Brahney, J., Hallerud, M., Heim, E., Hahnenberger, M. & Sukumaran, S. Plastic rain in protected areas of america. Science 368, 1257–1260 (2020).
Morales, A. C. et al. Atmospheric emission of nanoplastics from sewer pipe repairs. Nat. Nanotechnol. 17, 1171–1177 (2022).
Pauly, J. L. et al. Inhaled cellulosic and plastic fibers present in human lung tissue. Most cancers Epidemiol. Biomarkers Prev. 7, 419–428 (1998).
Prust, M., Meijer, J. & Westerink, R. H. S. The plastic mind: neurotoxicity of micro- and nanoplastics. Half. Fibre Toxicol. 17, 24 (2020).
Liu, X. et al. Bioeffects of inhaled nanoplastics on neurons and alteration of animal behaviors by deposition within the mind. Nano Lett. 22, 1091–1099 (2022).
Chen, H. et al. Residing close to main roads and the incidence of dementia, Parkinson’s illness, and a number of sclerosis: a population-based cohort research. Lancet 389, 718–726 (2017).
Yu, Z. et al. Lengthy-term publicity to ultrafine particles and particulate matter constituents and the chance of amyotrophic lateral sclerosis. Environ. Well being Perspect. 129, 97702 (2021).
Taylor, J. P., Brown, R. H. & Cleveland, D. W. Decoding ALS: from genes to mechanism. Nature 539, 197–206 (2016).
Kiernan, M. C. et al. Amyotrophic lateral sclerosis. Lancet 377, 942–955 (2011).
Ling, S. C., Polymenidou, M. & Cleveland, D. W. Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 79, 416–438 (2013).
Sreedharan, J. et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319, 1668–1672 (2008).
Neumann, M. et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130–133 (2006).
Baughn, M. W. et al. Mechanism of STMN2 cryptic splice-polyadenylation and its correction for TDP-43 proteinopathies. Science 379, 1140–1149 (2023).
Jo, M. et al. The position of TDP-43 propagation in neurodegenerative ailments: integrating insights from medical and experimental research. Exp. Mol. Med. 52, 1652–1662 (2020).
Banani, S. F., Lee, H. O., Hyman, A. A. & Rosen, M. Okay. Biomolecular condensates: organizers of mobile biochemistry. Nat. Rev. Mol. Cell Biol. 18, 285–298 (2017).
McGurk, L. et al. Poly(ADP-ribose) prevents pathological part separation of TDP-43 by selling liquid demixing and stress granule localization. Mol. Cell 71, 703–717.e709 (2018).
Lu, S. et al. Warmth-shock chaperone HSPB1 regulates cytoplasmic TDP-43 part separation and liquid-to-gel transition. Nat. Cell Biol. 24, 1378–1393 (2022).
Wang, C. et al. Stress induces dynamic, cytotoxicity-antagonizing TDP-43 nuclear our bodies by way of paraspeckle LncRNA NEAT1-mediated liquid-liquid part separation. Mol Cell 79, 443–458.e447 (2020).
Liu, X. et al. Serum. apolipoprotein A-I depletion is causative to silica nanoparticles-induced cardiovascular harm. Proc. Natl Acad. Sci. USA 118, e2108131118 (2021).
Kik, Okay., Bukowska, B. & Sicinska, P. Polystyrene nanoparticles: sources, prevalence within the setting, distribution in tissues, accumulation and toxicity to numerous organisms. Environ. Pollut. 262, 114297 (2020).
Zhao, Y. G. & Zhang, H. Part separation in membrane biology: the interaction between membrane-bound organelles and membraneless condensates. Dev. Cell 55, 30–44 (2020).
Zuo, X. et al. TDP-43 aggregation induced by oxidative stress causes international mitochondrial imbalance in ALS. Nat. Struct. Mol. Biol. 28, 132–142 (2021).
Wolozin, B. & Ivanov, P. Stress granules and neurodegeneration. Nat. Rev. Neurosci. 20, 649–666 (2019).
Gu, J. et al. Hsp70 chaperones TDP-43 in dynamic, liquid-like part and prevents it from amyloid aggregation. Cell Res. 31, 1024–1027 (2021).
Chen-Plotkin, A. S., Lee, V. M. & Trojanowski, J. Q. TAR DNA-binding protein 43 in neurodegenerative illness. Nat. Rev. Neurol. 6, 211–220 (2010).
Gasset-Rosa, F. et al. Cytoplasmic TDP-43 de-mixing unbiased of stress granules drives inhibition of nuclear import, lack of nuclear TDP-43, and cell demise. Neuron 102, 339–357.e337 (2019).
Neumann, M. et al. Phosphorylation of S409/410 of TDP-43 is a constant characteristic in all sporadic and familial types of TDP-43 proteinopathies. Acta Neuropathol. 117, 137–149 (2009).
Laferrière, F. et al. TDP-43 extracted from frontotemporal lobar degeneration topic brains shows distinct mixture assemblies and neurotoxic results reflecting illness development charges. Nat. Neurosci. 22, 65–77 (2019).
Frottin, F. et al. The nucleolus capabilities as a phase-separated protein high quality management compartment. Science 365, 342–347 (2019).
Eisele, Y. S. et al. Concentrating on protein aggregation for the therapy of degenerative ailments. Nat. Rev. Drug Discov. 14, 759–780 (2015).
Conicella, A. E. et al. TDP-43 α-helical construction tunes liquid–liquid part separation and performance. Proc. Natl Acad. Sci. USA 117, 5883–5894 (2020).
Yu, H. et al. HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells. Science 371, eabb4309 (2021).
Callahan, M. Okay., Chaillot, D., Jacquin, C., Clark, P. R. & Ménoret, A. Differential acquisition of antigenic peptides by Hsp70 and Hsc70 below oxidative situations. J. Biol. Chem. 277, 33604–33609 (2002).
Suk, T. R. & Rousseaux, M. W. C. The position of TDP-43 mislocalization in amyotrophic lateral sclerosis. Mol. Neurodegener. 15, 45 (2020).
Gottschald, O. R. et al. TIAR and TIA-1 mRNA-binding proteins co-aggregate below situations of fast oxygen decline and excessive hypoxia and suppress the HIF-1α pathway. J. Mol. Cell. Biol. 2, 345–356 (2010).
Boeynaems, S. & Gitler, A. D. Pour some sugar on TDP(-43). Mol. Cell 71, 649–651 (2018).
Streit, L. et al. Stress induced TDP-43 mobility loss unbiased of stress granules. Nat. Commun. 13, 5480 (2022).
Duan, Y. et al. PARylation regulates stress granule dynamics, part separation, and neurotoxicity of disease-related RNA-binding proteins. Cell Res. 29, 233–247 (2019).
Chhangani, D., Martin-Pena, A. & Rincon-Limas, D. E. Molecular, purposeful, and pathological facets of TDP-43 fragmentation. iScience 24, 102459 (2021).
Linse, S. et al. Nucleation of protein fibrillation by nanoparticles. Proc. Natl Acad. Sci. USA 104, 8691–8696 (2007).
Sassani, M. et al. Magnetic resonance spectroscopy reveals mitochondrial dysfunction in amyotrophic lateral sclerosis. Mind 143, 3603–3618 (2020).
Colasuonno, F., Worth, R. & Moreno, S. Higher and decrease motor neurons and the skeletal muscle: implication for amyotrophic lateral sclerosis (ALS). Adv. Anat. Embryol. Cell Biol. 236, 111–129 (2023).
Mead, R. J., Shan, N., Reiser, H. J., Marshall, F. & Shaw, P. J. Amyotrophic lateral sclerosis: a neurodegenerative dysfunction poised for profitable therapeutic translation. Nat. Rev. Drug Discov. 22, 185–212 (2023).
Kurashige, T. et al. TDP-43 accumulation inside intramuscular nerve bundles of sufferers with amyotrophic lateral sclerosis. JAMA Neurol. 79, 693–701 (2022).
Grunwald, M. S. et al. The oxidation of HSP70 is related to purposeful impairment and lack of stimulatory capability. Cell Stress Chaperones 19, 913–925 (2014).
Solar, H. et al. Oral publicity of polystyrene microplastics and doxycycline impacts mice neurological perform by way of intestine microbiota disruption: the orchestrating position of fecal microbiota transplantation. J. Hazard. Mater. 467, 133714 (2024).
Subramanian, A. et al. Gene set enrichment evaluation: a knowledge-based method for decoding genome-wide expression profiles. Proc. Natl Acad. Sci. USA 102, 15545–15550 (2005).
Feldman, A. T. & Wolfe, D. Tissue processing and hematoxylin and eosin staining. Strategies Mol. Biol. 1180, 31–43 (2014).