The dataset represents a theoretical fragment space rather than a catalogue of experimentally confirmed peptides. The presence of a predicted fragment does not establish that the peptide is generated in vivo, remains stable in a biological sample, or is detectable by a particular mass-spectrometric platform. Experimental proteomics, degradomics, and mass-spectrometry studies are therefore required to establish the biological generation, stability, abundance, and detectability of individual LMNB2-derived peptides.Future releases of the Lamin-B2 Degradome Foundation Atlas may incorporate disease-associated sequence variants, post-translational modifications, experimentally validated cleavage products, tissue- and cell-type-specific degradome profiles, and complementary experimental proteomics data. These extensions will progressively bridge the theoretical LMNB2 peptide landscape with experimentally informed models of Lamin-B2 turnover, nuclear architecture, cell-cycle biology, developmental processes, neurobiology, and disease-associated cellular changes. 2026-10-02T08:43:55Z Dataset Dataset 10.5522/04/34054953.v1 https://figshare.com/articles/dataset/Lamin-B2_Degradome_Foundation_Atlas/34054953 CC0