Relevant bibliographies by topics / Proteinopathy

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Proteinopathy'

Author: Grafiati
Published: 1 February 2025

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Journal articles on the topic "Proteinopathy"

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Taylor, J. Paul. "Multisystem proteinopathy: Table." Neurology 85, no. 8 (July 24, 2015): 658–60. http://dx.doi.org/10.1212/wnl.0000000000001862.

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Valderhaug, Vibeke D., Kristine Heiney, Ola Huse Ramstad, Geir Bråthen, Wei-Li Kuan, Stefano Nichele, Axel Sandvig, and Ioanna Sandvig. "Early functional changes associated with alpha-synuclein proteinopathy in engineered human neural networks." American Journal of Physiology-Cell Physiology 320, no. 6 (June 1, 2021): C1141—C1152. http://dx.doi.org/10.1152/ajpcell.00413.2020.

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A patterned spread of proteinopathy represents a common characteristic of many neurodegenerative diseases. In Parkinson’s disease (PD), misfolded forms of α-synuclein proteins accumulate in hallmark pathological inclusions termed Lewy bodies and Lewy neurites. Such protein aggregates seem to affect selectively vulnerable neuronal populations in the substantia nigra and to propagate within interconnected neuronal networks. Research findings suggest that these proteinopathic inclusions are present at very early time points in disease development, even before clear behavioral symptoms of dysfunction arise. In this study, we investigate the early pathophysiology developing after induced formation of such PD-related α-synuclein inclusions in a physiologically relevant in vitro setup using engineered human neural networks. We monitor the neural network activity using multielectrode arrays (MEAs) for a period of 3 wk following proteinopathy induction to identify associated changes in network function, with a special emphasis on the measure of network criticality. Self-organized criticality represents the critical point between resilience against perturbation and adaptational flexibility, which appears to be a functional trait in self-organizing neural networks, both in vitro and in vivo. We show that although developing pathology at early onset is not clearly manifest in standard measurements of network function, it may be discerned by investigating differences in network criticality states.
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Paraskevas, George P., Mara Bourbouli, Ioannis Zaganas, and Elisabeth Kapaki. "The emerging TDP-43 proteinopathy." Neuroimmunology and Neuroinflammation 5, no. 5 (May 10, 2018): 17. http://dx.doi.org/10.20517/2347-8659.2018.18.

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Bhuiyan, Md Shenuarin, J. Scott Pattison, Hanna Osinska, Jeanne James, James Gulick, Patrick M. McLendon, Joseph A. Hill, Junichi Sadoshima, and Jeffrey Robbins. "Enhanced autophagy ameliorates cardiac proteinopathy." Journal of Clinical Investigation 123, no. 12 (November 1, 2013): 5284–97. http://dx.doi.org/10.1172/jci70877.

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Taylor, Laura M., Pamela J. McMillan, Brian C. Kraemer, and Nicole F. Liachko. "Tau tubulin kinases in proteinopathy." FEBS Journal 286, no. 13 (May 22, 2019): 2434–46. http://dx.doi.org/10.1111/febs.14866.

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Chen, Han-Jou, and Jacqueline C. Mitchell. "Mechanisms of TDP-43 Proteinopathy Onset and Propagation." International Journal of Molecular Sciences 22, no. 11 (June 2, 2021): 6004. http://dx.doi.org/10.3390/ijms22116004.

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TDP-43 is an RNA-binding protein that has been robustly linked to the pathogenesis of a number of neurodegenerative disorders, including amyotrophic lateral sclerosis and frontotemporal dementia. While mutations in the TARDBP gene that codes for the protein have been identified as causing disease in a small subset of patients, TDP-43 proteinopathy is present in the majority of cases regardless of mutation status. This raises key questions regarding the mechanisms by which TDP-43 proteinopathy arises and spreads throughout the central nervous system. Numerous studies have explored the role of a variety of cellular functions on the disease process, and nucleocytoplasmic transport, protein homeostasis, RNA interactions and cellular stress have all risen to the forefront as possible contributors to the initiation of TDP-43 pathogenesis. There is also a small but growing body of evidence suggesting that aggregation-prone TDP-43 can recruit physiological TDP-43, and be transmitted intercellularly, providing a mechanism whereby small-scale proteinopathy spreads from cell to cell, reflecting the spread of clinical symptoms observed in patients. This review will discuss the potential role of the aforementioned cellular functions in TDP-43 pathogenesis, and explore how aberrant pathology may spread, and result in a feed-forward cascade effect, leading to robust TDP-43 proteinopathy and disease.
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Deng, Jianwen, Peng Wang, Xiaoping Chen, Haipeng Cheng, Jianghong Liu, Kazuo Fushimi, Li Zhu, and Jane Y. Wu. "FUS interacts with ATP synthase beta subunit and induces mitochondrial unfolded protein response in cellular and animal models." Proceedings of the National Academy of Sciences 115, no. 41 (September 24, 2018): E9678—E9686. http://dx.doi.org/10.1073/pnas.1806655115.

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FUS (fused in sarcoma) proteinopathy is a group of neurodegenerative diseases characterized by the formation of inclusion bodies containing the FUS protein, including frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Previous studies show that mitochondrial damage is an important aspect of FUS proteinopathy. However, the molecular mechanisms by which FUS induces mitochondrial damage remain to be elucidated. Our biochemical and genetic experiments demonstrate that FUS interacts with the catalytic subunit of mitochondrial ATP synthase (ATP5B), disrupts the formation of ATP synthase complexes, and inhibits mitochondrial ATP synthesis. FUS expression activates the mitochondrial unfolded protein response (UPRmt). Importantly, down-regulating expression of ATP5B or UPRmt genes in FUS transgenic flies ameliorates neurodegenerative phenotypes. Our data show that mitochondrial impairment is a critical early event in FUS proteinopathy, and provide insights into the pathogenic mechanism of FUS-induced neurodegeneration.
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Stepenko, Yulia V., Veronika S. Shmigerova, Darya A. Kostina, Olesya V. Shcheblykina, Nina I. Zhernakova, Alexey V. Solin, Natalia V. Koroleva, Vera A. Markovskaya, Olga V. Dudnikova, and Anton A. Bolgov. "Study of the neuroprotective properties of the heteroreceptor EPOR/CD131 agonist of peptide structure in tau-proteinopathy modeling." Research Results in Pharmacology 10, no. 2 (June 17, 2024): 41–47. http://dx.doi.org/10.18413/rrpharmacology.10.492.

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Introduction: Tau proteinopathy is a pathology associated with the activation of post-translational modifications and interactions of pathophysiological cascades of neuroinflammation with hyperphosphorylation of Tau aggregates. Therefore, preference is given to agents that have properties in reducing or slowing down the processes of neuroinflammation and post-translational modifications in the brain. Materials and Methods: The study was conducted on male and female homozygous individuals of a transgenic murine line with overexpression of mutant human Tau gene (P301S) and a background wild mouse line C57Bl/6J. To assess the progression of Tau proteinopathy, behavioral tests were used at two control time points, and the last one measured the level of neuroinflammation markers and tau-proteinopathy. Results and Discussion: In the group of P301S mice treated with ARA-290, an improvement in the phenotypic picture of Tau proteinopathy was demonstrated compared with intact animals. In the Barnes circular maze test, mice showed a decrease in the total distance traveled and the latent time spent on the platform, which indicates a rapid entry into the shelter. In the O-shaped maze test, the group maintained a fairly high level of spontaneous exploratory behavior. In the vertical rod test, the animals recorded the best time indicators that they needed to turn and maintain balance compared to the intact group. A statistically significant decrease in the level of GSK-3β and an increase in CDK5 and PP2A were revealed, which indicates a dephosphorylating effect on Tau protein, as well as markers of neuroinflammation. NF-KB and TNF-α were significantly reduced by 57% and 32%, respectively, compared to the intact group. Conclusion: In the model of transgenic P301S murine line with overexpression of the mutant human Tau gene, the peptide agonist of the EPOR/CD 131 heteroreceptor demonstrated neuroprotective properties, which were confirmed by indicators of behavioral tests and markers of neuroinflammation and tau-proteinopathy.
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Zheng, Qingwen, Huabo Su, Mark J. Ranek, and Xuejun Wang. "Autophagy and p62 in Cardiac Proteinopathy." Circulation Research 109, no. 3 (July 22, 2011): 296–308. http://dx.doi.org/10.1161/circresaha.111.244707.

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Hasegawa, Masato, Tetsuaki Arai, Takashi Nonaka, Fuyuki Kametani, Mari Yoshida, Kenji Ikeda, and Haruhiko Akiyama. "Proteomic analyses of TDP-43 proteinopathy." Neuroscience Research 68 (January 2010): e35. http://dx.doi.org/10.1016/j.neures.2010.07.399.

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Dissertations / Theses on the topic "Proteinopathy"

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Armstrong, Bryson Walter. "The role of karyopherin-alpha in the pathogenesis of TDP-43 proteinopathy." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/45074.

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Aberrant cellular processing and targeting of TDP-43 has been implicated in a wide variety of neurological diseases such as frontotemporal lobar degeneration with ubiquitinated inclusions (FTLD-U) and amyotrophic lateral sclerosis (ALS). These diseases are characterized by the sequestration of TDP-43 into the cytoplasm of afflicted neurons, leading to the formation of ubiquitinated, cytoplasmic inclusions and an increased susceptibility to cellular insults. While the underlying causes of TDP-43 proteinopathy are unknown, we are investigating the role of a protein family known as the karyopherins in the nuclear targeting of TDP-43. Using co-immunoprecipitation in SH-SY5Y cells we determined that a major binding partner of TDP-43 is karyopherin-alpha 2 (KPNA2). Next, utilizing a high-density peptide array comprised of overlapping peptide sequences derived from TDP-43 we identified six regions where KPNA2 may directly interact with TDP-43. From these regions we developed six small, cell-penetrating peptides designed to specifically inhibit the interaction between KPNA2 and TDP-43. Through the use of these synthetic peptides, we were able to interfere with the binding of KPNA2 to TDP-43 in vitro. We found that the disruption of this specific protein-protein interaction was not sufficient to induce TDP-43 cytoplasmic sequestration, as determined by co-immunoprecipitation and subcellular fractionation assays. As our research focused primarily on healthy SH-SY5Y cells, future studies will focus on investigating the effects of peptide-mediated TDP-43 nuclear import impairment paired alongside oxidative insult. We will also investigate whether compensatory mechanisms within SH-SY5Y cells are responsible for the nuclear localization of TDP-43 in the absence of KPNA2-mediated nuclear import.
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Kornfield, James M. "TDP-43 proteinopathy: tracing the roots of a newly classified neurodegenerative disease." Thesis, Boston University, 2013. https://hdl.handle.net/2144/21197.

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Thesis (M.A.)PLEASE NOTE: Boston University Libraries did not receive an Authorization To Manage form for this thesis or dissertation. It is therefore not openly accessible, though it may be available by request. If you are the author or principal advisor of this work and would like to request open access for it, please contact us at open-help@bu.edu. Thank you.
TAR DNA Binding Protein-43 (TDP-43) proteinopathy is a disease pathology that underlies a broad field of neurodegenerative disorders. Most prominently, TDP-43 aggregates are the hallmark of Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Lobar Degeneration (FTLD). The implication of TDP-43 in ALS, in particular, has helped initiate a cascade of research to determine the properties of the previously obscure protein. From these studies, it is now known that TDP-43 is a DNA and RNA binding protein, important for the splicing and regulation of many transcripts. In the disease state, TDP-43 is modified in a way that fuels its accumulation into cytoplasmic aggregates called inclusions. This paper will delineate the current understanding of the mechanisms behind TDP-43 proteinopathy and the resultant clinical conditions. The body of evidence firmly supports a clinical spectrum of TDP-43 proteinopathy that ranges between pure motor neuron disease (MND) and pure frontotemporal dementia (FTD). It also appears that the root cause of neurodegeneration in these disorders comes about through a combination of a gain of toxic function and a loss of normal TDP-43. Continued research into the molecular processes leading to the capitulation of TDP-43 holds great promise for the development of new drug targets to help treat the spectrum of TDP-43 proteinopathy.
2031-01-01
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PISCIOTTANI, ALESSANDRA. "Axonal mRNA dysregulation in a cellular model of TDP-43 proteinopathy: a functional and -omic analysis." Doctoral thesis, Università Vita-Salute San Raffaele, 2022. http://hdl.handle.net/20.500.11768/128351.

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Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disease that mainly affects upper and lower motor neurons. Only 10% of cases are familial, while the majority are sporadic. TDP-43, encoded by the TARDBP gene, is an RNA-binding protein that plays essential regulatory roles in RNA metabolism, from transcription and splicing to transport and translation. While TARDBP mutations are only found in 2-5% of ALS cases, 97% of patients, both sporadic and familial, show nuclear TDP-43 depletion as well as its cytoplasmic accumulation and aggregate formation, known as TDP-43 proteinopathy. Several lines of evidence suggest that ALS is a distal axonopathy in which axonal degeneration precedes motor neuron death. Since axonal translation is essential for the development, maintenance and function of this subcellular compartment, we hypothesized that altered axonal mRNA levels resulting from TDP-43 deregulation may severely affect axonal biology in motor neurons, a cell type whose axon accounts for over 99% of the total cellular volume. In this project we characterized highly enriched cultures of mouse cortical motor neurons overexpressing wt TDP-43 (wtTDP) or carrying a familial ALS mutation, A315T (mutTDP). Both models exhibit cytoplasmic accumulation of TDP-43-positive aggregates, accompanied by reduced axonal mRNA translation, increased oxidative stress, impaired exocytosis and changes in Ca2+ homeostasis. Thanks to microfluidic chambers, wt- and mutTDP axons and cell bodies were physically separated, permitting the unbiased RNA-seq analysis of both subcellular territories. Through a miniaturized sucrose gradient protocol developed by Gabriella Viero’s lab, polysome-engaged and subpolysomal mRNAs were analyzed separately in comparison to control neurons. I focused on translatome and transcriptome changes related to the functional alterations observed by our group. Both wtTDP and mutTDP axons show a marked deregulation of polysomal transcripts involved in mRNA translation, the response to oxidative stress and presynaptic function, underlining the importance of axonal translation in key functional and homeostatic processes. Finally, electrophysiological recordings of wt- and mutTDP neurons revealed a significantly increase in electrical synapses. While potentially serving as a compensatory mechanism for the reduced connectivity of wt- and mutTDP neurons, gap junctions and hemichannels may contribute to the spread of toxic small molecules and to the maladaptive dissemination of neuronal damage from its focal origin.
La Sclerosi Laterale Amiotrofica (SLA) è una malattia neurodegenerativa incurabile che colpisce principalmente il primo e il secondo motoneurone. Solo il 10% dei casi sono familiari, mentre la maggior parte sono sporadici. TDP-43, codificata dal gene TARDBP, è una proteina legante l’RNA che ha un ruolo regolatorio essenziale nel metabolismo dell’RNA, dalla trascrizione e splicing al trasporto e traduzione. Mentre le mutazioni di TARDBP rappresentano solo il 2-5% dei casi di SLA, il 97% dei pazienti, sia sporadici che familiari, mostrano una deplezione nucleare di TDP-43 così come il suo accumulo citoplasmatico e la formazione di aggregati, noti come TDP-43 proteinopatia. Diverse evidenze suggeriscono che la SLA sia una assonopatia distale, in cui la degenerazione assonale precede la morte del motoneurone. Poichè la traduzione assonale è essenziale per lo sviluppo, il mantenimento e il funzionamento di questo compartimento subcellulare, noi ipotizziamo che livelli alterati di mRNA dovuti alla deregolazione di TDP-43 può alterare la biologia assonale nei motoneuroni, un tipo cellulare il cui l’assone rappresenta il 99% del volume totale della cellula. In questo progetto abbiamo caratterizzato colture altamente arricchite di motoneuroni corticali murini overesprimenti TDP-43 wt (wtTDP) o con una mutazione familiare, A315T (mutTDP). Entrambi i modelli presentano un accumulo citoplasmatico di aggregati positivi per TDP-43, accompagnato da una ridotta traduzione assonale degli mRNA, aumentato stress ossidativo, alterata esocitosi e cambiamenti nell’omeostati del calcio. Mediante l’uso di camerette microfluidiche, assoni e corpi cellulari wt- e mutTDP sono stati fisicamente separati, permettendo un’analisi imparziale di RNA-seq di entrambi i compartimenti subcellulari. Mediante un protocollo con gradiente di saccarosio sviluppato dal laboratorio di Gabriella Viero, gli mRNA polisomali e sub-polisomali sono stati analizzati separatamente e comparati ai neuroni di controllo. Mi sono focalizzata sui cambiamenti del translatoma e trascrittoma relativi alle alterazioni funzionali osservati dal nostro gruppo. Sia gli assoni wtTDP che mutTDP presentano una evidente deregolazione dei trascritti polisomali coinvolti nella traduzione degli mRNA, nella risposta allo stress ossidativo e nella funzione presinaptica, sottolineando l’importanza della traduzione assonale nei processi chiave funzionali e omeostatici. Infine, le registrazioni di elettrofisiologia dei neuroni wtTDP e mutTDP hanno mostrato un aumento significativo delle sinapsi elettriche. Oltre a rappresentare potenzialmente un meccanismo di compensazione della ridotta connettività dei neuroni wtTDP e TDP-43, le gap junctions e gli emicanali, potrebbero contribuire alla diffusione di piccole molecole tossiche e una diffusione maladattiva del danno neuronale a partire dalla sua origine focale.
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Ury-Thiery, Vicky. "Agrégation in vitro de la protéine amyloïde Tau et étude de son impact sur des modèles membranaires par différentes méthodes biophysiques." Electronic Thesis or Diss., Bordeaux, 2024. http://www.theses.fr/2024BORD0440.

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Les maladies neurodégénératives, telles que les maladies d'Alzheimer et de Parkinson, affectent les fonctions cognitives et motrices. Elles se caractérisent par une perte progressive de neurones, sans possibilité de régénération. Avec le vieillissement de la population, ces pathologies, principalement liées à l'âge, représentent un enjeu sociétal majeur. L'absence de diagnostic précoce, de traitements efficaces et la méconnaissance des mécanismes en jeu soulignent la nécessité d'en approfondir la compréhension. Les patients atteints de ces maladies présentent des accumulations de protéines anormales sous forme d’agrégats insolubles, dans ou à proximité des cellules cérébrales. Bien que chaque protéinopathie présente des agrégats spécifiques, elles partagent des caractéristiques communes, notamment leur structure appelée amyloïde. Ces amyloïdes, formés par l’auto-assemblage de monomères protéiques mal conformés par empilement, adoptent une structure caractéristique dite en cross-β. Plusieurs protéines amyloïdes pathogènes ont été identifiées et sont associées à diverses maladies neurodégénératives. La protéine Tau, impliquée dans la maladie d'Alzheimer et plus largement dans un groupe de démences appelées tauopathies, est principalement localisée dans les neurones, où elle stabilise les microtubules, éléments structurants du cytosquelette cellulaire. Toutefois, dans des conditions pathologiques, Tau se dissocie des microtubules, devient hyperphosphorylée et forme des agrégats amyloïdes fibrillaires. Les mécanismes exacts de cette agrégation restent mal compris. L'étude de l'agrégation de Tau repose sur la production in vitro de fibres amyloïdes. En raison de sa solubilité élevée liée à sa charge positive, la formation de ces fibres nécessite l’ajout de molécules polyanioniques, appelées cofacteurs, telles que l’héparine (un polysaccharide), des ARN ou des lipides. Cependant, des incertitudes demeurent quant au rôle précis de ces cofacteurs : catalysent-ils simplement l'agrégation ou sont-ils intégrés dans la structure des fibres ? Si tel est le cas, quel impact cela a-t-il sur la morphologie des agrégats ? La capacité de Tau à s'agréger en présence de lipides suscite des interrogations sur son comportement vis à vis des différentes membranes des neurones. L’interaction de Tau avec les membranes plasmiques a été démontrée, et pourrait jouer un rôle autant dans des processus physiologiques que pathologiques. Tau, en présence de lipides anioniques, altère-t-elle l’intégrité membranaire ? Qu'en est-il des lipides non anioniques ? Pour répondre à ces questions, ce projet de thèse combine plusieurs approches biophysiques : spectroscopie infrarouge à réflexion totale atténuée (ATR-FTIR), microscopie à force atomique (AFM), microscopie électronique à transmission (MET) et résonance plasmonique de surface par ondes guidées (PWR). L’étude est structurée autour de deux axes principaux : (i) caractériser l’agrégation de Tau en présence de différents cofacteurs anioniques (héparine, ARN, phospholipides) et étudier l'impact sur la morphologie des fibres ; (ii) évaluer l’effet de l’interaction de Tau avec des membranes lipidiques de différentes compositions sur leur intégrité. Les résultats de cette thèse apportent de nouvelles perspectives sur les mécanismes pathogéniques de Tau et pourraient contribuer à une meilleure compréhension des tauopathies, ainsi qu'au développement de stratégies thérapeutiques
Neurodegenerative diseases, such as Alzheimer’s and Parkinson’s, affect cognitive and motor functions. They are characterized by a progressive loss of neurons, with no possibility of regeneration. With an aging population, these predominantly age-related diseases represent a major societal challenge. The lack of early diagnosis, effective treatments, and understanding of the underlying mechanisms highlights the need for further investigation. Patients suffering from these diseases exhibit abnormal protein accumulations in the form of insoluble aggregates, within or near brain cells. Although each proteinopathy presents specific aggregates, they share common features, notably their amyloid structure. These amyloids, formed by the misfolded protein monomers’ self-assembly through stacking, adopt a characteristic cross-β structure. Several pathogenic amyloid proteins have been identified and are associated with various neurodegenerative diseases. The Tau protein, implicated in Alzheimer’s disease and more broadly in a group of dementias known as tauopathies, is primarily located in neurons, where it stabilizes microtubules, structural elements of the cellular cytoskeleton. However, under pathological conditions, Tau dissociates from the microtubules, becomes hyperphosphorylated, and forms fibrillar amyloid aggregates. The exact mechanisms of this aggregation remain poorly understood. The study of Tau aggregation relies on the in vitro production of amyloid fibers. Due to its high solubility associated with its positive charge, fiber formation requires the addition of polyanionic molecules, called cofactors, such as heparin (a polysaccharide), RNA, or lipids. However, uncertainties remain regarding the exact role of these cofactors: do they simply catalyze aggregation, or are they integrated into the fiber structure? If so, what impact does this have on the morphology of the aggregates? Tau's ability to aggregate in the presence of lipids raises questions about its behavior in relation to the different membranes of neurons. Tau’s interaction with plasma membranes has been demonstrated and may play a role in both physiological and pathological processes. Does Tau, in the presence of anionic lipids, compromise membrane integrity? What about non-anionic lipids? To address these questions, this thesis project combines several biophysical approaches: attenuated total reflection Fourier-transform infrared spectroscopy (ATR-FTIR), atomic force microscopy (AFM), transmission electron microscopy (TEM), and plasmon waveguide resonance (PWR). The study is structured around two main axes: (i) characterizing Tau aggregation in the presence of different anionic cofactors (heparin, RNA, phospholipids) and studying their impact on fiber morphology; (ii) assessing the effect of Tau's interaction with lipid membranes of varying compositions on membrane integrity. The results of this thesis provide new insights into the pathogenic mechanisms of Tau and may contribute to a better understanding of tauopathies as well as the development of therapeutic strategies
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Book chapters on the topic "Proteinopathy"

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Thal, Dietmar R., Melissa E. Murray, and Dennis W. Dickson. "Alzheimer's disease (Aβ and Tau proteinopathy)." In Greenfield's Neuropathology 10e Set, 1012–41. 10th ed. Boca Raton: CRC Press, 2024. http://dx.doi.org/10.1201/9781003389699-32.

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Josephs, Keith A. "Clinical Aspects of TDP‐43 Proteinopathy, Neurofilament Inclusion Body Disease and Dementias Lacking Distinctive Proteinopathy." In Dementias, 377–82. Elsevier, 2008. http://dx.doi.org/10.1016/s0072-9752(07)01235-3.

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Bharathi, Vidhya, Amandeep Girdhar, and Basant K. Patel. "TDP-43 proteinopathy mechanisms from non-mammalian model systems." In TDP-43 and Neurodegeneration, 153–81. Elsevier, 2022. http://dx.doi.org/10.1016/b978-0-12-820066-7.00002-3.

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Espay, Alberto J., Karl Herrup, and Timothy Daly. "Finding the falsification threshold of the toxic proteinopathy hypothesis in neurodegeneration." In Precision Medicine in Neurodegenerative Disorders, Part I, 143–54. Elsevier, 2023. http://dx.doi.org/10.1016/b978-0-323-85538-9.00008-0.

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Kritikos, Minos, Samuel E. Gandy, Jaymie R. Meliker, Benjamin J. Luft, and Sean A. P. Clouston. "Acute versus Chronic Exposures to Inhaled Particulate Matter and Neurocognitive Dysfunction: Pathways to Alzheimer’s Disease or a Related Dementia." In Advances in Alzheimer’s Disease. IOS Press, 2021. http://dx.doi.org/10.3233/aiad210028.

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An estimated 92% of the world’s population live in regions where people are regularly exposed to high levels of anthropogenic air pollution. Historically, research on the effects of air pollution have focused extensively on cardiovascular and pulmonary health. However, emerging evidence from animal and human studies has suggested that chronic exposures to air pollution detrimentally change the functioning of the central nervous system with the result being proteinopathy, neurocognitive impairment, and neurodegenerative disease. Case analyses of aging World Trade Center responders suggests that a single severe exposure may also induce a neuropathologic response. The goal of this report was to explore the neuroscientific support for the hypothesis that inhaled particulate matter might cause an Alzheimer’s-like neurodegenerative disease, in order to consider proposed mechanisms and latency periods linking inhaled particulate matter and neurodegeneration, and to propose new directions in this line of research.
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Gupta, Nimisha, and Dr Farheen Waziri. "PROTEINOPATHIES: A REVIEW ON CURRENT SCENARIO AND THERAPEUTIC INTERVENTIONS." In Futuristic Trends in Biotechnology Volume 3 Book 14, 144–60. Iterative International Publisher, Selfypage Developers Pvt Ltd, 2024. http://dx.doi.org/10.58532/v3bbbt14p2ch3.

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There are certain neurodegenerative as well as non-neurodegenerative disorders whose characteristic feature is the presence of protein aggregates. The aggregates can be of different types, shapes, and sizes. These aggregates are harmful because they sequester the proteins and RNAs essential for cellular function. Protein aggregates found in these proteinopathies are thus an area of major interest in the scientific community. In recent years, scientists have tried to develop diagnostic and therapeutic measures targeting the protein aggregates. This review article aims to provide an overview of the advances that have been made in the last five years in terms of understanding of the protein aggregates found in the disease, its diagnosis, and its treatment. To achieve this, PubMed and Google Scholar were searched for reviews and research papers published from 2015-2020 using the following keywords: ‘protein aggregation’, ‘proteinopathy’, ‘protein aggregation disorders’ etc.
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Diederich, Nico J., and Christopher G. Goetz. "Parkinson’s Disease." In The Evolutionary Roots of Human Brain Diseases, edited by Nico J. Diederich, Martin Brüne, Katrin Amunts, and Christopher G. Goetz, 205–27. Oxford University PressNew York, 2024. http://dx.doi.org/10.1093/med/9780197676592.003.0010.

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Abstract Parkinson’s disease (PD) is a neurodegenerative disease characterized by bradykinesia, tremor, and rigidity, all due to basal gangliar dopaminergic deficits. Behavioral and autonomic non-motor symptoms accompany the core motor syndrome. The precise pathophysiology of PD is incompletely understood, and the hypothesis of an ascending proteinopathy cannot explain the temporal parallelism of motor and non-motor syndromes. The authors reconsider PD from an evolutionary perspective, noting that PD occurs only in humans. At the anatomical level, the vulnerable dysfunctioning nuclei of PD are evolutionarily old and overburdened by human telencephalization. While taking over new tasks and enduring continuous, energy requiring, challenges due to human longevity, the structural composition of these archaic areas has remained largely unchanged over millions of years. At the functional level, reflex, immediate reactions to environmental stimuli are primarily affected. An evolutionary focus on PD encourages exploration of involved circuitries and transmitters beyond the best-explored dopaminergic deficits.
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Conference papers on the topic "Proteinopathy"

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Sarah, Fullam, Power Alan, Stack Jessica, Bermingham Niamh, McNamara Brian, and Merwick Aine. "VCP multisystem proteinopathy: a ubiquitous culprit of neuronal degeneration." In Association of British Neurologists: Annual Meeting Abstracts 2023. BMJ Publishing Group Ltd, 2023. http://dx.doi.org/10.1136/jnnp-2023-abn.229.

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Gwin, M. S., S. B. Voth, S. Subedi Paudel, N. Onanyan, A. Darby, C. M. Francis, and T. Stevens. "Essential Role for Gamma Secretase Activating Protein (GSAP) in Infection-Elicited Endothelial Proteinopathy." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a5275.

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Roos, Raymond P., Katsuhisa Masaki, Yoshifumi Sonobe, and Ghanashyam Ghadge. "TDP-43 PROTEINOPATHY IN THE PATHOGENESIS OF THEILER'S MURINE ENCEPHALOMYELITIS VIRUS INDUCED DISEASES." In Viruses: Discovering Big in Small. TORUS PRESS, 2019. http://dx.doi.org/10.30826/viruses-2019-10.

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4

Abakumets, V. Y., and K. Ya Bulanava. "THE INFLUENCE OF INSULIN FIBRILLATION." In SAKHAROV READINGS 2021: ENVIRONMENTAL PROBLEMS OF THE XXI CENTURY. International Sakharov Environmental Institute of Belarusian State University, 2021. http://dx.doi.org/10.46646/sakh-2021-2-7-10.

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Violation of protein folding leads to the development of a number of systemic and neurodegenerative diseases-proteinopathy. In these pathologies, proteins acquire an incorrect conformation that differs from the native one, become functionally inactive, toxic, and prone to aggregation and deposition in various organs and tissues. There is a widespread hypothesis that the primary cytotoxic agents in the development of proteinopathies are protein oligomers that are prone to aggregation. These diseases include Parkinson’s disease, Creutzfeldt-Jakob disease, type 2 diabetes, and many others.
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Lysikova, Ekaterina. "MOLECULAR MECHANISMS OF SUPPRESSION OF THE PROGRESSION OF FUS PROTEINOPATHY IN THE NERVOUS SYSTEM OF TRANSGENIC MICE." In XVII INTERNATIONAL INTERDISCIPLINARY CONGRESS NEUROSCIENCE FOR MEDICINE AND PSYCHOLOGY. LCC MAKS Press, 2021. http://dx.doi.org/10.29003/m2209.sudak.ns2021-17/237-238.

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Gattas, Susannah, Mark Davis, Merrilee Needham, Emily Watson, Robert Henderson, and Pamela McCombe. "3207 Case series of multisystem proteinopathy due to valosin-containing protein (VCP) gene variants: an inconsistent phenotype." In ANZAN Annual Scientific Meeting 2024 Abstracts, A55.2—A55. BMJ Publishing Group Ltd, 2024. http://dx.doi.org/10.1136/bmjno-2024-anzan.156.

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Halber, Matthew, Sabrina Bulancea, and Simona Treidler. "Clinical and Electrophysiological Presentation of a Patient with Multisystem Proteinopathy Associated with Valosin-Containing Protein Mutation (P5-8.005)." In 2023 Annual Meeting Abstracts. Lippincott Williams & Wilkins, 2023. http://dx.doi.org/10.1212/wnl.0000000000202694.

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8

Stork, Larissa Rosa, Lucca Stephani Ribeiro, Izabella Savergnini Deprá, Luísa D’Ávila Camargo, and Maria Angélica Santos Novaes. "Tau protein and its role in Alzheimer’s disease physiopathology: a literature review." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.132.

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Background: Alzheimer’s disease (AD) is a neurodegenerative disorder characterized by a double proteinopathy: deposition of amyloid-β into plaques and hyperphosphorylation of Tau protein. Objectives: To understand the genetic and molecular aspects of Tau protein and its relationship with Alzheimer’s disease. Methods: We conducted a systematic literature search using Pubmed/ MEDLINE and ClinicalKey databases, applying the descriptors: “Alzheimer Disease” AND “Tau proteins’’ AND Tauopathies, during July and August of 2020. The inclusion criteria were English and Portuguese articles published between 2015 and 2020, with human limited study and free full text, excluding images, books, clinical tests, and narrative reviews. After analyzing titles and abstracts, we selected 12 articles and included 7 additional studies. Results: Mapt, the encoder gene of Tau, is located in the 17q21.3 locus and presents 16 exons that, when transcripted, originates 12 copies of mRNA by alternative splicing and 6 Tau’s isoforms. Tau is a microtubule-associated protein (MAP) responsible for cellular cytoskeleton stabilization and maintenance, promoting neuronal axonal transport. A kinase-phosphatase imbalance turns Tau hyperphosphorylated, disassociating it from tubulin and grouping it into insoluble paired helical filaments, which originates neurofibrillary tangles. The tauopathy’s progress causes neurotransmitter destabilization and neuronal death, inducing AD symptomatic manifestations. Conclusions: Due to the gradual worsening of the disease to more debilitating stages, studies focused on deepening the knowledge of genetic and molecular aspects of Tau protein are viable and promising alternatives to improve the quality of patient’s lives.
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Barbosa, Mateus Gonçalves de Sena, Ghaspar Gomes de Oliveira Alves Francisco, Rafaela Luiza Vilela de Souza, João Marcos Alcântara de Souza, and Nicollas Nunes Rabelo. "Chronic traumatic encephalopathy in military and sportsists: a factual problem?: a systematic review." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.324.

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Background: Chronic traumatic encephalopathy (CTE) is a progressive neurodegenerative disease linked to tau protein associated with recurrent brain trauma, clinically marked by mood, personality, cognitive and behavioral changes. Objectives: The objective of the study was to demonstrate whether athletes and military personnel can really be victims of CTE and to elucidate this same pathology. Design and setting: This is a systematic review, based on the PRISMA guidelines and a literature review with a summary of the evidence found. Methods: Articles were selected, published from 1934 to 2020, in PubMed and Scielo using the descriptors: “chronic traumatic encephalopathy”, “cerebral concussion”, “players”, “boxers”, “athletes” and “military”. Inclusion criteria were: studies available in English, Spanish and Portuguese published, with randomized clinical trial, cohort study or meta-analysis. Results: In 52 articles, 14 were selected for qualitative synthesis in the results table that addresses chronic traumatic encephalopathy in football, soccer and rugby players, boxers and the military. Neuropathologically, CTE is characterized by cerebral atrophy, a pelvic septum cavity with fenestrations, dense diffuse immunoreactive inclusions and a TDP-43 proteinopathy. Microscopically, there are extensive neurofibrillary tangles and spindle-shaped and filiform neurites throughout the brain. Conclusions: American football players, boxers and military men are more likely to trigger CTE, due to the constant mechanical shocks from their heads. The most frequent clinical manifestations were: headache, aggression, dementia, executive dysfunction and suicide. CTE is definitely diagnosed only at autopsy.
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Pedroza, Lucas Aleixo Leal, Francisco Agenor de Oliveira Neto, Antonio Marinho da Silva Neto,, Carlos Henrique Madeiros Castelletti, and Priscila Gubert. "ANÁLISE IN SILICO DO POTENCIAL DE AGREGAÇÃO DE RESÍDUOS DA TDP 43 HUMANA." In XXVII Semana de Biomedicina Inovação e Ciência. Editora IME, 2021. http://dx.doi.org/10.51161/9786588884119/17.

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Introdução: A TDP-43 (Target DNA protein) é uma proteína de 414 aminoácidos contendo 2 domínios de ligação ao RNA (RRM1 e RRM2), que vão do aminoácido 101 ao 265, uma região N-terminal (resíduo 1 ao 100) e uma região rica em Glicina (266 - 414), que em condições fisiológicas possui papel fundamental no metabolismo de RNAs e formação e manutenção dos grânulos de estresse. Entretanto, em condições patológicas, ainda pouco compreendidas, esta proteína pode formar agregados citotóxicos em células neuronais, causando danos mitocondriais, no proteossoma, e levando à neurodegeneração. Estes fatores tornam este quadro de proteinopatia a marca histopatológica de doenças como esclerose lateral amiotrífica (ELA) e demência fronto-temporal (DFT) [1]. Objetivos: Analisar o potencial de agregação dos resíduos da TDP-43 a partir de ferramentas computacionais. Metodologia: A estrutura tridimensional da TDP-43 foi obtida no banco de dados do AlphaFold protein structure database [2] com código AF-Q13148-F1-model_v1. A análise do potencial de agregação foi avaliado pelo Aggrescan3D 2.0, que permite analisar o potencial de agregação de aminoácidos a partir de uma estrutura conformacional proteíca [3] Resultados: O domínio rico em glicina (266 – 414) apresentou mais resíduos com alto potencial de formar agregados (50 aminoácidos) com índice acima de 0.000 (valores positivos), enquanto os demais domínios somados apresentaram apenas 12 aminoácidos com este potencial, sendo 7 destes referentes ao NTD (score máximo de 1.1713 em V94) e 5 nos RRMs (score máximo de 1.0120 em I249) de acordo com o score de pontuação do Aggrescan3D. Dentre aqueles que mais pontuaram tem-se a fenilalanina 316 (2.1992) e a isoleucina 383 (2.0641). De acordo com dados da literatura, a região rica em glicina está diretamente relacionada com a interação da TDP-43 com demais estruturas citoplasmáticas, inclusive com a formação de agregados, especialmente nas regiões de grânulos de estresse, fator esse que provavelmente ocorre em função da alta flexibilidade que a glicina confere ao domínio. Apesar da ausência de dados, é esperado que os RRM demonstrem scores menores, visto o seu papel no metabolismo de RNAs. Conclusão: Nota-se então que a região rica em glicina da TDP-43 apresenta mais resíduos com potencial de formar agregados citotóxicos, quando comparados aos demais domínios, tornando esta região, um possível alvo farmacológico para a inibição do avanço da proteinopatia. Ademais, novos estudos estão sendo realizados pelo grupo, a fim de compreender melhor as implicações da flexibilidade do domínio rico em glicina no potencial de agregação dos resíduos adjacentes.
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