{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T16:33:14Z","timestamp":1787502794646,"version":"build-2736575974"},"reference-count":210,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2025,12,8]],"date-time":"2025-12-08T00:00:00Z","timestamp":1765152000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100005743","name":"Universit\u00e0 Cattolica del Sacro Cuore","doi-asserted-by":"publisher","award":["D1.2024"],"award-info":[{"award-number":["D1.2024"]}],"id":[{"id":"10.13039\/501100005743","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005743","name":"Universit\u00e0 Cattolica del Sacro Cuore","doi-asserted-by":"publisher","award":["D1.2025"],"award-info":[{"award-number":["D1.2025"]}],"id":[{"id":"10.13039\/501100005743","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003196","name":"Italian Ministry of Health","doi-asserted-by":"publisher","award":["Ricerca Corrente 2025"],"award-info":[{"award-number":["Ricerca Corrente 2025"]}],"id":[{"id":"10.13039\/501100003196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","award":["DM 1557 11.10.2022"],"award-info":[{"award-number":["DM 1557 11.10.2022"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Italian Ministry of University and Research","award":["2022YNENP3"],"award-info":[{"award-number":["2022YNENP3"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Mitochondrial dysfunction is a pivotal contributor to neurodegeneration. Neurons heavily rely on mitochondrial oxidative metabolism and therefore need highly efficient quality control mechanisms, including proteostasis, mitochondrial biogenesis, fusion\u2013fission dynamics, and mitophagy, to sustain bioenergetics and synaptic function. With aging, deterioration of mitochondrial quality control pathways leads to impaired oxidative phosphorylation, excessive reactive oxygen species generation, calcium imbalance, and defective clearance of damaged organelles, ultimately compromising neuronal viability. Pathological protein aggregates, such as \u03b1-synuclein in Parkinson\u2019s disease, \u03b2-amyloid and tau in Alzheimer\u2019s disease, and misfolded superoxide dismutase 1 and transactive response DNA-binding protein 43 in amyotrophic lateral sclerosis, further aggravate mitochondrial stress, establishing self-perpetuating cycles of neurotoxicity. Such mitochondrial defects underscore mitochondria as a convergent pathogenic hub and a promising therapeutic target for neuroprotection. Intermediate filaments (IFs), traditionally viewed as passive structural elements, have recently gained attention for their roles in cytoplasmic organization, mitochondrial positioning, and energy regulation. Emerging evidence indicates that IF\u2013mitochondria interactions critically influence organelle morphology and function in neurons. This review highlights the multifaceted involvement of mitochondrial dysfunction and IF dynamics in neurodegeneration, emphasizing their potential as targets for novel therapeutic strategies.<\/jats:p>","DOI":"10.3390\/ijms262411852","type":"journal-article","created":{"date-parts":[[2025,12,8]],"date-time":"2025-12-08T15:30:07Z","timestamp":1765207807000},"page":"11852","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Linking Cell Architecture to Mitochondrial Signaling in Neurodegeneration: The Role of Intermediate Filaments"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9567-6983","authenticated-orcid":false,"given":"Emanuele","family":"Marzetti","sequence":"first","affiliation":[{"name":"Fondazione Policlinico Universitario \u201cAgostino Gemelli\u201d IRCCS, L.go A. Gemelli 8, 00168 Rome, Italy"},{"name":"Department of Geriatrics, Orthopedics and Rheumatology, Universit\u00e0 Cattolica del Sacro Cuore, L.go F. Vito 1, 00168 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0009-4190-3875","authenticated-orcid":false,"given":"Rosa","family":"Di Lorenzo","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Environment, Universit\u00e0 degli Studi di Bari Aldo Moro, Via Edoardo Orabona 4, 70125 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5472-2365","authenticated-orcid":false,"given":"Riccardo","family":"Calvani","sequence":"additional","affiliation":[{"name":"Fondazione Policlinico Universitario \u201cAgostino Gemelli\u201d IRCCS, L.go A. Gemelli 8, 00168 Rome, Italy"},{"name":"Department of Geriatrics, Orthopedics and Rheumatology, Universit\u00e0 Cattolica del Sacro Cuore, L.go F. Vito 1, 00168 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7482-9514","authenticated-orcid":false,"given":"H\u00e9lio Jos\u00e9","family":"Coelho-J\u00fanior","sequence":"additional","affiliation":[{"name":"Fondazione Policlinico Universitario \u201cAgostino Gemelli\u201d IRCCS, L.go A. Gemelli 8, 00168 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francesco","family":"Landi","sequence":"additional","affiliation":[{"name":"Fondazione Policlinico Universitario \u201cAgostino Gemelli\u201d IRCCS, L.go A. Gemelli 8, 00168 Rome, Italy"},{"name":"Department of Geriatrics, Orthopedics and Rheumatology, Universit\u00e0 Cattolica del Sacro Cuore, L.go F. Vito 1, 00168 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9148-3129","authenticated-orcid":false,"given":"Vito","family":"Pesce","sequence":"additional","affiliation":[{"name":"Department of Biosciences, Biotechnologies and Environment, Universit\u00e0 degli Studi di Bari Aldo Moro, Via Edoardo Orabona 4, 70125 Bari, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7032-3487","authenticated-orcid":false,"given":"Anna","family":"Picca","sequence":"additional","affiliation":[{"name":"Fondazione Policlinico Universitario \u201cAgostino Gemelli\u201d IRCCS, L.go A. Gemelli 8, 00168 Rome, Italy"},{"name":"Department of Medicine and Surgery, LUM University, Str. Statale 100, 70010 Casamassima, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,12,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1721","DOI":"10.1152\/physrev.00041.2021","article-title":"Mitochondrial quality control in health and in Parkinson\u2019s disease","volume":"102","author":"Eldeeb","year":"2022","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Dominiak, A., Gawinek, E., Banaszek, A.A., and Wilkaniec, A. (2025). Mitochondrial quality control in neurodegeneration and cancer: A common denominator, distinct therapeutic challenges. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26178693"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Wang, P., Deng, J., Dong, J., Liu, J., Bigio, E.H., Mesulam, M., Wang, T., Sun, L., Wang, L., and Lee, A.Y.L. (2019). TDP-43 induces mitochondrial damage and activates the mitochondrial unfolded protein response. PLoS Genet., 15.","DOI":"10.1371\/journal.pgen.1007947"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1038\/emboj.2012.38","article-title":"Mitochondrial quality control: A matter of life and death for neurons","volume":"31","author":"Rugarli","year":"2012","journal-title":"EMBO J."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1038\/nrneurol.2014.228","article-title":"Disturbed mitochondrial dynamics and neurodegenerative disorders","volume":"11","author":"Carelli","year":"2015","journal-title":"Nat. Rev. Neurol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1038\/s41536-020-00107-x","article-title":"Mitochondrial dysfunction in neurological disorders: Exploring mitochondrial transplantation","volume":"5","author":"Norat","year":"2020","journal-title":"NPJ Regen. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1042\/BJ20071072","article-title":"Vimentin supports mitochondrial morphology and organization","volume":"410","author":"Tang","year":"2008","journal-title":"Biochem. J."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1083\/jcb.200603161","article-title":"New consensus nomenclature for mammalian keratins","volume":"174","author":"Schweizer","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"608","DOI":"10.1016\/j.tcb.2005.09.004","article-title":"Cellular integrity plus: Organelle-related and protein-targeting functions of intermediate filaments","volume":"15","author":"Toivola","year":"2005","journal-title":"Trends Cell Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1267\/ahc.10009","article-title":"Seven kinds of intermediate filament networks in the cytoplasm of polarized cells: Structure and function","volume":"43","author":"Iwatsuki","year":"2010","journal-title":"Acta Histochem. Cytochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1007\/s00418-013-1101-1","article-title":"Review on intermediate filaments of the nervous system and their pathological alterations","volume":"140","author":"Eyer","year":"2013","journal-title":"Histochem. Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1096\/fj.10-179408","article-title":"Synemin isoforms differentially organize cell junctions and desmin filaments in neonatal cardiomyocytes","volume":"26","author":"Lund","year":"2012","journal-title":"FASEB J."},{"key":"ref_13","first-page":"665","article-title":"Nestin structure and predicted function in cellular cytoskeletal organisation","volume":"20","author":"Michalczyk","year":"2005","journal-title":"Histol. Histopathol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"4200","DOI":"10.1038\/s41467-019-12029-4","article-title":"Vimentin filaments interact with the actin cortex in mitosis allowing normal cell division","volume":"10","author":"Duarte","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Jokhadar, \u0160.Z., Stojkovi\u0107, B., Vidak, M., Sor\u010dan, T., Liovic, M., Gouveia, M., Travasso, R.D.M., and Derganc, J. (2020). Cortical stiffness of keratinocytes measured by lateral indentation with optical tweezers. PLoS ONE, 15.","DOI":"10.1101\/2020.03.31.018473"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Ndiaye, A.B., Koenderink, G.H., and Shemesh, M. (2022). Intermediate filaments in cellular mechanoresponsiveness: Mediating cytoskeletal crosstalk from membrane to nucleus and back. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.882037"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Stenvall, C.G.A., Nystr\u00f6m, J.H., Butler-Hallissey, C., Jansson, T., Heikkil\u00e4, T.R.H., Adam, S.A., Foisner, R., Goldman, R.D., Ridge, K.M., and Toivola, D.M. (2022). Cytoplasmic keratins couple with and maintain nuclear envelope integrity in colonic epithelial cells. Mol. Biol. Cell, 33.","DOI":"10.1091\/mbc.E20-06-0387"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1016\/j.jcmgh.2021.12.009","article-title":"Desmoplakin maintains transcellular keratin scaffolding and protects from intestinal injury","volume":"13","author":"Gross","year":"2022","journal-title":"Cell. Mol. Gastroenterol. Hepatol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1006\/geno.1995.1036","article-title":"Structural organization of the human gene (LMNB1) encoding nuclear lamin B1","volume":"27","author":"Lin","year":"1995","journal-title":"Genomics"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Graziano, S., Coll-Bonfill, N., Teodoro-Castro, B., Kuppa, S., Jackson, J., Shashkova, E., Mahajan, U., Vindigni, A., Antony, E., and Gonzalo, S. (2021). Lamin A\/C recruits ssDNA protective proteins RPA and RAD51 to stalled replication forks to maintain fork stability. J. Biol. Chem., 297.","DOI":"10.1101\/2021.06.22.449466"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1083\/jcb.132.4.643","article-title":"Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells","volume":"132","author":"Goulielmos","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Sanghvi-Shah, R., and Weber, G.F. (2017). Intermediate filaments at the junction of mechanotransduction, migration, and development. Front. Cell Dev. Biol., 5.","DOI":"10.3389\/fcell.2017.00081"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Schwarz, N., and Leube, R.E. (2016). Intermediate filaments as organizers of cellular space: How they affect mitochondrial structure and function. Cells, 5.","DOI":"10.3390\/cells5030030"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1134\/S0006297924040114","article-title":"Unique role of vimentin in the intermediate filament proteins family","volume":"89","author":"Alieva","year":"2024","journal-title":"Biochem. Mosc."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1083\/jcb.131.5.1315","article-title":"Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons","volume":"131","author":"Morris","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1146\/annurev.biochem.73.011303.073823","article-title":"Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds","volume":"73","author":"Herrmann","year":"2004","journal-title":"Annu. Rev. Biochem."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Marzetti, E., Di Lorenzo, R., Calvani, R., Pesce, V., Landi, F., Coelho-J\u00fanior, H.J., and Picca, A. (2025). From cell architecture to mitochondrial signaling: Role of intermediate filaments in health, aging, and disease. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26031100"},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Romano, R., Del Fiore, V.S., and Bucci, C. (2022). Role of the intermediate filament protein peripherin in health and disease. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232315416"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/0092-8674(82)90323-3","article-title":"Putative association of mitochondria with a subpopulation of intermediate-sized filaments in cultured human skin fibroblasts","volume":"31","author":"Bravo","year":"1982","journal-title":"Cell"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1083\/jcb.150.6.1283","article-title":"Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function","volume":"150","author":"Milner","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"9046","DOI":"10.1523\/JNEUROSCI.23-27-09046.2003","article-title":"Mechanisms of mitochondria-neurofilament interactions","volume":"23","author":"Wagner","year":"2003","journal-title":"J. Neurosci."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Fern\u00e1ndez Casafuz, A.B., De Rossi, M.C., and Bruno, L. (2023). Mitochondrial cellular organization and shape fluctuations are differentially modulated by cytoskeletal networks. Sci. Rep., 13, Erratum in Sci. Rep. 2023, 13, 7543. https:\/\/doi.org\/10.1038\/s41598-023-34566-1.","DOI":"10.1038\/s41598-023-31121-w"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"114157","DOI":"10.1016\/j.expneurol.2022.114157","article-title":"Gas5 inhibition promotes the axon regeneration in the adult mammalian nervous system","volume":"356","author":"Han","year":"2022","journal-title":"Exp. Neurol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1007\/s10571-022-01313-5","article-title":"Identifying genes that affect differentiation of human neural stem cells and myelination of mature oligodendrocytes","volume":"43","author":"Ye","year":"2023","journal-title":"Cell. Mol. Neurobiol."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Aragona, M., Porcino, C., Briglia, M., Mhalhel, K., Abbate, F., Levanti, M., Montalbano, G., Laur\u00e0, R., Lauriano, E.R., and German\u00e0, A. (2023). Vimentin localization in the zebrafish oral cavity: A potential role in taste buds regeneration. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms242115619"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1083\/jcb.200710151","article-title":"Plectin isoform 1b mediates mitochondrion-intermediate filament network linkage and controls organelle shape","volume":"181","author":"Winter","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"3181","DOI":"10.1093\/hmg\/ddg345","article-title":"Plectin 5\u2032-transcript diversity: Short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms","volume":"12","author":"Rezniczek","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"2282","DOI":"10.1091\/mbc.e10-09-0766","article-title":"Vimentin intermediate filaments modulate the motility of mitochondria","volume":"22","author":"Nekrasova","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1242\/bio.011874","article-title":"Vimentin is involved in regulation of mitochondrial motility and membrane potential by Rac1","volume":"4","author":"Matveeva","year":"2015","journal-title":"Biol. Open"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1089\/dna.2005.24.680","article-title":"Spontaneously immortalized mouse embryo fibroblasts: Growth behavior of wild-type and vimentin-deficient cells in relation to mitochondrial structure and activity","volume":"24","author":"Tolstonog","year":"2005","journal-title":"DNA Cell Biol."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Kuznetsov, A.V., Javadov, S., Grimm, M., Margreiter, R., Ausserlechner, M.J., and Hagenbuchner, J. (2020). Crosstalk between mitochondria and cytoskeleton in cardiac cells. Cells, 9.","DOI":"10.3390\/cells9010222"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1096\/fj.14-259903","article-title":"Mitochondrial membrane potential is regulated by vimentin intermediate filaments","volume":"29","author":"Chernoivanenko","year":"2015","journal-title":"FASEB J."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Dayal, A.A., Parfenteva, O.I., Wang, H., Gebreselase, B.A., Gyoeva, F.K., Alieva, I.B., and Minin, A.A. (2024). Vimentin intermediate filaments maintain membrane potential of mitochondria in growing neurites. Biology, 13.","DOI":"10.20944\/preprints202411.1173.v1"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1111\/j.1349-7006.2006.00161.x","article-title":"Regulatory mechanisms and functions of intermediate filaments: A study using site- and phosphorylation state-specific antibodies","volume":"97","author":"Izawa","year":"2006","journal-title":"Cancer Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/s10974-008-9139-8","article-title":"Mice expressing L345P Mutant desmin exhibit morphological and functional changes of skeletal and cardiac mitochondria","volume":"29","author":"Kostareva","year":"2008","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"33267","DOI":"10.1074\/jbc.274.47.33267","article-title":"Modulation of mitochondrial Ca2+ homeostasis by Bcl-2","volume":"274","author":"Zhu","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1529\/biophysj.103.036210","article-title":"Analysis of functional coupling: Mitochondrial creatine kinase and adenine nucleotide translocase","volume":"87","author":"Vendelin","year":"2004","journal-title":"Biophys. J."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Hol, E.M., and Capetanaki, Y. (2017). Type III intermediate filaments desmin, glial fibrillary acidic protein (GFAP), vimentin, and peripherin. Cold Spring Harb. Perspect. Biol., 9.","DOI":"10.1101\/cshperspect.a021642"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"4521","DOI":"10.1091\/mbc.e08-03-0284","article-title":"Glial fibrillary acidic protein filaments can tolerate the incorporation of assembly-compromised GFAP-delta, but with consequences for filament organization and alphaB-crystallin association","volume":"19","author":"Wen","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"23996","DOI":"10.1074\/jbc.274.34.23996","article-title":"Intermediate filament protein partnership in astrocytes","volume":"274","author":"Eliasson","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.ceb.2015.02.004","article-title":"Glial fibrillary acidic protein (GFAP) and the astrocyte intermediate filament system in diseases of the central nervous system","volume":"32","author":"Hol","year":"2015","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.molcel.2010.08.004","article-title":"Identification of regulators of chaperone-mediated autophagy","volume":"39","author":"Bandyopadhyay","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"295","DOI":"10.4161\/auto.4144","article-title":"Chaperone-mediated autophagy","volume":"3","author":"Dice","year":"2007","journal-title":"Autophagy"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2320","DOI":"10.1002\/stem.1196","article-title":"Astrocytes negatively regulate neurogenesis through the Jagged1-mediated Notch pathway","volume":"30","author":"Wilhelmsson","year":"2012","journal-title":"Stem Cells"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"15199","DOI":"10.1523\/JNEUROSCI.2049-15.2015","article-title":"Reciprocal regulation of mitochondrial dynamics and calcium signaling in astrocyte processes","volume":"35","author":"Jackson","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"15996","DOI":"10.1523\/JNEUROSCI.2068-15.2015","article-title":"Miro1 regulates activity-driven positioning of mitochondria within astrocytic processes apposed to synapses to regulate intracellular calcium signaling","volume":"35","author":"Stephen","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.1016\/j.yexcr.2007.04.004","article-title":"GFAP and its role in Alexander disease","volume":"313","author":"Quinlan","year":"2007","journal-title":"Exp. Cell Res."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Gao, L., Zhang, Z., Lu, J., and Pei, G. (2019). Mitochondria are dynamically transferring between human neural cells and alexander disease-associated GFAP mutations impair the astrocytic transfer. Front. Cell Neurosci., 13.","DOI":"10.3389\/fncel.2019.00316"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1016\/j.trecan.2017.10.003","article-title":"Mitochondrial transfer in the leukemia microenvironment","volume":"3","author":"Griessinger","year":"2017","journal-title":"Trends Cancer"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Torralba, D., Baixauli, F., and S\u00e1nchez-Madrid, F. (2016). Mitochondria know no boundaries: Mechanisms and functions of intercellular mitochondrial transfer. Front. Cell Dev. Biol., 4.","DOI":"10.3389\/fcell.2016.00107"},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Simone, L., Capobianco, D.L., Di Palma, F., Binda, E., Legnani, F.G., Vescovi, A.L., Svelto, M., and Pisani, F. (2023). GFAP serves as a structural element of tunneling nanotubes between glioblastoma cells and could play a role in the intercellular transfer of mitochondria. Front. Cell Dev. Biol., 11.","DOI":"10.3389\/fcell.2023.1221671"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"10006","DOI":"10.1523\/JNEUROSCI.2580-06.2006","article-title":"Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS","volume":"26","author":"Yuan","year":"2006","journal-title":"J. Neurosci."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.mcn.2017.05.010","article-title":"The third wave: Intermediate filaments in the maturing nervous system","volume":"84","author":"Kirkcaldie","year":"2017","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.ceb.2020.10.011","article-title":"The Dazzling Rise of Neurofilaments: Physiological functions and roles as biomarkers","volume":"68","author":"Bomont","year":"2021","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1083\/jcb.200202037","article-title":"Gene replacement in mice reveals that the heavily phosphorylated tail of neurofilament heavy subunit does not affect axonal caliber or the transit of cargoes in slow axonal transport","volume":"158","author":"Rao","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1002\/jnr.10212","article-title":"Overexpression of neurofilament h disrupts normal cell structure and function","volume":"68","author":"Szebenyi","year":"2002","journal-title":"J. Neurosci. Res."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/0022-2836(88)90459-7","article-title":"Structure of the peripheral domains of neurofilaments revealed by low angle rotary shadowing","volume":"202","author":"Hisanaga","year":"1988","journal-title":"J. Mol. Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"4019","DOI":"10.1016\/S0021-9258(18)32770-4","article-title":"The distribution of phosphorylation sites among identified proteolytic fragments of mammalian neurofilaments","volume":"258","author":"Julien","year":"1983","journal-title":"J. Biol. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1002\/jemt.1070270305","article-title":"Interactions between brain mitochondria and cytoskeleton: Evidence for specialized outer membrane domains involved in the association of cytoskeleton-associated proteins to mitochondria in situ and in vitro","volume":"27","author":"Leterrier","year":"1994","journal-title":"Microsc. Res. Tech."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1096\/fj.11-196345","article-title":"Normal role of the low-molecular-weight neurofilament protein in mitochondrial dynamics and disruption in Charcot-Marie-Tooth disease","volume":"26","author":"Gentil","year":"2012","journal-title":"FASEB J."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"3213","DOI":"10.1096\/fj.09-129585","article-title":"Real-time imaging reveals defects of fast axonal transport induced by disorganization of intermediate filaments","volume":"23","author":"Perrot","year":"2009","journal-title":"FASEB J."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"2837","DOI":"10.1093\/hmg\/11.23.2837","article-title":"Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport","volume":"11","author":"Brownlees","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"4232","DOI":"10.1523\/JNEUROSCI.6248-09.2010","article-title":"Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro\/Milton complex","volume":"30","author":"Misko","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0248-4900(92)90193-5","article-title":"Structure of the mouse gene encoding peripherin: A neuronal intermediate filament protein","volume":"76","author":"Karpov","year":"1992","journal-title":"Biol. Cell"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1016\/0896-6273(89)90228-6","article-title":"Structure of the gene encoding peripherin, an NGF-regulated neuronal-specific Type III intermediate filament protein","volume":"2","author":"Thompson","year":"1989","journal-title":"Neuron"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1006\/geno.1994.1410","article-title":"The structure of the human peripherin gene (PRPH) and identification of potential regulatory elements","volume":"22","author":"Foley","year":"1994","journal-title":"Genomics"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1002\/j.1460-2075.1989.tb03564.x","article-title":"Multiple mRNAs encode peripherin, a neuronal intermediate filament protein","volume":"8","author":"Landon","year":"1989","journal-title":"EMBO J."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1111\/j.1471-4159.2007.05198.x","article-title":"A Novel peripherin isoform generated by alternative translation is required for normal filament network formation","volume":"104","author":"McLean","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1833","DOI":"10.1523\/JNEUROSCI.3222-07.2008","article-title":"An aggregate-inducing peripherin isoform generated through intron retention is upregulated in amyotrophic lateral sclerosis and associated with disease pathology","volume":"28","author":"Xiao","year":"2008","journal-title":"J. Neurosci."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1159\/000112348","article-title":"Regulation of peripherin in mouse neuroblastoma and rat PC 12 pheochromocytoma cell lines","volume":"6","author":"Portier","year":"1983","journal-title":"Dev. Neurosci."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1523\/JNEUROSCI.08-02-00555.1988","article-title":"Distribution of a novel 57 kDa intermediate filament (IF) protein in the nervous system","volume":"8","author":"Parysek","year":"1988","journal-title":"J. Neurosci."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1083\/jcb.106.1.181","article-title":"A Nerve growth factor-regulated messenger RNA encodes a new intermediate filament protein","volume":"106","author":"Leonard","year":"1988","journal-title":"J. Cell Biol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1002\/jnr.490300110","article-title":"Some neural intermediate filaments contain both peripherin and the neurofilament proteins","volume":"30","author":"Parysek","year":"1991","journal-title":"J. Neurosci. Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"8501","DOI":"10.1523\/JNEUROSCI.1081-12.2012","article-title":"Peripherin is a subunit of peripheral nerve neurofilaments: Implications for differential vulnerability of CNS and peripheral nervous system axons","volume":"32","author":"Yuan","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1083\/jcb.147.3.531","article-title":"Late onset of motor neurons in mice overexpressing wild-type peripherin","volume":"147","author":"Beaulieu","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1046\/j.1471-4159.2003.01653.x","article-title":"Peripherin-mediated death of motor neurons rescued by overexpression of neurofilament NF-H proteins","volume":"85","author":"Beaulieu","year":"2003","journal-title":"J. Neurochem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"3495","DOI":"10.1091\/mbc.11.10.3495","article-title":"Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein\/dynactin","volume":"11","author":"Shah","year":"2000","journal-title":"Mol. Biol. Cell"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"3799","DOI":"10.1242\/jcs.112.21.3799","article-title":"Kinesin-mediated transport of neurofilament protein oligomers in growing axons","volume":"112","author":"Yabe","year":"1999","journal-title":"J. Cell Sci."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1002\/jnr.490270312","article-title":"Differential regulation of peripherin and neurofilament gene expression in regenerating rat DRG Nneurons","volume":"27","author":"Wong","year":"1990","journal-title":"J. Neurosci. Res."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"4562","DOI":"10.1093\/brain\/awad234","article-title":"Peripherin is a biomarker of axonal damage in peripheral nervous system disease","volume":"146","author":"Keddie","year":"2023","journal-title":"Brain"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"3206","DOI":"10.1111\/ejn.16111","article-title":"Peripherin: A proposed biomarker of traumatic axonal injury triggered by mechanical force","volume":"58","author":"Fang","year":"2023","journal-title":"Eur. J. Neurosci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1242\/jcs.059113","article-title":"Syncoilin modulates peripherin filament networks and is necessary for large-calibre motor neurons","volume":"123","author":"Clarke","year":"2010","journal-title":"J. Cell Sci."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"5069","DOI":"10.1091\/mbc.e03-06-0376","article-title":"A Role for intermediate filaments in determining and maintaining the shape of nerve cells","volume":"14","author":"Helfand","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1046\/j.1471-4159.2002.00853.x","article-title":"Reduced number of unmyelinated sensory axons in peripherin null mice","volume":"81","author":"Nguyen","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2925","DOI":"10.1242\/dev.001925","article-title":"Spatiotemporal definition of neurite outgrowth, refinement and retraction in the developing mouse cochlea","volume":"134","author":"Huang","year":"2007","journal-title":"Development"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/1749-8104-7-38","article-title":"Synaptic profiles during neurite extension, refinement and retraction in the developing cochlea","volume":"7","author":"Huang","year":"2012","journal-title":"Neural Dev."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1159\/000354238","article-title":"Functional interaction between amyloid-\u03b2 precursor protein and peripherin neurofilaments: A shared pathway leading to Alzheimer\u2019s disease and amyotrophic lateral sclerosis?","volume":"13","author":"Muresan","year":"2014","journal-title":"Neurodegener. Dis."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1159\/000439256","article-title":"Shared molecular mechanisms in Alzheimer\u2019s disease and amyotrophic lateral sclerosis: Neurofilament-dependent transport of SAPP, FUS, TDP-43 and SOD1, with endoplasmic reticulum-like tubules","volume":"16","author":"Muresan","year":"2016","journal-title":"Neurodegener. Dis."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1007\/s00401-012-1063-8","article-title":"Charcot-Marie-Tooth type 2B disease-causing RAB7A mutant proteins show altered interaction with the neuronal intermediate filament peripherin","volume":"125","author":"Cogli","year":"2013","journal-title":"Acta Neuropathol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1046\/j.0305-1846.2001.00332.x","article-title":"Apoptosis in amyotrophic lateral sclerosis: A review of the evidence","volume":"27","author":"Sathasivam","year":"2001","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"16653","DOI":"10.1074\/jbc.M710436200","article-title":"Protein kinase C\u03b5 binds peripherin and induces its aggregation, which is accompanied by apoptosis of neuroblastoma cells","volume":"283","author":"Sunesson","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"23491","DOI":"10.1074\/jbc.M611703200","article-title":"Identification of peripherin as a akt substrate in neurons","volume":"282","author":"Konishi","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1021\/pr100742r","article-title":"ATP Enhances neuronal differentiation of PC12 Cells by activating PKC\u03b1 interactions with cytoskeletal proteins","volume":"10","author":"Nielsen","year":"2011","journal-title":"J. Proteome Res."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1046\/j.1471-4159.1996.67041365.x","article-title":"Interleukin-6 induces expression of peripherin and cooperates with Trk receptor signaling to promote neuronal differentiation in PC12 cells","volume":"67","author":"Sterneck","year":"1996","journal-title":"J. Neurochem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"5116","DOI":"10.1074\/jbc.M002959200","article-title":"Fibroblast growth factor receptor 3 induces gene expression primarily through ras-independent signal transduction pathways","volume":"276","author":"Choi","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_106","first-page":"3156","article-title":"Identification and characterization of mRNAs regulated by nerve growth factor in PC12 cells","volume":"7","author":"Leonard","year":"1987","journal-title":"Mol. Cell. Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/j.bbalip.2013.11.014","article-title":"MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond","volume":"1841","author":"Vance","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1046\/j.1432-1327.1999.00658.x","article-title":"Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact","volume":"264","author":"Achleitner","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"39224","DOI":"10.1074\/jbc.M302301200","article-title":"Stable interactions between mitochondria and endoplasmic reticulum allow rapid accumulation of calcium in a subpopulation of mitochondria","volume":"278","author":"Filippin","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1083\/jcb.200608073","article-title":"Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels","volume":"175","author":"Szabadkai","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.cell.2010.06.007","article-title":"Essential regulation of cell bioenergetics by constitutive InsP3 receptor Ca2+ transfer to mitochondria","volume":"142","author":"Miller","year":"2010","journal-title":"Cell"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/20959","article-title":"Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC","volume":"399","author":"Shimizu","year":"1999","journal-title":"Nature"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.chemphyslip.2013.12.008","article-title":"Mitochondrial cardiolipin\/phospholipid trafficking: The role of membrane contact site complexes and lipid transfer proteins","volume":"179","author":"Schlattner","year":"2014","journal-title":"Chem. Phys. Lipids"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1242\/jcs.01667","article-title":"Identification of trichoplein, a novel keratin filament-binding protein","volume":"118","author":"Nishizawa","year":"2005","journal-title":"J. Cell Sci."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1038\/embor.2010.151","article-title":"Trichoplein\/mitostatin regulates endoplasmic reticulum-mitochondria juxtaposition","volume":"11","author":"Cerqua","year":"2010","journal-title":"EMBO Rep."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1083\/jcb.201404147","article-title":"A keratin scaffold regulates epidermal barrier formation, mitochondrial lipid composition, and activity","volume":"211","author":"Kumar","year":"2015","journal-title":"J. Cell Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"2245","DOI":"10.1091\/mbc.12.8.2245","article-title":"Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells","volume":"12","author":"Smirnova","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"36373","DOI":"10.1074\/jbc.M303758200","article-title":"HFis1, a novel component of the mammalian mitochondrial fission machinery","volume":"278","author":"James","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.1091\/mbc.e07-12-1287","article-title":"The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells","volume":"19","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1242\/jcs.114.5.867","article-title":"Control of mitochondrial morphology by a human mitofusin","volume":"114","author":"Santel","year":"2001","journal-title":"J. Cell Sci."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"15927","DOI":"10.1073\/pnas.0407043101","article-title":"OPA1 requires mitofusin 1 to promote mitochondrial fusion","volume":"101","author":"Cipolat","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"3939","DOI":"10.1080\/15548627.2021.1897962","article-title":"KRT8 (keratin 8) attenuates necrotic cell death by facilitating mitochondrial fission-mediated mitophagy through interaction with plec (plectin)","volume":"17","author":"Baek","year":"2021","journal-title":"Autophagy"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1016\/j.bbabio.2006.04.013","article-title":"The relationship between mitochondrial shape and function and the cytoskeleton","volume":"1757","author":"Anesti","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.cophys.2018.03.003","article-title":"Mitochondrial-cytoskeletal interactions: Dynamic associations that facilitate network function and remodeling","volume":"3","author":"Moore","year":"2018","journal-title":"Curr. Opin. Physiol."},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"M\u00f3nico, A., Duarte, S., Pajares, M.A., and P\u00e9rez-Sala, D. (2019). Vimentin Disruption by Lipoxidation and Electrophiles: Role of the Cysteine Residue and Filament Dynamics. Redox Biol., 23.","DOI":"10.1016\/j.redox.2019.101098"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"5304","DOI":"10.1111\/febs.15321","article-title":"Vimentin S-glutathionylation at Cys328 inhibits filament elongation and induces severing of mature filaments in vitro","volume":"287","author":"Szczepanowski","year":"2020","journal-title":"FEBS J."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Lois-Bermejo, I., Gonz\u00e1lez-Jim\u00e9nez, P., Duarte, S., Pajares, M.A., and P\u00e9rez-Sala, D. (2022). Vimentin tail segments are differentially exposed at distinct cellular locations and in response to stress. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.908263"},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Griesser, E., Vemula, V., M\u00f3nico, A., P\u00e9rez-Sala, D., and Fedorova, M. (2021). Dynamic posttranslational modifications of cytoskeletal proteins unveil hot spots under nitroxidative stress. Redox Biol., 44.","DOI":"10.1016\/j.redox.2021.102014"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1016\/j.cell.2020.02.012","article-title":"A quantitative tissue-specific landscape of protein redox regulation during aging","volume":"180","author":"Xiao","year":"2020","journal-title":"Cell"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"7287","DOI":"10.1038\/ncomms8287","article-title":"Vimentin filament organization and stress sensing depend on its single cysteine residue and zinc binding","volume":"6","author":"Oeste","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Huynh, T.N., Toperzer, J., Scherer, A., Gumina, A., Brunetti, T., Mansour, M.K., Markovitz, D.M., and Russo, B.C. (2024). Vimentin regulates mitochondrial ROS production and inflammatory responses of neutrophils. Front. Immunol., 15.","DOI":"10.3389\/fimmu.2024.1416275"},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"H\u00e5versen, L., Sundelin, J.P., Mardinoglu, A., Rutberg, M., St\u00e5hlman, M., Wilhelmsson, U., Hult\u00e9n, L.M., Pekny, M., Fogelstrand, P., and Bentzon, J.F. (2018). Vimentin deficiency in macrophages induces increased oxidative stress and vascular inflammation but attenuates atherosclerosis in mice. Sci. Rep., 8.","DOI":"10.1038\/s41598-018-34659-2"},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Elsnicova, B., Hornikova, D., Tibenska, V., Kolar, D., Tlapakova, T., Schmid, B., Mallek, M., Eggers, B., Schl\u00f6tzer-Schrehardt, U., and Peeva, V. (2022). Desmin knock-out cardiomyopathy: A heart on the verge of metabolic crisis. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms231912020"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Viedma-Poyatos, \u00c1., Gonz\u00e1lez-Jim\u00e9nez, P., Pajares, M.A., and P\u00e9rez-Sala, D. (2022). Alexander disease GFAP R239C mutant shows increased susceptibility to lipoxidation and elicits mitochondrial dysfunction and oxidative stress. Redox Biol., 55.","DOI":"10.1016\/j.redox.2022.102415"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2755","DOI":"10.1111\/febs.15864","article-title":"New roles for desmin in the maintenance of muscle homeostasis","volume":"289","author":"Agnetti","year":"2022","journal-title":"FEBS J."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1093\/hmg\/ddw081","article-title":"Intermediate filament aggregates cause mitochondrial dysmotility and increase energy demands in giant axonal neuropathy","volume":"25","author":"Israeli","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"5369","DOI":"10.1091\/mbc.e04-03-0272","article-title":"The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton","volume":"15","author":"Styers","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Margiotta, A., and Bucci, C. (2016). Role of intermediate filaments in vesicular traffic. Cells, 5.","DOI":"10.3390\/cells5020020"},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Romano, R., Cordella, P., and Bucci, C. (2025). The type III intermediate filament protein peripherin regulates lysosomal degradation activity and autophagy. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26020549"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"6494","DOI":"10.1128\/MCB.23.18.6494-6506.2003","article-title":"Phagosomes fuse with late endosomes and\/or lysosomes by extension of membrane protrusions along microtubules: Role of Rab7 and RILP","volume":"23","author":"Harrison","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"4837","DOI":"10.1242\/jcs.01370","article-title":"Role for Rab7 in maturation of late autophagic vacuoles","volume":"117","author":"Bucci","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1111\/jnc.12928","article-title":"A Two-hybrid screen identifies an unconventional role for the intermediate filament peripherin in regulating the subcellular distribution of the SNAP25-interacting protein, SIP30","volume":"131","author":"Gentil","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.bbrc.2010.11.098","article-title":"Identification of complexin ii in astrocytes: A possible regulator of glutamate release in these cells","volume":"404","author":"Hazell","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/S1474-4422(21)00465-8","article-title":"Recent advances in the diagnosis and prognosis of amyotrophic lateral sclerosis","volume":"21","author":"Goutman","year":"2022","journal-title":"Lancet Neurol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1186\/s40478-022-01418-4","article-title":"BDNF-dependent modulation of axonal transport is selectively impaired in ALS","volume":"10","author":"Tosolini","year":"2022","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.neulet.2016.11.002","article-title":"A view from the ending: Axonal dieback and regeneration following SCI","volume":"652","author":"Hill","year":"2017","journal-title":"Neurosci. Lett."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"\u0160tetk\u00e1rov\u00e1, I., and Ehler, E. (2021). Diagnostics of amyotrophic lateral sclerosis: Up to date. Diagnostics, 11.","DOI":"10.3390\/diagnostics11020231"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/nrn3380","article-title":"Axonal transport deficits and neurodegenerative diseases","volume":"14","author":"Millecamps","year":"2013","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.jns.2003.08.016","article-title":"Expression of peripherin in ubiquinated inclusions of amyotrophic lateral sclerosis","volume":"217","author":"He","year":"2004","journal-title":"J. Neurol. Sci."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/0006-8993(90)90832-V","article-title":"Regulation of peripherin and neurofilament expression in regenerating rat motor neurons","volume":"529","author":"Troy","year":"1990","journal-title":"Brain Res."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1097\/00005072-199209000-00008","article-title":"Peripherin and neurofilament protein coexist in spinal spheroids of motor neuron disease","volume":"51","author":"Corbo","year":"1992","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.jns.2010.12.023","article-title":"Peripherin partially localizes in bunina bodies in amyotrophic lateral sclerosis","volume":"302","author":"Mizuno","year":"2011","journal-title":"J. Neurol. Sci."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1111\/neup.12484","article-title":"Colocalization of Bunina bodies and TDP-43 inclusions in a case of sporadic amyotrophic lateral sclerosis with Lewy body-like hyaline inclusions","volume":"38","author":"Miki","year":"2018","journal-title":"Neuropathology"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1083\/jcb.200107058","article-title":"Apoptotic death of neurons exhibiting peripherin aggregates is mediated by the proinflammatory cytokine tumor necrosis factor-alpha","volume":"155","author":"Robertson","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Lee, W.C., Chen, Y.Y., Kan, D., and Chien, C.L. (2012). A neuronal death model: Overexpression of neuronal intermediate filament protein peripherin in PC12 cells. J. Biomed. Sci., 19.","DOI":"10.1186\/1423-0127-19-8"},{"key":"ref_156","doi-asserted-by":"crossref","unstructured":"Bordoni, M., Pansarasa, O., Scarian, E., Cristofani, R., Leone, R., Fantini, V., Garofalo, M., Diamanti, L., Bernuzzi, S., and Gagliardi, S. (2022). Lysosomes dysfunction causes mitophagy impairment in PBMCs of sporadic ALS patients. Cells, 11.","DOI":"10.3390\/cells11081272"},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Genin, E.C., Abou-Ali, M., and Paquis-Flucklinger, V. (2023). Mitochondria, a key target in amyotrophic lateral sclerosis pathogenesis. Genes, 14.","DOI":"10.3390\/genes14111981"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Grel, H., Woznica, D., Ratajczak, K., Kalwarczyk, E., Anchimowicz, J., Switlik, W., Olejnik, P., Zielonka, P., Stobiecka, M., and Jakiela, S. (2023). Mitochondrial dynamics in neurodegenerative diseases: Unraveling the role of fusion and fission processes. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241713033"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1126\/science.1086071","article-title":"Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice","volume":"302","author":"Clement","year":"2003","journal-title":"Science"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1139\/o99-003","article-title":"Interactions between peripherin and neurofilaments in cultured cells: Disruption of peripherin assembly by the NF-M and NF-H subunits","volume":"77","author":"Beaulieu","year":"1999","journal-title":"Biochem. Cell Biol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"5321","DOI":"10.1523\/JNEUROSCI.20-14-05321.2000","article-title":"Formation of intermediate filament protein aggregates with disparate effects in two transgenic mouse models lacking the neurofilament light subunit","volume":"20","author":"Beaulieu","year":"2000","journal-title":"J. Neurosci."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.brainres.2018.10.032","article-title":"MiR-105 and MiR-9 Regulate the mRNA stability of neuronal intermediate filaments. implications for the pathogenesis of amyotrophic lateral sclerosis (ALS)","volume":"1706","author":"Hawley","year":"2019","journal-title":"Brain Res."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"552.e1","DOI":"10.1016\/j.neurobiolaging.2010.02.011","article-title":"A novel peripherin gene (PRPH) mutation identified in one sporadic amyotrophic lateral sclerosis patient","volume":"32","author":"Corrado","year":"2011","journal-title":"Neurobiol. Aging"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"45951","DOI":"10.1074\/jbc.M408139200","article-title":"A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosis","volume":"279","author":"Gowing","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1111\/j.1750-3639.2004.tb00066.x","article-title":"A pathogenic peripherin gene mutation in a patient with amyotrophic lateral sclerosis","volume":"14","author":"Leung","year":"2004","journal-title":"Brain Pathol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1083\/jcb.200205027","article-title":"A neurotoxic peripherin splice variant in a mouse model of ALS","volume":"160","author":"Robertson","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1111\/j.1471-4159.2006.03932.x","article-title":"Defective axonal transport of neurofilament proteins in neurons overexpressing peripherin","volume":"98","author":"Millecamps","year":"2006","journal-title":"J. Neurochem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/S0969-9961(03)00036-6","article-title":"Peripherin is not a contributing factor to motor neuron disease in a mouse model of amyotrophic lateral sclerosis caused by mutant superoxide dismutase","volume":"13","author":"Beaulieu","year":"2003","journal-title":"Neurobiol. Dis."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"2974","DOI":"10.1523\/JNEUROSCI.19-08-02974.1999","article-title":"Overexpression of alpha-internexin causes abnormal neurofilamentous accumulations and motor coordination deficits in transgenic mice","volume":"19","author":"Ching","year":"1999","journal-title":"J. Neurosci."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/j.bbadis.2006.05.004","article-title":"Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis","volume":"1762","author":"Rakhit","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"2716","DOI":"10.1523\/JNEUROSCI.5689-03.2004","article-title":"3\u2032 Untranslated region in a light neurofilament (NF-L) mRNA triggers aggregation of NF-L and mutant superoxide dismutase 1 proteins in neuronal cells","volume":"24","author":"Lin","year":"2004","journal-title":"J. Neurosci."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"3143","DOI":"10.1007\/s12035-017-0543-1","article-title":"TDP-43 and cytoskeletal proteins in ALS","volume":"55","author":"Oberstadt","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1016\/j.expneurol.2003.10.004","article-title":"Amyotrophic lateral sclerosis is a distal axonopathy: Evidence in mice and man","volume":"185","author":"Fischer","year":"2004","journal-title":"Exp. Neurol."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.jchemneu.2016.03.003","article-title":"Axonal degeneration, distal collateral branching and neuromuscular junction architecture alterations occur prior to symptom onset in the SOD1G93A mouse model of amyotrophic lateral sclerosis","volume":"76","author":"Clark","year":"2016","journal-title":"J. Chem. Neuroanat."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"e70030","DOI":"10.1111\/ejn.70030","article-title":"Peripherin, a new promising biomarker in neurological disorders","volume":"61","author":"Manco","year":"2025","journal-title":"Eur. J. Neurosci."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1038\/s41582-021-00616-3","article-title":"Blood GFAP as an emerging biomarker in brain and spinal cord disorders","volume":"18","author":"Abdelhak","year":"2022","journal-title":"Nat. Rev. Neurol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/j.tins.2015.04.003","article-title":"Glial fibrillary acidic protein: From intermediate filament assembly and gliosis to neurobiomarker","volume":"38","author":"Yang","year":"2015","journal-title":"Trends Neurosci."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.jocn.2015.10.008","article-title":"Glial fibrillary acidic protein as a marker of astrocytic activation in the cerebrospinal fluid of patients with amyotrophic lateral sclerosis","volume":"26","author":"Benninger","year":"2016","journal-title":"J. Clin. Neurosci."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1002\/acn3.51708","article-title":"Serum levels of glial fibrillary acidic protein in patients with amyotrophic lateral sclerosis","volume":"10","author":"Verde","year":"2023","journal-title":"Ann. Clin. Transl. Neurol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1136\/jnnp-2018-318868","article-title":"Different neuroinflammatory profile in amyotrophic lateral sclerosis and frontotemporal dementia is linked to the clinical phase","volume":"90","author":"Oeckl","year":"2019","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1930","DOI":"10.1111\/ene.15321","article-title":"Integrated evaluation of a panel of neurochemical biomarkers to optimize diagnosis and prognosis in amyotrophic lateral sclerosis","volume":"29","author":"Falzone","year":"2022","journal-title":"Eur. J. Neurol."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Mastrangelo, A., Vacchiano, V., Zenesini, C., Ruggeri, E., Baiardi, S., Cherici, A., Avoni, P., Polischi, B., Santoro, F., and Capellari, S. (2023). Amyloid-beta co-pathology is a major determinant of the elevated plasma GFAP values in amyotrophic lateral sclerosis. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241813976"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1126\/science.6308771","article-title":"Lewy bodies of Parkinson\u2019s disease contain neurofilament antigens","volume":"221","author":"Goldman","year":"1983","journal-title":"Science"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1186\/s13024-024-00756-2","article-title":"\u03b1-synuclein pathology disrupts mitochondrial function in dopaminergic and cholinergic neurons at-risk in Parkinson\u2019s disease","volume":"19","author":"Geibl","year":"2024","journal-title":"Mol. Neurodegener."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1111\/j.1471-4159.1990.tb02325.x","article-title":"Mitochondrial complex I deficiency in Parkinson\u2019s disease","volume":"54","author":"Schapira","year":"1990","journal-title":"J. Neurochem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"461","DOI":"10.3233\/JPD-130230","article-title":"The role of oxidative stress in Parkinson\u2019s disease","volume":"3","author":"Dias","year":"2013","journal-title":"J. Parkinsons Dis."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0304-3940(03)00903-0","article-title":"Mutation analysis of the neurofilament M gene in Parkinson\u2019s disease","volume":"351","author":"Fischer","year":"2003","journal-title":"Neurosci. Lett."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.neuron.2016.05.018","article-title":"Neurofilament light chain in blood and CSF as marker of disease progression in mouse models and in neurodegenerative diseases","volume":"91","author":"Bacioglu","year":"2016","journal-title":"Neuron"},{"key":"ref_189","doi-asserted-by":"crossref","unstructured":"Di Lazzaro, G., Picca, A., Boldrini, S., Bove, F., Marzetti, E., Petracca, M., Piano, C., Bentivoglio, A.R., and Calabresi, P. (2024). Differential profiles of serum cytokines in Parkinson\u2019s disease according to disease duration. Neurobiol. Dis., 190.","DOI":"10.1016\/j.nbd.2023.106371"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"102566","DOI":"10.1016\/j.arr.2024.102566","article-title":"Molecular mechanisms of neurofilament alterations and its application in assessing neurodegenerative disorders","volume":"102","author":"Devarakonda","year":"2024","journal-title":"Ageing Res. Rev."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"e70111","DOI":"10.1111\/cts.70111","article-title":"Longitudinal correlation of cerebrospinal fluid GFAP and the progression of cognition decline in different clinical subtypes of Parkinson\u2019s disease","volume":"17","author":"Liu","year":"2024","journal-title":"Clin. Transl. Sci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"7537","DOI":"10.1007\/s00415-024-12669-7","article-title":"Plasma NfL, GFAP, amyloid, and p-tau species as prognostic biomarkers in Parkinson\u2019s disease","volume":"271","author":"Pilotto","year":"2024","journal-title":"J. Neurol."},{"key":"ref_193","doi-asserted-by":"crossref","unstructured":"Youssef, P., Hughes, L., Kim, W.S., Halliday, G.M., Lewis, S.J.G., Cooper, A., and Dzamko, N. (2023). Evaluation of Plasma Levels of NFL, GFAP, UCHL1 and tau as Parkinson\u2019s disease biomarkers using multiplexed single molecule counting. Sci. Rep., 13.","DOI":"10.1038\/s41598-023-32480-0"},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1111\/jnc.12742","article-title":"Enteric GFAP expression and phosphorylation in Parkinson\u2019s disease","volume":"130","author":"Clairembault","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1080\/15548627.2019.1603548","article-title":"LRRK2 mutations impair depolarization-induced mitophagy through inhibition of mitochondrial accumulation of RAB10","volume":"16","author":"Wauters","year":"2020","journal-title":"Autophagy"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1186\/s13041-016-0261-z","article-title":"Amyloid \u03b2 oligomers elicit mitochondrial transport defects and fragmentation in a time-dependent and pathway-specific manner","volume":"9","author":"Rui","year":"2016","journal-title":"Mol. Brain"},{"key":"ref_197","doi-asserted-by":"crossref","unstructured":"Di Lorenzo, R., Zecca, C., Chimienti, G., Latronico, T., Liuzzi, G.M., Pesce, V., Dell\u2019Abate, M.T., Borlizzi, F., Giugno, A., and Urso, D. (2025). Reliable new biomarkers of mitochondrial oxidative stress and neuroinflammation in cerebrospinal fluid and plasma from Alzheimer\u2019s disease patients: A pilot study. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26167792"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1001\/jamaneurol.2025.2972","article-title":"Evolving role of plasma phosphorylated tau 217 in Alzheimer disease-time for tau","volume":"82","author":"Binks","year":"2025","journal-title":"JAMA Neurol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s00401-024-02828-5","article-title":"Pathologic and clinical correlates of region-specific brain GFAP in Alzheimer\u2019s disease","volume":"148","author":"Phillips","year":"2024","journal-title":"Acta Neuropathol."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"3505","DOI":"10.1093\/brain\/awab223","article-title":"Plasma GFAP is an early marker of amyloid-\u03b2 but not tau pathology in Alzheimer\u2019s disease","volume":"144","author":"Pereira","year":"2021","journal-title":"Brain"},{"key":"ref_201","doi-asserted-by":"crossref","unstructured":"Kim, K.Y., Shin, K.Y., and Chang, K.A. (2023). GFAP as a potential biomarker for Alzheimer\u2019s disease: A systematic review and meta-analysis. Cells, 12.","DOI":"10.3390\/cells12091309"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"e70209","DOI":"10.1002\/alz.70209","article-title":"Plasma GFAP for populational enrichment of clinical trials in preclinical Alzheimer\u2019s disease","volume":"21","author":"Bellaver","year":"2025","journal-title":"Alzheimers Dement."},{"key":"ref_203","doi-asserted-by":"crossref","unstructured":"Wojda\u0142a, A.L., Bellomo, G., Gaetani, L., Toja, A., Chipi, E., Shan, D., Chiasserini, D., and Parnetti, L. (2023). Trajectories of CSF and plasma biomarkers across Alzheimer\u2019s disease continuum: Disease staging by NF-L, p-tau181, and GFAP. Neurobiol. Dis., 189.","DOI":"10.1016\/j.nbd.2023.106356"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.nbd.2005.12.007","article-title":"Mutant Huntingtin aggregates impair mitochondrial movement and trafficking in cortical neurons","volume":"22","author":"Chang","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1186\/s40478-024-01802-2","article-title":"Disruption of the mitochondrial network in a mouse model of Huntington\u2019s disease visualized by in-tissue multiscale 3D electron microscopy","volume":"12","author":"Torres","year":"2024","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"eaat7108","DOI":"10.1126\/scitranslmed.aat7108","article-title":"Evaluation of mutant Huntingtin and neurofilament proteins as potential markers in Huntington\u2019s disease","volume":"10","author":"Byrne","year":"2018","journal-title":"Sci. Transl. Med."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/s40478-020-0880-6","article-title":"Single-nucleus RNA-Seq identifies Huntington disease astrocyte states","volume":"8","author":"Sosunov","year":"2020","journal-title":"Acta Neuropathol. Commun."},{"key":"ref_208","doi-asserted-by":"crossref","unstructured":"Brown, T.G., Thayer, M.N., VanTreeck, J.G., Zarate, N., Hart, D.W., Heilbronner, S., and Gomez-Pastor, R. (2023). Striatal spatial heterogeneity, clustering, and white matter association of GFAP+ astrocytes in a mouse model of Huntington\u2019s disease. Front. Cell Neurosci., 17.","DOI":"10.3389\/fncel.2023.1094503"},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Zeng, Z., Wei, M., Zhang, S., Cui, H., Dagda, R.K., and Gasanoff, E.S. (2025). Bee venom proteins enhance proton absorption by membranes composed of phospholipids of the myelin sheath and endoplasmic reticulum: Pharmacological relevance. Pharmaceuticals, 18.","DOI":"10.3390\/ph18091334"},{"key":"ref_210","doi-asserted-by":"crossref","unstructured":"Gasanoff, E.S., and Dagda, R.K. (2024). Cobra venom cytotoxins as a tool for probing mechanisms of mitochondrial energetics and understanding mitochondrial membrane structure. Toxins, 16.","DOI":"10.3390\/toxins16070287"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/24\/11852\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,12,10]],"date-time":"2025-12-10T05:23:43Z","timestamp":1765344223000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/24\/11852"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,8]]},"references-count":210,"journal-issue":{"issue":"24","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["ijms262411852"],"URL":"https:\/\/doi.org\/10.3390\/ijms262411852","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,8]]}}}