{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T18:14:27Z","timestamp":1789582467923,"version":"build-2803163510"},"reference-count":204,"publisher":"MDPI AG","issue":"16","license":[{"start":{"date-parts":[[2025,8,14]],"date-time":"2025-08-14T00:00:00Z","timestamp":1755129600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Traumatic Brain Injury (TBI) is a major global health concern and a leading cause of death and disability, especially in young adults. It triggers complex secondary injury cascades, e.g., calcium dysregulation, mitochondrial dysfunction and protease activation, that extend well beyond the initial mechanical insult to drive ongoing neurodegeneration. The calcium-dependent protease calpain has emerged as a central mediator of TBI cellular pathology. Calpain cleaves a broad range of cytoskeletal and regulatory proteins across neuronal compartments, disrupting axonal integrity, synaptic function and calcium homeostasis. Despite decades of research, calpain remains an elusive therapeutic target. In this review, we examine the spatial and temporal patterns of calpain activation in the traumatically injured brain, categorize key calpain substrates by structure and location, and assess their mechanistic roles in TBI pathology. We also review recent advances in next-generation calpain-2 selective inhibitors with enhanced specificity and preclinical efficacy and discuss the emerging use of calpain-cleaved protein fragments such as SBDP145 and SNTF as candidate biomarkers for TBI diagnosis and progression. Drawing on molecular, preclinical, and clinical data, we argue that calpain warrants renewed attention as both a therapeutic target and mechanistic biomarker in TBI. It may be time for Cinderella to leave the basement.<\/jats:p>","DOI":"10.3390\/cells14161253","type":"journal-article","created":{"date-parts":[[2025,8,14]],"date-time":"2025-08-14T14:51:46Z","timestamp":1755183106000},"page":"1253","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Calpain in Traumatic Brain Injury: From Cinderella to Central Player"],"prefix":"10.3390","volume":"14","author":[{"given":"Carla","family":"Schallerer","sequence":"first","affiliation":[{"name":"School of Medicine and Health, Technical University of Munich, 81675 Munich, Germany"},{"name":"Department of Pharmacology, Yale School of Medicine, New Haven, CT 06510, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephan","family":"Neuschmid","sequence":"additional","affiliation":[{"name":"School of Medicine and Health, Technical University of Munich, 81675 Munich, Germany"},{"name":"Department of Pharmacology, Yale School of Medicine, New Haven, CT 06510, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9657-9704","authenticated-orcid":false,"given":"Barbara E.","family":"Ehrlich","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Yale School of Medicine, New Haven, CT 06510, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0001-4035-8061","authenticated-orcid":false,"given":"Declan","family":"McGuone","sequence":"additional","affiliation":[{"name":"Department of Pathology, Yale School of Medicine, New Haven, CT 06510, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,8,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1016\/S1474-4422(22)00309-X","article-title":"Traumatic brain injury: Progress and challenges in prevention, clinical care, and research","volume":"21","author":"Maas","year":"2022","journal-title":"Lancet Neurol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/S1474-4422(17)30371-X","article-title":"Traumatic brain injury: Integrated approaches to improve prevention, clinical care, and research","volume":"16","author":"Maas","year":"2017","journal-title":"Lancet Neurol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1093\/brain\/awae350","article-title":"Exploiting blood-based biomarkers to align preclinical models with human traumatic brain injury","volume":"148","author":"Lisi","year":"2024","journal-title":"Brain"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1089\/neu.2008.0586","article-title":"Classification of Traumatic Brain Injury for Targeted Therapies","volume":"25","author":"Saatman","year":"2008","journal-title":"J. Neurotrauma"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Wachtler, N., O\u2019brien, R., Ehrlich, B.E., and McGuone, D. (2025). Exploring Calcium Channels as Potential Therapeutic Targets in Blast Traumatic Brain Injury. Pharmaceuticals, 18.","DOI":"10.3390\/ph18020223"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Weber, J.T. (2012). Altered Calcium Signaling Following Traumatic Brain Injury. Front. Pharmacol., 3.","DOI":"10.3389\/fphar.2012.00060"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1016\/j.bbi.2012.06.008","article-title":"Neuroinflammation after traumatic brain injury: Opportunities for therapeutic intervention","volume":"26","author":"Kumar","year":"2012","journal-title":"Brain Behav. Immun."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.nbd.2013.08.010","article-title":"Role of calpains in the injury-induced dysfunction and degeneration of the mammalian axon","volume":"60","author":"Ma","year":"2013","journal-title":"Neurobiol. Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1089\/neu.1997.14.121","article-title":"Mechanisms of Calpain Proteolysis Following Traumatic Brain Injury: Implications for Pathology and Therapy: A Review and Update","volume":"14","author":"Kampfl","year":"1997","journal-title":"J. Neurotrauma"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1080\/14737159.2018.1428089","article-title":"An update on diagnostic and prognostic biomarkers for traumatic brain injury","volume":"18","author":"Wang","year":"2018","journal-title":"Expert Rev. Mol. Diagn."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1002\/med.21534","article-title":"Involvement of calpain in the neuropathogenesis of Alzheimer\u2019s disease","volume":"39","author":"Mahaman","year":"2018","journal-title":"Med. Res. Rev."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.3233\/JAD-215182","article-title":"Calpain-Mediated Alterations in Astrocytes Before and During Amyloid Chaos in Alzheimer\u2019s Disease","volume":"84","author":"Schultz","year":"2021","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.nurt.2009.11.002","article-title":"Calpain as a Therapeutic Target in Traumatic Brain Injury","volume":"7","author":"Saatman","year":"2010","journal-title":"Neurotherapeutics"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1007\/s13311-023-01407-y","article-title":"Calpain-2 Inhibitors as Therapy for Traumatic Brain Injury","volume":"20","author":"Baudry","year":"2023","journal-title":"Neurotherapeutics"},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Suryavanshi, P., Baule, S., and Glykys, J. (2024). Trauma in Neonatal Acute Brain Slices Alters Calcium and Network Dynamics and Causes Calpain-Mediated Cell Death. Eneuro, 11.","DOI":"10.1523\/ENEURO.0007-24.2024"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0021-9258(18)51762-2","article-title":"A Neutral, Calcium-activated Proteinase from the Soluble Fraction of Rat Brain","volume":"239","author":"Guroff","year":"1964","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1152\/physrev.00029.2002","article-title":"The Calpain System","volume":"83","author":"Goll","year":"2003","journal-title":"Physiol. Rev."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/0065-2571(81)90026-1","article-title":"Intracellular Ca2+-dependent protease (CALPAIN) and its high-molecular-weight endogenous inhibitor (CALPASTATIN)","volume":"19","author":"Murachi","year":"1981","journal-title":"Adv. Enzym. Regul."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"140616","DOI":"10.1016\/j.bbapap.2021.140616","article-title":"Calpains for dummies: What you need to know about the calpain family","volume":"1869","author":"Spinozzi","year":"2021","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.bbapap.2011.08.005","article-title":"Calpains\u2014An elaborate proteolytic system","volume":"1824","author":"Ono","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"E Croall, D., and Ersfeld, K. (2007). The calpains: Modular designs and functional diversity. Genome Biol., 8.","DOI":"10.1186\/gb-2007-8-6-218"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1093\/oxfordjournals.jbchem.a003025","article-title":"Dissociation of m-Calpain Subunits Occurs after Autolysis of the N-Terminus of the Catalytic Subunit, and Is Not Required for Activation","volume":"130","author":"Nakagawa","year":"2001","journal-title":"J. Biochem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"6106","DOI":"10.1074\/jbc.M310460200","article-title":"Calpain Activation by Cooperative Ca2+ Binding at Two Non-EF-hand Sites","volume":"279","author":"Moldoveanu","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1333","DOI":"10.1006\/bbrc.2001.4279","article-title":"Domain III of Calpain Is a Ca2+-Regulated Phospholipid-Binding Domain","volume":"280","author":"Tompa","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"6880","DOI":"10.1093\/emboj\/18.24.6880","article-title":"Crystal structure of calpain reveals the structural basis for Ca2+-dependent protease activity and a novel mode of enzyme activation","volume":"18","author":"Hosfield","year":"1999","journal-title":"EMBO J."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1046\/j.1471-4159.2001.00493.x","article-title":"Specific proteolysis of the NR2 subunit at multiple sites by calpain","volume":"78","author":"Guttmann","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Su, W., Zhou, Q., Wang, Y., Chishti, A., Li, Q.Q., Dayal, S., Shiehzadegan, S., Cheng, A., Moore, C., and Bi, X. (2020). Deletion of the Capn1 Gene Results in Alterations in Signaling Pathways Related to Alzheimer\u2019s Disease, Protein Quality Control and Synaptic Plasticity in Mouse Brain. Front. Genet., 11.","DOI":"10.3389\/fgene.2020.00334"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Wang, Y., Liu, Y., Bi, X., and Baudry, M. (2020). Calpain-1 and Calpain-2 in the Brain: New Evidence for a Critical Role of Calpain-2 in Neuronal Death. Cells, 9.","DOI":"10.3390\/cells9122698"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1523\/JNEUROSCI.2193-14.2015","article-title":"Different Patterns of Electrical Activity Lead to Long-term Potentiation by Activating Different Intracellular Pathways","volume":"35","author":"Zhu","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e1181","DOI":"10.1002\/prp2.1181","article-title":"Identification and neuroprotective properties of NA-184, a calpain-2 inhibitor","volume":"12","author":"Baudry","year":"2024","journal-title":"Pharmacol. Res. Perspect."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1089\/neu.2017.5024","article-title":"Protection against TBI-Induced Neuronal Death with Post-Treatment with a Selective Calpain-2 Inhibitor in Mice","volume":"35","author":"Wang","year":"2018","journal-title":"J. Neurotrauma"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1111\/jnc.14837","article-title":"The calcium-activated protease calpain regulates netrin-1 receptor deleted in colorectal cancer-induced axon outgrowth in cortical neurons","volume":"152","author":"Duquette","year":"2019","journal-title":"J. Neurochem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1016\/j.ajhg.2016.05.009","article-title":"Mutations in CAPN1 Cause Autosomal-Recessive Hereditary Spastic Paraplegia","volume":"98","author":"Bouslam","year":"2016","journal-title":"Am. J. Hum. Genet."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1002\/syn.1053","article-title":"Activation of calpain may alter the postsynaptic density structure and modulate anchoring of NMDA receptors","volume":"40","author":"Vinade","year":"2001","journal-title":"Synapse"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1387\/ijdb.072448fr","article-title":"Calpain 2 expression pattern and sub-cellular localization during mouse embryogenesis","volume":"52","author":"Raynaud","year":"2008","journal-title":"Int. J. Dev. Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3829","DOI":"10.1242\/jcs.02562","article-title":"Regulating cell migration: Calpains make the cut","volume":"118","author":"Franco","year":"2005","journal-title":"J. Cell Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2499","DOI":"10.1128\/MCB.24.6.2499-2512.2004","article-title":"Epidermal Growth Factor Activates m-Calpain (Calpain II), at Least in Part, by Extracellular Signal-Regulated Kinase-Mediated Phosphorylation","volume":"24","author":"Glading","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1007\/s00401-002-0528-6","article-title":"Calpain activation in neurodegenerative diseases: Confocal immunofluorescence study with antibodies specifically recognizing the active form of calpain 2","volume":"104","author":"Adamec","year":"2002","journal-title":"Acta Neuropathol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2873","DOI":"10.1038\/s41401-022-00965-9","article-title":"Sustained over-expression of calpain-2 induces age-dependent dilated cardiomyopathy in mice through aberrant autophagy","volume":"43","author":"Ji","year":"2022","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"20106","DOI":"10.1016\/S0021-9258(19)47225-6","article-title":"Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and \u03bc-types","volume":"264","author":"Sorimachi","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1016\/j.nmd.2008.08.005","article-title":"Calpain 3, the \u201cgatekeeper\u201d of proper sarcomere assembly, turnover and maintenance","volume":"18","author":"Beckmann","year":"2008","journal-title":"Neuromuscul. Disord."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1093\/brain\/awh408","article-title":"LGMD2A: Genotype\u2013phenotype correlations based on a large mutational survey on the calpain 3 gene","volume":"128","author":"Leturcq","year":"2005","journal-title":"Brain"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1186\/s13104-017-2927-8","article-title":"Calpain-5 gene expression in the mouse eye and brain","volume":"10","author":"Schaefer","year":"2017","journal-title":"BMC Res. Notes"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Mahajan, V.B., Skeie, J.M., Bassuk, A.G., Fingert, J.H., Braun, T.A., Daggett, H.T., Folk, J.C., Sheffield, V.C., Stone, E.M., and Barsh, G.S. (2012). Calpain-5 Mutations Cause Autoimmune Uveitis, Retinal Neovascularization, and Photoreceptor Degeneration. PLoS Genet., 8.","DOI":"10.1371\/journal.pgen.1003001"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/S0925-4773(99)00214-2","article-title":"Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6 and Capn11 during development","volume":"89","author":"Dear","year":"1999","journal-title":"Mech. Dev."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2548","DOI":"10.1128\/MCB.00992-06","article-title":"Calpain 6 Is Involved in Microtubule Stabilization and Cytoskeletal Organization","volume":"27","author":"Tonami","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"2237","DOI":"10.3892\/ol.2017.5687","article-title":"Decreased calpain 6 expression is associated with tumorigenesis and poor prognosis in HNSCC","volume":"13","author":"Xiang","year":"2017","journal-title":"Oncol. Lett."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2514","DOI":"10.1002\/ijc.26246","article-title":"Calpain-6 is an endothelin-1 signaling dependent protective factor in chemoresistant osteosarcoma","volume":"130","author":"Marion","year":"2011","journal-title":"Int. J. Cancer"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"e84515","DOI":"10.7554\/eLife.84515","article-title":"The Calpain-7 protease functions together with the ESCRT-III protein IST1 within the midbody to regulate the timing and completion of abscission","volume":"12","author":"Paine","year":"2023","journal-title":"eLife"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3642","DOI":"10.1111\/febs.12886","article-title":"Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway","volume":"281","author":"Maemoto","year":"2014","journal-title":"FEBS J."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"Dai, D., Wu, D., Ni, R., Li, P., Tian, Z., Shui, Y., Hu, H., and Wei, Q. (2023). Novel insights into the progression and prognosis of the calpain family members in hepatocellular carcinoma: A comprehensive integrated analysis. Front. Mol. Biosci., 10.","DOI":"10.3389\/fmolb.2023.1162409"},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Hata, S., Abe, M., Suzuki, H., Kitamura, F., Toyama-Sorimachi, N., Abe, K., Sakimura, K., Sorimachi, H., and Barsh, G.S. (2010). Calpain 8\/nCL-2 and Calpain 9\/nCL-4 Constitute an Active Protease Complex, G-Calpain, Involved in Gastric Mucosal Defense. PLoS Genet., 6.","DOI":"10.1371\/journal.pgen.1001040"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"28525","DOI":"10.1074\/jbc.M100603200","article-title":"Characterization and Expression of Calpain 10: A Novel Ubiquitous Calpain with Nuclear Localization","volume":"276","author":"Ma","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Hatta, T., Iemura, S.-I., Ohishi, T., Nakayama, H., Seimiya, H., Yasuda, T., Iizuka, K., Fukuda, M., Takeda, J., and Natsume, T. (2018). Calpain-10 regulates actin dynamics by proteolysis of microtubule-associated protein 1B. Sci. Rep., 8.","DOI":"10.1038\/s41598-018-35204-x"},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Ling, C., Groop, L., Del Guerra, S., Lupi, R., and Maedler, K. (2009). Calpain-10 Expression Is Elevated in Pancreatic Islets from Patients with Type 2 Diabetes. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0006558"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1002\/mrd.20466","article-title":"Calpain 11 is unique to mouse spermatogenic cells","volume":"73","author":"Brown","year":"2006","journal-title":"Mol. Reprod. Dev."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.jid.2016.07.043","article-title":"Calpain 12 Function Revealed through the Study of an Atypical Case of Autosomal Recessive Congenital Ichthyosis","volume":"137","author":"Bochner","year":"2016","journal-title":"J. Investig. Dermatol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1006\/geno.2000.6289","article-title":"Gene Structure, Chromosomal Localization, and Expression Pattern of Capn12, a New Member of the Calpain Large Subunit Gene Family","volume":"68","author":"Dear","year":"2000","journal-title":"Genomics"},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Chukai, Y., Sudo, T., Fukuda, T., Tomita, H., Sugano, E., and Ozaki, T. (2024). Proteolysis of mitochondrial calpain-13 in cerebral ischemia-reperfusion injury. Biochem. Biophys. Rep., 39.","DOI":"10.1016\/j.bbrep.2024.101768"},{"key":"ref_60","first-page":"e86355","article-title":"Eosinophilic esophagitis\u2013linked calpain 14 is an IL-13\u2013induced protease that mediates esophageal epithelial barrier impairment","volume":"1","author":"Davis","year":"2016","journal-title":"J. Clin. Investig."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"3054","DOI":"10.1093\/hmg\/ddaa198","article-title":"Biallelic variants in the small optic lobe calpain CAPN15 are associated with congenital eye anomalies, deafness and other neurodevelopmental deficits","volume":"29","author":"Zha","year":"2020","journal-title":"Hum. Mol. Genet."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Zha, C., Huang, A., Kailasam, S., Young, D., Dufour, A., Sossin, W.S., and Goymer, P. (2025). Identifying putative substrates of Calpain-15 in neurodevelopment. PLoS ONE, 20.","DOI":"10.1371\/journal.pone.0319489"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Yoder, M.W., Wright, N.T., and Borzok, M.A. (2023). Calpain Regulation and Dysregulation\u2014Its Effects on the Intercalated Disk. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241411726"},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Peng, P., Min, L., Song, S., Zhao, J., Li, L., Yang, C., Shao, M., Zhang, M., Wu, H., and Zhang, J. (2016). Elevated Expression of Calpain-4 Predicts Poor Prognosis in Patients with Gastric Cancer after Gastrectomy. Int. J. Mol. Sci., 17.","DOI":"10.3390\/ijms17101612"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"S12","DOI":"10.2337\/diabetes.53.2007.S12","article-title":"Structure, Activation, and Biology of Calpain","volume":"53","author":"Suzuki","year":"2004","journal-title":"Diabetes"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1042\/bj3620383","article-title":"A novel human small subunit of calpains","volume":"362","author":"Farkas","year":"2002","journal-title":"Biochem. J."},{"key":"ref_67","first-page":"160","article-title":"Neuropathology of the Head Injuries","volume":"3","author":"Gennarelli","year":"1998","journal-title":"Semin. Clin. Neuropsychiatry"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"3130","DOI":"10.1523\/JNEUROSCI.5119-05.2006","article-title":"Mechanoporation Induced by Diffuse Traumatic Brain Injury: An Irreversible or Reversible Response to Injury?","volume":"26","author":"Farkas","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1923","DOI":"10.1523\/JNEUROSCI.21-06-01923.2001","article-title":"Traumatic Axonal Injury Induces Calcium Influx Modulated by Tetrodotoxin-Sensitive Sodium Channels","volume":"21","author":"Wolf","year":"2001","journal-title":"J. Neurosci."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Musyaju, S., Modi, H.R., Shear, D.A., Scultetus, A.H., and Pandya, J.D. (2025). Time Course of Mitochondrial Antioxidant Markers in a Preclinical Model of Severe Penetrating Traumatic Brain Injury. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26030906"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1619","DOI":"10.1089\/089771502762300274","article-title":"NMDA Receptor Activation Contributes to a Portion of the Decreased Mitochondrial Membrane Potential and Elevated Intracellular Free Calcium in Strain-Injured Neurons","volume":"19","author":"Ahmed","year":"2002","journal-title":"J. Neurotrauma"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1126\/science.1709304","article-title":"Ca2 + Permeability of KA-AMPA\u2014Gated Glutamate Receptor Channels Depends on Subunit Composition","volume":"252","author":"Hollmann","year":"1991","journal-title":"Science"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0896-6273(92)90120-3","article-title":"Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit","volume":"8","author":"Burnashev","year":"1992","journal-title":"Neuron"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1016\/j.neuron.2007.06.001","article-title":"The Role of the GluR2 Subunit in AMPA Receptor Function and Synaptic Plasticity","volume":"54","author":"Isaac","year":"2007","journal-title":"Neuron"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1016\/S0006-3495(99)77036-0","article-title":"Voltage-Dependent Sodium Channel Function Is Regulated Through Membrane Mechanics","volume":"77","author":"Shcherbatko","year":"1999","journal-title":"Biophys. J."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"C823","DOI":"10.1152\/ajpcell.00505.2008","article-title":"Membrane trauma and Na+leak from Nav1.6 channels","volume":"297","author":"Wang","year":"2009","journal-title":"Am. J. Physiol. Physiol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1089\/neu.2009.1003","article-title":"Neuroprotective Effects of Selective N-Type VGCC Blockade on Stretch-Injury-Induced Calcium Dynamics in Cortical Neurons","volume":"27","author":"Shahlaie","year":"2010","journal-title":"J. Neurotrauma"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1523\/JNEUROSCI.12-02-00430.1992","article-title":"Ionic mechanisms of anoxic injury in mammalian CNS white matter: Role of Na+ channels and Na+-Ca2+ exchanger","volume":"12","author":"Stys","year":"1992","journal-title":"J. Neurosci."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.nbd.2011.12.051","article-title":"Delayed calcium dysregulation in neurons requires both the NMDA receptor and the reverse Na+\/Ca2+ exchanger","volume":"46","author":"Brittain","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1038\/s41419-019-1908-3","article-title":"Dynamin and reverse-mode sodium calcium exchanger blockade confers neuroprotection from diffuse axonal injury","volume":"10","author":"Omelchenko","year":"2019","journal-title":"Cell Death Dis."},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Chou, A.-C., Ju, Y.-T., Pan, C.-Y., and Obukhov, A.G. (2015). Calmodulin Interacts with the Sodium\/Calcium Exchanger NCX1 to Regulate Activity. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0138856"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.coph.2018.03.004","article-title":"Metabotropic glutamate receptors: Targets for neuroprotective therapies in Parkinson disease","volume":"38","author":"Masilamoni","year":"2018","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1016\/j.neuropharm.2010.10.022","article-title":"Metabotropic glutamate receptors: From the workbench to the bedside","volume":"60","author":"Nicoletti","year":"2011","journal-title":"Neuropharmacology"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1089\/089771504322972068","article-title":"Group I Metabotropic Receptor Antagonism Blocks Depletion of Calcium Stores and Reduces Potentiated Capacitative Calcium Entry in Strain-Injured Neurons and Astrocytes","volume":"21","author":"Chen","year":"2004","journal-title":"J. Neurotrauma"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Orem, B.C., Rajaee, A., and Stirling, D.P. (2020). IP3R-mediated intra-axonal Ca2+ release contributes to secondary axonal degeneration following contusive spinal cord injury. Neurobiol. Dis., 146.","DOI":"10.1016\/j.nbd.2020.105123"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.nbd.2017.07.011","article-title":"Intracellular calcium release through IP 3 R or RyR contributes to secondary axonal degeneration","volume":"106","author":"Orem","year":"2017","journal-title":"Neurobiol. Dis."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1152\/jn.01004.2003","article-title":"Distinct Intracellular Calcium Profiles Following Influx Through N- Versus L-Type Calcium Channels: Role of Ca2+-Induced Ca2+ Release","volume":"92","author":"Tully","year":"2004","journal-title":"J. Neurophysiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1111\/j.1471-4159.2012.07859.x","article-title":"Calpain-cleaved type 1 inositol 1,4,5-trisphosphate receptor impairs ER Ca2+ buffering and causes neurodegeneration in primary cortical neurons","volume":"123","author":"Kopil","year":"2012","journal-title":"J. Neurochem."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.mehy.2012.11.004","article-title":"The role of mitochondrial calcium uniporter in neuroprotection in traumatic brain injury","volume":"80","author":"Cheng","year":"2013","journal-title":"Med. Hypotheses"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1089\/neu.1999.16.1067","article-title":"Effect of N-Acetylcysteine on Mitochondrial Function Following Traumatic Brain Injury in Rats","volume":"16","author":"Xiong","year":"1999","journal-title":"J. Neurotrauma"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/S0005-2728(98)00110-8","article-title":"Mitochondria as regulators of apoptosis: Doubt no more","volume":"1366","author":"Susin","year":"1998","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1038\/sj.jcbfm.9600297","article-title":"Time Course of Post-Traumatic Mitochondrial Oxidative Damage and Dysfunction in a Mouse Model of Focal Traumatic Brain Injury: Implications for Neuroprotective Therapy","volume":"26","author":"Singh","year":"2006","journal-title":"J. Cereb. Blood Flow Metab."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Mira, R.G., Quintanilla, R.A., and Cerpa, W. (2023). Mild Traumatic Brain Injury Induces Mitochondrial Calcium Overload and Triggers the Upregulation of NCLX in the Hippocampus. Antioxidants, 12.","DOI":"10.3390\/antiox12020403"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1111\/j.1471-4159.2009.06531.x","article-title":"Initial calcium release from intracellular stores followed by calcium dysregulation is linked to secondary axotomy following transient axonal stretch injury","volume":"112","author":"Staal","year":"2010","journal-title":"J. Neurochem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1111\/jnc.12313","article-title":"Actin filaments and microtubules in dendritic spines","volume":"126","author":"Shirao","year":"2013","journal-title":"J. Neurochem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1083\/jcb.99.2.705","article-title":"Control of axonal caliber by neurofilament transport","volume":"99","author":"Hoffman","year":"1984","journal-title":"J. Cell Biol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/sj.embor.7400360","article-title":"Structural rearrangements in tubulin following microtubule formation","volume":"6","author":"Krebs","year":"2005","journal-title":"Embo Rep."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1083\/jcb.200109026","article-title":"Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments","volume":"155","author":"Jenkins","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1083\/jcb.201003008","article-title":"Actin in dendritic spines: Connecting dynamics to function","volume":"189","author":"Hotulainen","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1126\/science.1232251","article-title":"Actin, Spectrin, and Associated Proteins Form a Periodic Cytoskeletal Structure in Axons","volume":"339","author":"Xu","year":"2013","journal-title":"Science"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1097\/00005072-199607000-00010","article-title":"Prolonged Calpain-mediated Spectrin Breakdown Occurs Regionally Following Experimental Brain Injury in the Rat","volume":"55","author":"Saatman","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/S0166-2236(99)01479-4","article-title":"Calpain and caspase: Can you tell the difference?","volume":"23","author":"Wang","year":"2000","journal-title":"Trends Neurosci."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.expneurol.2007.01.023","article-title":"Temporal relationship of peroxynitrite-induced oxidative damage, calpain-mediated cytoskeletal degradation and neurodegeneration after traumatic brain injury","volume":"205","author":"Deng","year":"2007","journal-title":"Exp. Neurol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1097\/NEN.0b013e3181996bfe","article-title":"Biochemical, Structural, and Biomarker Evidence for Calpain-Mediated Cytoskeletal Change After Diffuse Brain Injury Uncomplicated by Contusion","volume":"68","author":"McGinn","year":"2009","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1097\/00005072-199904000-00007","article-title":"The Role of Calpail-Mediated Spectrin Proteolysis in Traumatically Induced Axonal Injury","volume":"58","author":"Siman","year":"1999","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1111\/j.1750-3639.2010.00412.x","article-title":"Proteolysis of Submembrane Cytoskeletal Proteins Ankyrin-G and \u03b1II-Spectrin Following Diffuse Brain Injury: A Role in White Matter Vulnerability at Nodes of Ranvier","volume":"20","author":"Reeves","year":"2010","journal-title":"Brain Pathol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1089\/neu.1997.14.369","article-title":"Immunohistochemical Study of Calpain-Mediated Breakdown Products to \u03b1-Spectrin Following Controlled Cortical Impact Injury in the Rat","volume":"14","author":"Newcomb","year":"1997","journal-title":"J. Neurotrauma"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"2437","DOI":"10.1097\/00001756-199808030-00002","article-title":"Regional calpain and caspase-3 proteolysis of \u03b1-spectrin after traumatic brain injury","volume":"9","author":"Pike","year":"1998","journal-title":"NeuroReport"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.bbr.2016.04.041","article-title":"PrPC expression and calpain activity independently mediate the effects of closed head injury in mice","volume":"340","author":"Rubenstein","year":"2018","journal-title":"Behav. Brain Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.brainres.2013.12.031","article-title":"Cytoskeletal protein \u03b1\u2013II spectrin degradation in the brain of repeated blast exposed mice","volume":"1549","author":"Valiyaveettil","year":"2014","journal-title":"Brain Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1046\/j.1471-4159.2001.00510.x","article-title":"Accumulation of non-erythroid \u03b1II-spectrin and calpain-cleaved \u03b1II-spectrin breakdown products in cerebrospinal fluid after traumatic brain injury in rats","volume":"78","author":"Pike","year":"2001","journal-title":"J. Neurochem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1089\/neu.2010.1278","article-title":"\u03b1II-Spectrin Breakdown Products (SBDPs): Diagnosis and Outcome in Severe Traumatic Brain Injury Patients","volume":"27","author":"Mondello","year":"2010","journal-title":"J. Neurotrauma"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.neuint.2017.03.015","article-title":"Time courses of post-injury mitochondrial oxidative damage and respiratory dysfunction and neuronal cytoskeletal degradation in a rat model of focal traumatic brain injury","volume":"111","author":"Hill","year":"2017","journal-title":"Neurochem. Int."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"148475","DOI":"10.1016\/j.brainres.2023.148475","article-title":"Evaluating the effect of post-traumatic hypoxia on the development of axonal injury following traumatic brain injury in sheep","volume":"1817","author":"Sharkey","year":"2023","journal-title":"Brain Res."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Siman, R., Cui, H., Wewerka, S.S., Hamel, L., Smith, D.H., and Zwank, M.D. (2020). Serum SNTF, a Surrogate Marker of Axonal Injury, Is Prognostic for Lasting Brain Dysfunction in Mild TBI Treated in the Emergency Department. Front. Neurol., 11.","DOI":"10.3389\/fneur.2020.00249"},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Siman, R., Giovannone, N., Hanten, G., Wilde, E.A., McCauley, S.R., Hunter, J.V., Li, X., Levin, H.S., and Smith, D.H. (2013). Evidence That the Blood Biomarker SNTF Predicts Brain Imaging Changes and Persistent Cognitive Dysfunction in Mild TBI Patients. Front. Neurol., 4.","DOI":"10.3389\/fneur.2013.00190"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.1089\/neu.2014.3698","article-title":"Serum SNTF Increases in Concussed Professional Ice Hockey Players and Relates to the Severity of Postconcussion Symptoms","volume":"32","author":"Siman","year":"2015","journal-title":"J. Neurotrauma"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"898","DOI":"10.1007\/s12035-017-0764-3","article-title":"Erratum to: Degradation of \u03b2II-Spectrin Protein by Calpain-2 and Caspase-3 Under Neurotoxic and Traumatic Brain Injury Conditions","volume":"55","author":"Kobeissy","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1002\/cne.903170406","article-title":"Neurofilaments are prominent in bullfrog olfactory axons but are rarely seen in those of the tiger salamander, Ambystoma tigrinum","volume":"317","author":"Burton","year":"1992","journal-title":"J. Comp. Neurol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/j.bbrc.2004.09.223","article-title":"Characterization of the bovine neurofilament NF-M protein and cDNA sequence, and identification of in vitro and in vivo calpain cleavage sites","volume":"325","author":"Shaw","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"115382","DOI":"10.1016\/j.celrep.2025.115382","article-title":"Secreted neurofilament light chain after neuronal damage induces myeloid cell activation and neuroinflammation","volume":"44","author":"Kahn","year":"2025","journal-title":"Cell Rep."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1111\/j.1471-4159.1985.tb05442.x","article-title":"An Immunoblot Study of Neurofilament Degradation In Situ and During Calcium-Activated Proteolysis","volume":"44","author":"Schlaepfer","year":"1985","journal-title":"J. Neurochem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1002\/jnr.490130306","article-title":"Calcium-Activated neutral protease in the peripheral nerve, which requires \u03bcM order Ca2+, and its effect on the neurofilament triplet","volume":"13","author":"Kamakura","year":"1985","journal-title":"J. Neurosci. Res."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.neuron.2015.05.046","article-title":"Building the Neuronal Microtubule Cytoskeleton","volume":"87","author":"Kapitein","year":"2015","journal-title":"Neuron"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"8335","DOI":"10.1073\/pnas.85.21.8335","article-title":"Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and nonuniformity in the dendrite","volume":"85","author":"Baas","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1523\/JNEUROSCI.2430-15.2016","article-title":"Dendrites In Vitro and In Vivo Contain Microtubules of Opposite Polarity and Axon Formation Correlates with Uniform Plus-End-Out Microtubule Orientation","volume":"36","author":"Yau","year":"2016","journal-title":"J. Neurosci."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1083\/jcb.101.4.1371","article-title":"The distribution of tau in the mammalian central nervous system","volume":"101","author":"Binder","year":"1985","journal-title":"J. Cell Biol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1152\/physrev.1995.75.4.835","article-title":"Role of microtubule-associated proteins in the control of microtubule assembly","volume":"75","author":"Maccioni","year":"1995","journal-title":"Physiol. Rev."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1083\/jcb.98.1.320","article-title":"Widespread distribution of the major polypeptide component of MAP 1 (microtubule-associated protein 1) in the nervous system","volume":"98","author":"Bloom","year":"1984","journal-title":"J. Cell Biol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"2006","DOI":"10.1007\/s11064-007-9318-9","article-title":"Temporal Profiles of Cytoskeletal Protein Loss following Traumatic Axonal Injury in Mice","volume":"32","author":"Serbest","year":"2007","journal-title":"Neurochem. Res."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0143-4160(88)90036-X","article-title":"Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules","volume":"9","author":"Billger","year":"1988","journal-title":"Cell Calcium"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1042\/bj2230047","article-title":"Calpain and calpastatin in porcine retina. Identification and action on microtubule-associated proteins","volume":"223","author":"Yoshimura","year":"1984","journal-title":"Biochem. J."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1016\/0024-3205(87)90374-2","article-title":"Micromolar Ca2+ requiring protease from human platelets: Purification, partial characterization and effect on the cytoskeletal proteins","volume":"40","author":"Malik","year":"1987","journal-title":"Life Sci."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"8955","DOI":"10.1016\/S0021-9258(18)32150-1","article-title":"Purification and characterization of two forms of Ca2+-activated neutral protease from calf brain","volume":"258","author":"Malik","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Yadikar, H., Johnson, C., Pafundi, N., Mouhawasse, E., Nguyen, L., Torres, I., Kurup, M., Yang, Z., Kobeissy, F., and Yost, R. (2019). Novel Peptidomic Approach for Identification of Low and High Molecular Weight Tauopathy Peptides Following Calpain Digestion, and Primary Culture Neurotoxic Challenges. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20205213"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1111\/j.1432-1033.1995.009_1.x","article-title":"Calpain-Induced Proteolysis of Normal Human Tau and Tau Associated with Paired Helical Filaments","volume":"233","author":"Yang","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1016\/0006-291X(89)91150-9","article-title":"Proteolysis of tau by calpain","volume":"163","author":"Johnson","year":"1989","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Girouard, M.-P., Simas, T., Hua, L., Morquette, B., Khazaei, M.R., Unsain, N., Johnstone, A.D., Rambaldi, I., Sanz, R.L., and Di Raddo, M.-E. (2020). Collapsin Response Mediator Protein 4 (CRMP4) Facilitates Wallerian Degeneration and Axon Regeneration following Sciatic Nerve Injury. Eneuro, 7.","DOI":"10.1523\/ENEURO.0479-19.2020"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1089\/neu.2006.0078","article-title":"Calpain-mediated collapsin response mediator protein-1, -2, and -4 proteolysis after neurotoxic and traumatic brain injury","volume":"24","author":"Zhang","year":"2007","journal-title":"J. Neurotrauma"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1523\/JNEUROSCI.4485-05.2006","article-title":"Calpain-Cleaved Collapsin Response Mediator Protein-3 Induces Neuronal Death after Glutamate Toxicity and Cerebral Ischemia","volume":"26","author":"Hou","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1111\/j.1471-4159.2008.05860.x","article-title":"Knockdown of m-calpain increases survival of primary hippocampal neurons following NMDA excitotoxicity","volume":"108","author":"Bevers","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"8815","DOI":"10.1038\/ncomms9815","article-title":"Redistribution of Kv1 and Kv7 enhances neuronal excitability during structural axon initial segment plasticity","volume":"6","author":"Kuba","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1002\/ana.410330202","article-title":"Molecular dissection of the myelinated axon","volume":"33","author":"Waxman","year":"1993","journal-title":"Ann. Neurol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S0169-328X(02)00385-6","article-title":"Sodium channel Nav1.6 is expressed along nonmyelinated axons and it contributes to conduction","volume":"105","author":"Renganathan","year":"2002","journal-title":"Mol. Brain Res."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1046\/j.1460-9568.2000.00974.x","article-title":"Location of calcium transporters at presynaptic terminals","volume":"12","author":"Juhaszova","year":"2000","journal-title":"Eur. J. Neurosci."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1007\/s00401-022-02498-1","article-title":"Concussion leads to widespread axonal sodium channel loss and disruption of the node of Ranvier","volume":"144","author":"Song","year":"2022","journal-title":"Acta Neuropathol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"4605","DOI":"10.1523\/JNEUROSCI.0515-03.2004","article-title":"Traumatic Axonal Injury Induces Proteolytic Cleavage of the Voltage-Gated Sodium Channels Modulated by Tetrodotoxin and Protease Inhibitors","volume":"24","author":"Iwata","year":"2004","journal-title":"J. Neurosci."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"10350","DOI":"10.1523\/JNEUROSCI.2339-09.2009","article-title":"Calpain Mediates Proteolysis of the Voltage-Gated Sodium Channel \u03b1-Subunit","volume":"29","author":"Spaethling","year":"2009","journal-title":"J. Neurosci."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Arratia, L.M., Bermudes-Contreras, J.D., Juarez-Monroy, J.A., Romero-Mac\u00edas, E.A., Luna-Rojas, J.C., L\u00f3pez-Hidalgo, M., Vega, A.V., and Zamorano-Carrillo, A. (2024). Experimental and computational evidence that Calpain-10 binds to the carboxy terminus of NaV1.2 and NaV1.6. Sci. Rep., 14.","DOI":"10.1038\/s41598-024-57117-8"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.cell.2004.11.049","article-title":"Cleavage of the Plasma Membrane Na+\/Ca2+ Exchanger in Excitotoxicity","volume":"120","author":"Bano","year":"2005","journal-title":"Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1002\/jnr.22295","article-title":"Calpain activation and Na+\/Ca2+exchanger degradation occur downstream of calcium deregulation in hippocampal neurons exposed to excitotoxic glutamate","volume":"88","author":"Brustovetsky","year":"2009","journal-title":"J. Neurosci. Res."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1635","DOI":"10.1038\/sj.cdd.4402171","article-title":"Changes in calcium dynamics following the reversal of the sodium-calcium exchanger have a key role in AMPA receptor-mediated neurodegeneration via calpain activation in hippocampal neurons","volume":"14","author":"Carreira","year":"2007","journal-title":"Cell Death Differ."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1111\/j.1471-4159.2006.04063.x","article-title":"Glutamate-induced protease-mediated loss of plasma membrane Ca2+ pump activity in rat hippocampal neurons","volume":"98","author":"Pottorf","year":"2006","journal-title":"J. Neurochem."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Harris, K.M., and Weinberg, R.J. (2012). Ultrastructure of Synapses in the Mammalian Brain. Cold Spring Harb. Perspect. Biol., 4.","DOI":"10.1101\/cshperspect.a005587"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Sheng, M., and Kim, E. (2011). The Postsynaptic Organization of Synapses. Cold Spring Harb. Perspect. Biol., 3.","DOI":"10.1101\/cshperspect.a005678"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"e81407","DOI":"10.7554\/eLife.81407","article-title":"CaV1 and CaV2 calcium channels mediate the release of distinct pools of synaptic vesicles","volume":"12","author":"Mueller","year":"2023","journal-title":"eLife"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1113\/jphysiol.1985.sp015654","article-title":"Calcium-activated potassium channels in isolated presynaptic nerve terminals from rat brain","volume":"361","author":"Bartschat","year":"1985","journal-title":"J. Physiol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1085\/jgp.99.4.491","article-title":"Aminoglycoside antibiotics block voltage-dependent calcium channels in intact vertebrate nerve terminals","volume":"99","author":"Parsons","year":"1992","journal-title":"J. Gen. Physiol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1152\/physrev.1999.79.3.1019","article-title":"Ion Channels in Presynaptic Nerve Terminals and Control of Transmitter Release","volume":"79","author":"Meir","year":"1999","journal-title":"Physiol. Rev."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"379","DOI":"10.4161\/cam.24803","article-title":"The actin cytoskeleton in presynaptic assembly","volume":"7","author":"Nelson","year":"2013","journal-title":"Cell Adhes. Migr."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S0006-8993(00)02112-0","article-title":"Calpain-mediated truncation of rat brain AMPA receptors increases their Triton X-100 solubility","volume":"863","author":"Lu","year":"2000","journal-title":"Brain Res."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0304-3940(00)01101-0","article-title":"Calpain-mediated degradation of PSD-95 in developing and adult rat brain","volume":"286","author":"Lu","year":"2000","journal-title":"Neurosci. Lett."},{"key":"ref_163","first-page":"99","article-title":"Excitotoxicity and focal cerebral ischemia induce truncation of the NR2A and NR2B subunits of the NMDA receptor and cleavage of the scaffolding protein PSD-95","volume":"13","author":"Sobrado","year":"2007","journal-title":"Mol. Psychiatry"},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Chimura, T., Launey, T., Yoshida, N., and Norris, C.M. (2015). Calpain-Mediated Degradation of Drebrin by Excitotoxicity In vitro and In vivo. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0125119"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0006-8993(98)00067-5","article-title":"Calpain-mediated regulation of NMDA receptor structure and function","volume":"790","author":"Bi","year":"1998","journal-title":"Brain Res."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1046\/j.1471-4159.1997.68041484.x","article-title":"Characterization of Calpain-Mediated Proteolysis of GluR1 Subunits of \u03b1-Amino-3-Hydroxy-5-Methylisoxazole-4-Propionate Receptors in Rat Brain","volume":"68","author":"Bi","year":"1997","journal-title":"J. Neurochem."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"11322","DOI":"10.1523\/JNEUROSCI.23-36-11322.2003","article-title":"Selective Activation Induced Cleavage of the NR2B Subunit by Calpain","volume":"23","author":"Simpkins","year":"2003","journal-title":"J. Neurosci."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1124\/jpet.102.036962","article-title":"Proteolysis of the N-Methyl-d-Aspartate Receptor by Calpain In Situ","volume":"302","author":"Guttmann","year":"2002","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"7161","DOI":"10.1523\/JNEUROSCI.16-22-07161.1996","article-title":"Modulatory Role of Drebrin on the Cytoskeleton within Dendritic Spines in the Rat Cerebral Cortex","volume":"16","author":"Hayashi","year":"1996","journal-title":"J. Neurosci."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/j.neuron.2006.12.020","article-title":"Calpain-Mediated mGluR1\u03b1 Truncation: A Key Step in Excitotoxicity","volume":"53","author":"Xu","year":"2007","journal-title":"Neuron"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0014-5793(93)81345-Z","article-title":"Calcium-induced degradation of the Inositol (1,4,5)-trisphosphate receptor\/Ca2+-channel","volume":"323","author":"Magnusson","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"4772","DOI":"10.1074\/jbc.M110.167155","article-title":"The Mitochondrial Inner Membrane GTPase, Optic Atrophy 1 (Opa1), Restores Mitochondrial Morphology and Promotes Neuronal Survival following Excitotoxicity","volume":"286","author":"Xu","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.mito.2016.07.009","article-title":"Calpastatin overexpression reduces oxidative stress-induced mitochondrial impairment and cell death in human neuroblastoma SH-SY5Y cells by decreasing calpain and calcineurin activation, induction of mitochondrial fission and destruction of mitochondrial fusion","volume":"30","author":"Tangmansakulchai","year":"2016","journal-title":"Mitochondrion"},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Wang, Y., Hall, R.A., Lee, M., Kamgar-Parsi, A., Bi, X., and Baudry, M. (2017). The tyrosine phosphatase PTPN13\/FAP-1 links calpain-2, TBI and tau tyrosine phosphorylation. Sci. Rep., 7.","DOI":"10.1038\/s41598-017-12236-3"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"3077","DOI":"10.1089\/neu.2021.0229","article-title":"P13BP, a Calpain-2-Mediated Breakdown Product of PTPN13, Is a Novel Blood Biomarker for Traumatic Brain Injury","volume":"38","author":"Wang","year":"2021","journal-title":"J. Neurotrauma"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1089\/neu.2017.5368","article-title":"Gene Profiling of Nucleus Basalis Tau Containing Neurons in Chronic Traumatic Encephalopathy: A Chronic Effects of Neurotrauma Consortium Study","volume":"35","author":"Mufson","year":"2018","journal-title":"J. Neurotrauma"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"9222","DOI":"10.1523\/JNEUROSCI.1132-14.2014","article-title":"Specific Calpain Inhibition by Calpastatin Prevents Tauopathy and Neurodegeneration and Restores Normal Lifespan in Tau P301L Mice","volume":"34","author":"Rao","year":"2014","journal-title":"J. Neurosci."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.3233\/JAD-190281","article-title":"Inhibition of Calpain Protects Against Tauopathy in Transgenic P301S Tau Mice","volume":"69","author":"Liu","year":"2019","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"2628","DOI":"10.1073\/pnas.90.7.2628","article-title":"Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration","volume":"90","author":"Saito","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_180","first-page":"707","article-title":"Novel Selective Calpain 1 Inhibitors as Potential Therapeutics in Alzheimer\u2019s Disease","volume":"49","author":"Zhang","year":"2016","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"4081","DOI":"10.1523\/JNEUROSCI.23-10-04081.2003","article-title":"Inhibition of Calpains Prevents Neuronal and Behavioral Deficits in an MPTP Mouse Model of Parkinson\u2019s Disease","volume":"23","author":"Crocker","year":"2003","journal-title":"J. Neurosci."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1038\/ncomms2303","article-title":"A role for calpain-dependent cleavage of TDP-43 in amyotrophic lateral sclerosis pathology","volume":"3","author":"Yamashita","year":"2012","journal-title":"Nat. Commun."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"4842","DOI":"10.1523\/JNEUROSCI.22-12-04842.2002","article-title":"Calpain Activation in Huntington\u2019s Disease","volume":"22","author":"Gafni","year":"2002","journal-title":"J. Neurosci."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.jneuroim.2007.07.016","article-title":"Increased calpain correlates with Th1 cytokine profile in PBMCs from MS patients","volume":"190","author":"Imam","year":"2007","journal-title":"J. Neuroimmunol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1111\/jnc.12659","article-title":"Effects of a novel orally administered calpain inhibitor SNJ-1945 on immunomodulation and neurodegeneration in a murine model of multiple sclerosis","volume":"130","author":"Trager","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1126\/science.1258366","article-title":"SARM1 activation triggers axon degeneration locally via NAD+ destruction","volume":"348","author":"Gerdts","year":"2015","journal-title":"Science"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"13569","DOI":"10.1523\/JNEUROSCI.1197-13.2013","article-title":"Sarm1-Mediated Axon Degeneration Requires Both SAM and TIR Interactions","volume":"33","author":"Gerdts","year":"2013","journal-title":"J. Neurosci."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1126\/science.1223899","article-title":"dSarm\/Sarm1 Is Required for Activation of an Injury-Induced Axon Death Pathway","volume":"337","author":"Osterloh","year":"2012","journal-title":"Science"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1093\/brain\/aww001","article-title":"Attenuated traumatic axonal injury and improved functional outcome after traumatic brain injury in mice lacking Sarm1","volume":"139","author":"Henninger","year":"2016","journal-title":"Brain"},{"key":"ref_190","doi-asserted-by":"crossref","unstructured":"Miyamoto, T., Kim, C., Chow, J., Dugas, J.C., DeGroot, J., Bagdasarian, A.L., Thottumkara, A.P., Larhammar, M., Calvert, M.E., and Fox, B.M. (2024). SARM1 is responsible for calpain-dependent dendrite degeneration in mouse hippocampal neurons. J. Biol. Chem., 300.","DOI":"10.1016\/j.jbc.2024.105630"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1007\/s10072-022-06558-y","article-title":"The role of spectrin breakdown products in patients with traumatic brain injury: A systematic review and meta-analysis","volume":"44","author":"Liu","year":"2022","journal-title":"Neurol. Sci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/S1474-4422(19)30282-0","article-title":"Association between plasma GFAP concentrations and MRI abnormalities in patients with CT-negative traumatic brain injury in the TRACK-TBI cohort: A prospective multicentre study","volume":"18","author":"Yue","year":"2019","journal-title":"Lancet Neurol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"e664","DOI":"10.1016\/j.wneu.2019.12.095","article-title":"The Impact of Drug and Alcohol Intoxication on Glasgow Coma Scale Assessment in Patients with Traumatic Brain Injury","volume":"135","author":"DiGiorgio","year":"2020","journal-title":"World Neurosurg."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Gan, Z.S., Stein, S.C., Swanson, R., Guan, S., Garcia, L., Mehta, D., and Smith, D.H. (2019). Blood Biomarkers for Traumatic Brain Injury: A Quantitative Assessment of Diagnostic and Prognostic Accuracy. Front. Neurol., 10.","DOI":"10.3389\/fneur.2019.00446"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1080\/14737159.2024.2306876","article-title":"The game changer: UCH-L1 and GFAP-based blood test as the first marketed in vitro diagnostic test for mild traumatic brain injury","volume":"24","author":"Kobeissy","year":"2024","journal-title":"Expert Rev. Mol. Diagn."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1001\/jamaneurol.2016.0039","article-title":"Time Course and Diagnostic Accuracy of Glial and Neuronal Blood Biomarkers GFAP and UCH-L1 in a Large Cohort of Trauma Patients With and Without Mild Traumatic Brain Injury","volume":"73","author":"Papa","year":"2016","journal-title":"JAMA Neurol."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.ajem.2024.12.005","article-title":"A high-performance core laboratory GFAP\/UCH-L1 test for the prediction of intracranial injury after mild traumatic brain injury","volume":"89","author":"Welch","year":"2024","journal-title":"Am. J. Emerg. Med."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/S1474-4422(18)30231-X","article-title":"Serum GFAP and UCH-L1 for prediction of absence of intracranial injuries on head CT (ALERT-TBI): A multicentre observational study","volume":"17","author":"Bazarian","year":"2018","journal-title":"Lancet Neurol."},{"key":"ref_199","doi-asserted-by":"crossref","unstructured":"Syzdykbayev, M., Kazymov, M., Aubakirov, M., Kurmangazina, A., Kairkhanov, E., Kazangapov, R., Bryzhakhina, Z., Imangazinova, S., and Sheinin, A. (2024). A Modern Approach to the Treatment of Traumatic Brain Injury. Medicines, 11.","DOI":"10.3390\/medicines11050010"},{"key":"ref_200","doi-asserted-by":"crossref","unstructured":"Ghiam, M.K., Patel, S.D., Hoffer, A., Selman, W.R., Hoffer, B.J., and Hoffer, M.E. (2021). Drug Repurposing in the Treatment of Traumatic Brain Injury. Front. Neurosci., 15.","DOI":"10.3389\/fnins.2021.635483"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1111\/jnc.12118","article-title":"Pharmacological analysis of the cortical neuronal cytoskeletal protective efficacy of the calpain inhibitor SNJ-1945 in a mouse traumatic brain injury model","volume":"125","author":"Bains","year":"2013","journal-title":"J. Neurochem."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"2233","DOI":"10.1089\/neu.2010.1474","article-title":"A Pharmacological Analysis of the Neuroprotective Efficacy of the Brain- and Cell-Permeable Calpain Inhibitor MDL-28170 in the Mouse Controlled Cortical Impact Traumatic Brain Injury Model","volume":"27","author":"Thompson","year":"2010","journal-title":"J. Neurotrauma"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"7446","DOI":"10.1021\/bi060425j","article-title":"Calpain Inhibition by \u03b1-Ketoamide and Cyclic Hemiacetal Inhibitors Revealed by X-ray Crystallography,","volume":"45","author":"Cuerrier","year":"2006","journal-title":"Biochemistry"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"4089","DOI":"10.1021\/jm950541c","article-title":"Novel Peptidyl \u03b1-Keto Amide Inhibitors of Calpains and Other Cysteine Proteases","volume":"39","author":"Li","year":"1996","journal-title":"J. Med. Chem."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/14\/16\/1253\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T18:27:23Z","timestamp":1760034443000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/14\/16\/1253"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,8,14]]},"references-count":204,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2025,8]]}},"alternative-id":["cells14161253"],"URL":"https:\/\/doi.org\/10.3390\/cells14161253","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,8,14]]}}}