Relevant bibliographies by topics / Misfolding disease

Academic literature on the topic 'Misfolding disease'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Misfolding disease"

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Bellotti, Vittorio, and Monica Stoppini. "Protein Misfolding Diseases." Open Biology Journal 2, no. 1 (December 31, 2009): 228–34. http://dx.doi.org/10.2174/1874196700902010228.

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Diseases caused by protein misfolding are an emerging pathologic category that are thought to share some basic common mechanisms and display impressive heterogeneity in terms of tissue involvement, age of onset and clinical features. The growing recognition of the impact that protein misfolding has on human diseases is certainly related to the phenomenon of population aging and the expansion of the population in which these diseases are more frequent, but it is also based on a scientific revolution that looks at protein dynamics and relates these data to their potential pathologic implications. The multidisciplinary exchange of knowledge between experts in apparently unrelated diseases, such as sickle cell anemia and Alzheimer’s disease, has helped clarify the pathogenesis of these and many other diseases. The quick expansion of knowledge on the mechanisms of these diseases is priming pharmaceutical research that is now providing the first prototype drugs.
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GUPTA, ARTI, and ANJALI PANDEY. "Protein misfolding and neurodegenerative disease." ASIAN SCIENCE 11, no. 1 (June 15, 2016): 69–73. http://dx.doi.org/10.15740/has/as/11.1/69-73.

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Dobson, Chris. "PROTEIN FOLDING, MISFOLDING AND DISEASE." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A50. http://dx.doi.org/10.1042/bst028a050a.

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Hofmann, Christoph, Hugo A. Katus, and Shirin Doroudgar. "Protein Misfolding in Cardiac Disease." Circulation 139, no. 18 (April 30, 2019): 2085–88. http://dx.doi.org/10.1161/circulationaha.118.037417.

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Whiteman, Pat, Sarah Hutchinson, and Penny A. Handford. "Fibrillin-1 Misfolding and Disease." Antioxidants & Redox Signaling 8, no. 3-4 (March 2006): 338–46. http://dx.doi.org/10.1089/ars.2006.8.338.

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Dobson, Christopher M. "Protein misfolding, evolution and disease." Trends in Biochemical Sciences 24, no. 9 (September 1999): 329–32. http://dx.doi.org/10.1016/s0968-0004(99)01445-0.

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Moore, Roger A., Lara M. Taubner, and Suzette A. Priola. "Prion protein misfolding and disease." Current Opinion in Structural Biology 19, no. 1 (February 2009): 14–22. http://dx.doi.org/10.1016/j.sbi.2008.12.007.

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Ursini, Fulvio, Kelvin J. A. Davies, Matilde Maiorino, Tiziana Parasassi, and Alex Sevanian. "Atherosclerosis: another protein misfolding disease?" Trends in Molecular Medicine 8, no. 8 (August 2002): 370–74. http://dx.doi.org/10.1016/s1471-4914(02)02382-1.

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Hammarström, Per. "Protein folding, misfolding and disease." FEBS Letters 583, no. 16 (July 16, 2009): 2579–80. http://dx.doi.org/10.1016/j.febslet.2009.07.016.

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Gregersen, Niels, Peter Bross, Søren Vang, and Jane H. Christensen. "Protein Misfolding and Human Disease." Annual Review of Genomics and Human Genetics 7, no. 1 (September 2006): 103–24. http://dx.doi.org/10.1146/annurev.genom.7.080505.115737.

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Dissertations / Theses on the topic "Misfolding disease"

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Guest, William Clay. "Template-directed protein misfolding in neurodegenerative disease." Thesis, University of British Columbia, 2012. http://hdl.handle.net/2429/41990.

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Protein misfolding diseases represent a large burden to human health for which only symptomatic treatment is generally available. These diseases, such as Creutzfeldt-Jakob disease, amyotrophic lateral sclerosis, and the systemic amyloidoses, are characterized by conversion of globular, nativelyfolded proteins into pathologic β-sheet rich protein aggregates deposited in affected tissues. Understanding the thermodynamic and kinetic details of protein misfolding on a molecular level depends on accurately appraising the free energies of the folded, partially unfolded intermediate, and misfolded protein conformers. There are multiple energetic and entropic contributions to the total free energy, including nonpolar, electrostatic, solvation, and configurational terms. To accurately assess the electrostatic contribution, a method to calculate the spatially-varying dielectric constant in a protein/water system was developed using a generalization of Kirkwood Frohlich theory along with brief all-atom molecular dynamics simulations. This method was combined with previously validated models for nonpolar solvation and configurational entropy in an algorithm to calculate the free energy change on partial unfolding of contiguous protein subsequences. Results were compared with those from a minimal, topologically-based Gō model and direct calculation of free energies by steered all-atom molecular dynamics simulations. This algorithm was applied to understand the early steps in the misfolding mechanism for β₂-microglobulin, prion protein, and superoxide dismutase 1 (SOD1). It was hypothesized that SOD1 misfolding may follow a template-directed mechanism like that discovered previously for prion protein, so misfolding of SOD1 was induced in cell culture by transfection with mutant SOD1 constructs and observed to stably propagate intracellularly and intercellularly much like an infectious prion. A defined minimal assay with recombinant SOD protein demonstrated the sufficiency of mutant SOD1 alone to trigger wtSOD1 misfolding, reminiscent of the “protein-only” hypothesis of prion spread. Finally, protein misfolding as a feature of disease may extend beyond neurodegeneration and amyloid formation to cancer, in which derangement of protein folding quality control may lead to antibodyrecognizable misfolded protein present selectively on cancer cell surfaces. The evidence for this hypothesis and possible therapeutic targets are discussed as a future direction.
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Lane, Fiona Mary. "Defining mechanisms of neurodegeneration associated with protein misfolding diseases." Thesis, University of Edinburgh, 2015. http://hdl.handle.net/1842/19542.

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Protein misfolding diseases (PMDs) are a broad group of disorders including Alzheimer’s, Parkinson’s and prion diseases. They are characterised by the presence of aggregated, misfolded host proteins which are thought to cause cell death. Prion diseases are associated with misfolded prion protein (PrPSc), which has a tendency to form fibrillar aggregates. By contrast, Alzheimer’s disease (AD) is associated with misfolded amyloid beta (Aβ), which aggregates to form characteristic Aβ plaques. A feature which is common across PMDs is that small assemblies (oligomers) of the misfolded proteins are thought to be the important neurotoxic species, and it has been proposed that there may be a shared mechanism leading to cell death across PMDs caused by oligomers. In this study, the toxicity of different misfolded forms of recombinant PrP (recPrP) and recombinant Aβ (recAβ) and the mechanisms leading to cell death were investigated using a primary cell culture model. In addition, the importance of the disulphide bond in recPrP in relation to oligomer formation was explored using size exclusion chromatography and mass spectrometry, the toxicity of the different resulting oligomer populations were also investigated. Both recPrP oligomers and fibrils were shown to cause toxicity to mouse primary cortical neurons. Interestingly, oligomers were shown to cause apoptotic cell death, while the fibrils did not, suggesting the activation of different pathways. By contrast, recAβ fibrils were shown to be non-toxic to cortical neurons, Aβ oligomers, however, were shown to cause toxicity. Similar to recPrP, my data showed that it is likely that recAβ 1-42 oligomers also cause apoptosis. However, by contrast this seemed to be caused by excitotoxicity, which was not found to be the case for recPrP. Additionally, I have shown that the presence or absence of the disulphide bond in PrP has a profound effect on the size of oligomers which form. RecPrP lacking a disulphide bond leads to the formation of larger oligomers which are highly toxic to primary neurons. Findings from this study suggest that structural properties such as the disulphide bond in PrP can affect the size and toxicity of oligomers, furthermore, whilst oligomers have been shown to be important in both AD and prion diseases, they may not trigger the same pathways leading to cell death.
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Roboti, Peristera. "Disease-related misfolding of the myelin proteolipid protein." Thesis, University of Manchester, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.493943.

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A wide range of mutations in the myelin integral plasma membrane proteolipid protein (PLP) are associated with dysmyelinating diseases of varying severity, and whilst missense mutations in PLP transmembrane domains cause severe disease few such mutants result in a mild phenotype. The molecular pathology of such diseases has generally been attributed to endoplasmic reticulum (ER) retention of misfolded ing in the induction of ER stress. However, the cellular mechanism(s) that control the observed phenotypic variations have not yet been elucidated. The work documented in this thesis established that the cellular fate of three distinct transmembrane missense mutants of PLP is differentially regulated by the ER quality control process upon stable inducible expression in HeLa cells.
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Cristofani, R. M. "PROTEIN MISFOLDING IN KENNEDY¿S DISEASE AND IN RELATED MOTOR NEURON DISEASES (MNDS)." Doctoral thesis, Università degli Studi di Milano, 2015. http://hdl.handle.net/2434/339901.

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Motor neuron diseases, like spinobulbar muscular atrophy (SBMA) and amyotrophic lateral sclerosis (ALS) are characterized by the presence of inclusions or aggregates of proteinaceous materials. In SBMA, inclusions are formed by testosterone dependent aggregates of mutant androgen receptor (AR) with an elongated polyglutamine tract (ARpolyQ), while in ALS inclusions contain several aggregated proteins including TDP43, ubiquilin, optineurin. Exceptions are familial ALS forms linked to superoxide dismutase 1 (SOD1) mutations, to mutated TDP43 and to C9ORF72 poly-dipeptides (DPRs), in which aggregates are mainly composed of mutant SOD1, mutant TDP43 or DPRs, respectively. In general, protein aggregation is due to generation of aberrant protein conformations (misfolding) combined to a failure, in neuronal cells, of the protein quality control (PQC) system, which may be insufficient to correctly remove the misfolded proteins. In other target tissue, such as the muscles, a different physiological PQC regulation may be helpful to remove misfolded proteins related to MNDs. The PQC system requires the activities of chaperones, degradative systems ubiquitin- proteasome (UPS) and autophagy. After misfolded protein recognition by chaperones, the dynein motor complex plays a crucial role to efficiently remove these species via autophagy, transporting them to autophagosome and assisting autophagosome- lysosome fusion. In this thesis, I have investigated the implications of protein misfolding in SBMA and in ALS. Taking advantage of a comparative analysis of misfolded proteins response in skeletal muscle and in spinal cord of SMBA mice, we proved that autophagy is dramatically perturbed in muscles. Indeed, we found the up-regulation of most autophagic markers (Beclin-1, ATG10, p62/SQSTM1, LC3). In addition, the chaperon small Heat Shock Protein B8 (HSPB8) and its co-chaperone BCL2-Associated Athanogene 3 (BAG3), required for autophagy, were robustly up-regulated together with other specific HSPB8 interactors (HSPB2 and HSPB3). Interestingly, the BAG3:BAG1 ratio, increased in muscle, suggesting preferential misfolded proteins routing to autophagy rather than to proteasome. Misfolded proteins, recognized by HSPB8-BAG3 complex, are actively transport by dynein to MTOC to be inserted in autophagosome and degraded by autophagy, Then, we analysed the role of dynein mediate transport in the autophagic removal of misfolded proteins. In immortalized motoneuronal NSC34 cells, we found that the reduction of dynein protein levels, obtained using a specific siRNA, resulted in autophagy inhibition and in unexpected testosterone dependent ARpolyQ aggregates reduction. Also, we found that pharmacological dynein inhibition, with erythro-9-(2- Hydroxy-3-nonyl) adenine hydrochloride (EHNA), in NSC34 cells expressing ARpolyQ, mutant SOD1, truncated TDP43 form or C9ORF72 DPRs, induced a great reduction of mutant protein aggregates, even in presence of an autophagy inhibitor (3-MA), but not of a proteasome inhibitor (MG132). By performing fractionation studies we found that EHNA increased the ARpolyQ levels in PBS and Triton-X100 fractions. Surprisingly, we found that ENHA effects were paralleled by an increased expression of BAG1, a co- chaperone which routes misfolded proteins to UPS, but not of BAG3 suggesting the prevalence of UPS functions. Indeed, when dynein activity was blocked, BAG3:BAG1 ratio was decreased, thus in favour of BAG1 expression, suggesting the involvement of the pro-degradative activity of BAG1 on ARpolyQ aggregates. Collectively, these data show that mutant ARpolyQ induces a potent autophagic response in muscle cells. This may be useful to evaluate the SBMA progression. In parallel, dynein blockage perturbs autophagy and modifies the response of PQC system to misfolded protein. This results in reduced aggregation of MNDs-related misfolded proteins, a phenomenon that may occurs via an increase in their solubility and the induction of UPS functions.
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O'Connor, Matthew. "Ruminant prion disease detection and characterisation using protein misfolding cyclic amplification." Thesis, University of Nottingham, 2017. http://eprints.nottingham.ac.uk/41599/.

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Prion diseases or transmissible spongiform encephalopathies (TSE) are characterised by the accumulation of a misfolded conformer (PrPSc) of a host encoded protein (PrPC). The misfolding event that leads to the formation PrPSc can be replicated in the in vitro amplification technique, protein misfolding cyclic amplification (PMCA). This thesis focuses on the application PMCA to study multiple aspects of prion misfolding in relation to ruminant prion diseases, specifically developing techniques to detect and characterise PrPSc in scrapie and BSE infections. Utilising recombinant hamster PrP (rPrP) as substrate in PMCA, multiple genotypes of scrapie were successfully amplified in an attempt to describe a quantifiable technique applicable to a wide range of scrapie isolates. Observations of non-specific protease resistant rPrP formation was investigated with modifications to the PMCA methodology, which ultimately proved unsuccessful in reducing non-specific protease resistant rPrP. Using brain PrPC as substrate, the quantitative PMCA technique was piloted with BSE to correlate in vitro replication efficiency with infectious titre in mouse bioassay, but no correlation was identified. Atypical forms of BSE occur primarily in older cattle, are asymptomatic and thought to be spontaneous diseases. None the less, infection models in rodents and primates have identified the zoonotic potential of H-type and L-type BSE. Therefore PMCA methods were developed which were able to successfully amplify both atypical forms of BSE. In particular, sensitive detection and discrimination from classical BSE was demonstrated for H-type BSE, which has not previously been amplified in PMCA. H-type BSE could be detected in 1x10¬-12 g brain material and was discriminated from classical BSE by increased protease sensitivity, relatively high molecular weight and antibody reactivity. Evidence exists for co-infection of TSE strains, yet scrapie and BSE co-infection in an ovine host remains unaddressed. To study the disease progression and tissue dissemination of co-infections a PMCA assay capable of specifically amplifying BSE PrPSc in the presence of excess scrapie was applied to artificially mixed brain homogenates containing BSE and scrapie, and compared to current statutory strain typing methods. The PMCA was found to have sensitivity and specificity of 100% in mixes containing 0.1% BSE and 99.9% scrapie brain material, which was more effective than conventional strain typing methods. The assay was then applied to the brain, spleen and lymph of scrapie and BSE experimental co-infections in two genotypes of sheep, and to animals which belonged to a flock with endemic natural scrapie and that also received experimental BSE infections. The PMCA data demonstrated that sheep with PRNP genotype ARQ/ARQ (at amino acid positions 134, 154 and 171) were resistant to BSE in a co-infection scenario. In sheep with PRNP genotype of VRQ/ARQ, mixed infections could occur, and animals with scrapie PrPSc only in the brain could harbour BSE PrPSc in peripheral tissues. Co-infection was also possible in sheep with natural scrapie infections. The assay was compared to conventional testing methods of western blotting, PrPd profiling and immunohistochemistry and displayed superior sensitivity in BSE detection. PMCA amplification of bovine BSE isolates in ovine substrates identified several instances in which the molecular characteristics of the PrPSc was scrapie-like in terms of molecular weight, antibody reactivity and glycoform profile, and in some cases PrPSc characteristic of BSE could no longer be recovered. This occurred in a genotype specific manner, ‘molecular switching’ was only apparent in ovine substrate VRQ/VRQ in accordance with previous findings. These results raise the possibility of such an event occurring in in vivo ovine BSE infections and the zoonotic potential of these scrapie like conformers are yet to be fully addressed.
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Sajjad, Muhammad Umar. "Regulation of the redox homeostasis during polyglutamine misfolding in Huntington's Disease." Thesis, University of Southampton, 2010. https://eprints.soton.ac.uk/168315/.

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Huntington's Disease (HD) is one of many neurodegenerative diseases that are associated with protein misfolding, aggregation and oxidative stress. While several changes in the redox homeostasis have been shown to occur in HD animal models and HD brains, the formal relationships between intracellular protein misfolding that occurs in HD, redox dysregulation and cellular toxicity are unknown. Therefore, several cellular models of intracellular polyglutamine (polyQ) protein misfolding were established for mechanistic studies. Various in vitro transient and stable cell expression systems expressing an N-terminal fragment of huntingtin (htt) (httExon 1, httEx1) with/or without a polyQ expansion and fused to fluorescent proteins were characterized. Mutant httEx1 (mhttEx1) constructs expressed in both neuronal and non-neuronal cell lines produced early polyQ aggregates and intracellular inclusion bodies (IBs) followed by cell toxicity that increased over time in time-course experiments. Using oxidation-sensitive probes, reactive oxygen species (ROS) were measured in polyQ-expressing cells using single, live-cell imaging analysis by confocal microscopy or population assays in order to explore the relationship between polyQ aggregation, ROS production and cellular toxicity. This study highlighted an early increase in ROS due to the expression of aggregation-prone mhttEx1 in both transient and stable cellular systems that coincided with polyQ aggregation, but preceded cell death. Suppression of ROS and toxicity was achieved by two antioxidant compounds (L-NAC and Trolox). Moreover, the use of MitoQ (Coenzyme Q10 covalently attached to triphenylphosphonium cation (TPP+)) at nanomolar concentrations abrogated the increased ROS due to mhttEx1 suggesting a mitochondrial origin of ROS. Given that molecular chaperones regulate the folding/misfolding of proteins and are involved in the regulation of the cellular redox homeostasis, the role of the redoxactivatable chaperone DJ-1 in HD was investigated. Protein expression analysis in HD cell models, a rodent model of HD and human HD brain samples showed an up-regulation of DJ-1 protein expression compared to control samples. Oxidation of DJ-1 was also elevated in the human HD cortex. To test for a functional role of DJ-1 elevation and oxidation in HD, DJ-1 was overexpressed with wild-type or mhttEx1 in cell lines and mouse primary astrocytes. Overexpression of DJ-1 accelerated mhttEx1 aggregation and toxicity both of which could be suppressed by exposure of cells to mild oxidants suggesting that DJ-1, when redox-activated to a chaperone, modulates polyQ aggregation and toxicity. This hypothesis was tested by overexpression of mhttEx1 with a DJ-1 mutant lacking a critical redox activatable cysteine (Cys106). The C106S-DJ-1 mutant lost its ability to reduce polyQ aggregation and toxicity under oxidising conditions upon co-expression with mhttEx1 suggesting that DJ-1 indeed functions as a modulator of polyQ misfolding and toxicity. Together this work suggests that ROS may be produced during polyQ aggregation and is involved in cellular toxicity. This study also shows that DJ-1 regulates both, polyQ aggregation and toxicity in cell models and given the increased DJ-1 expression in vitro and in vivo (human HD), this protein could be a potential target for HD therapy.
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BROGGINI, LUCA. "MOLECULAR DETERMINANTS UNDERLYING PROTEIN MISFOLDING AND AGGREGATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/831967.

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Proteins have evolved to adopt distinctive and well-defined functional states under physiological conditions, either as monomers or complexes. The achievement of a three-dimensional structure allows proteins to exert their physiological functions. Nevertheless, when proteins lose – or fail to acquire – their spatial organization, they can convert into aggregated species that can be harmful to the organism. Conformational diseases gather all those pathologies characterized by the misfolding and aggregation of proteins. Indeed, while the formation and deposition of proteinaceous aggregates can be toxic to cells, the lack of active folded protein disrupts normal physiological pathways. Although considerable progresses have been made in the recent years, to date conformational diseases are still incurable. Indeed, the incomplete understanding of the causes guiding protein misfolding and aggregation prevents the development of efficient treatments. At the same time, the complexity and the diversity of the processes leading to the formation of aggregated species make the task extremely challenging. This PhD project was developed to provide a more comprehensive overview of the molecular bases underlying the conversion of soluble and functional states into aggregated and potentially toxic species. To reach such aims, we applied an integrative approach on two model systems, neuroserpin (NS) and beta-2 microglobulin (2m). In particular, we combined a series of biophysical, biochemical and structural techniques to study these two proteins which have been largely used as model systems for serpin polymerization and amyloid formation, respectively. We found that protein misfolding and aggregation processes depend on several molecular properties, including primary sequence, denatured state compactness, thermal stability, ability to form oligomers under physiological conditions, and the presence of post-translation modifications. The data presented in this PhD thesis add valuable information to depict the complex framework of protein misfolding and aggregation.
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Trist, Benjamin. "Superoxide dismutase 1 in the aetiology of Parkinson’s disease." Thesis, The University of Sydney, 2019. http://hdl.handle.net/2123/20579.

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Parkinson’s disease is the most common neurodegenerative movement disorder worldwide, and is the fastest growing neurological disease ahead of Alzheimer’s disease. Characteristic motor dysfunction results from the selective death of dopamine neurons in the substantia nigra pars compacta, however the aetiology of this neuron loss remains unknown. As such, current treatments help to alleviate Parkinsonian motor symptoms, but none are able to slow or halt the rate of dopaminergic neuron loss. A greater understanding of the molecular pathways leading to dopamine neuron death will accelerate the development of disease-modifying treatments that slow or halt neurodegeneration in this disorder. This thesis focusses on three focal points within the parkinsonian degenerative cascade; oxidative stress, copper dyshomeostasis, and protein misfolding, and aims to introduce the antioxidant copper-binding protein, superoxide dismutase 1 (SOD1), as an important nexus between these key pathologies. I describe, for the first time, misfolding and dysfunction of SOD1 localized to degenerating brain regions in Parkinson’s disease, which is significantly associated with both Lewy proteinopathy and neuron death in these regions. Importantly, I provide evidence that the development of this pathology precedes nigral dopamine neuron loss, and is therefore likely to be a causative factor in, rather than a result of, neurodegeneration in Parkinson’s disease. The sole use of post-mortem tissues within this study ensured any identified biochemical changes accurately reflected endogenous changes occurring within PD and ALS patients; a major criticism of current model systems aiming to recapitulate PD and ALS pathology. My work proposes SOD1 may constitute a novel target for therapeutic interventions aiming to slow the rate of dopaminergic neuron loss in Parkinson’s disease. Novel SOD1 proteinopathy in the Parkinson’s disease brain bears remarkable similarities to neurotoxic SOD1 proteinopathy in a proportion of familial amyotrophic lateral sclerosis (fALS) patients, suggesting similar pathways to neuron death in both disorders. The absence of SOD1 gene mutations in Parkinson’s disease patients exhibiting substantial SOD1 proteinopathy strengthens data from SOD1-fALS research demonstrating that non-genetic factors play key roles in SOD1 misfolding and dysfunction, especially biometal dyshomeostasis and oxidative stress. I demonstrate that these factors may also underlie the misfolding of soluble wild-type SOD1 protein in the vulnerable ventral spinal cord in non-SOD1-fALS and sALS patients, and propose that SOD1 toxicity arises in these patients irrespective of the formation of large insoluble misfolded SOD1 deposits. Importantly, shared pathways to neurodegeneration in Parkinson’s disease and ALS identified within this thesis highlight the potential for the translation of therapeutic approaches targeting SOD1, already in clinical trials for ALS, into disease-modifying therapies for Parkinson’s disease.
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Kundra, Rishika. "Homeostasis of metastable proteins in Alzheimer's disease." Thesis, University of Cambridge, 2017. https://www.repository.cam.ac.uk/handle/1810/268485.

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Alzheimer’s disease (AD) is the most common cause of dementia, affecting almost 40 million people worldwide, and it is predicted that this number will rise to nearly 150 million by 2050. It results not only in enormous distress for affected individuals and carers but also a substantial economic burden on society. Although more than 100 years have passed since its discovery, no cure for AD exists, despite enormous efforts in basic and clinical research over the past few decades, due to limited understanding of its underlying mechanisms. Neurodegenerative disorders, of which AD is an example, are highly complex disorders characterized by extensive neuronal dysfunction associated with the misfolding and aggregation of a specific set of proteins, including amyloid plaques and neurofibrillary tangles in AD. One promising avenue for progress in the field is to improve our understanding of the mechanisms by which cellular dysfunction arises from the initial protein aggregation events. The studies described in the thesis are based on the recent finding that a large number of proteins are inherently supersaturated, being expressed at concentrations higher than their solubilities, and constituting a metastable subproteome potentially susceptible to aggregation. These studies illustrate the dependence of aggregation prone metastable proteins on the cellular degradation machineries. They also study the role of metastable proteins and their homeostasis complement in the vulnerability of various body and brain tissues to protein aggregation diseases. Using extensive sequencing data and network based systems biology approaches, they elucidate how fundamental physicochemical properties of an individual or group of proteins relate to their biological function or dysfunction.
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Griffiths-Jones, Samuel R. "Peptide models for protein beta-sheets." Thesis, University of Nottingham, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364650.

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Books on the topic "Misfolding disease"

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Bross, Peter, and Niels Gregersen. Protein Misfolding and Disease. New Jersey: Humana Press, 2003. http://dx.doi.org/10.1385/1592593941.

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Hill, Andrew F., Kevin J. Barnham, Stephen P. Bottomley, and Roberto Cappai, eds. Protein Folding, Misfolding, and Disease. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-60327-223-0.

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name, No. Protein misfolding and disease: Principles and protocols. Totowa, NJ: Humana Press, Inc., 2003.

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Peter, Bross, and Gregersen Niels, eds. Protein misfolding and disease: Principles and protocols. Totowa, N.J: Humana Press, 2003.

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Protein folding, misfolding, and disease: Methods and protocols. New York: Humana, 2011.

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Bross, Peter, and Niels Gregersen, eds. Protein Misfolding and Cellular Stress in Disease and Aging. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-756-3.

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Protein misfolding and cellular stress in disease and aging: Concepts and protocols. New York: Humana Press, 2010.

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Ramirez-Alvarado, Marina, Jeffery W. Kelly, and Christopher M. Dobson, eds. Protein Misfolding Diseases. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.

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Gomes, Cláudio M., ed. Protein Misfolding Diseases. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8820-4.

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Ferenc, Orosz, Ovádi Judit 1941-, and SpringerLink (Online service), eds. Protein Folding and Misfolding: Neurodegenerative Diseases. Dordrecht: Springer Netherlands, 2009.

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Book chapters on the topic "Misfolding disease"

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Edmunds, Tim. "Gaucher Disease." In Protein Misfolding Diseases, 469–85. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch21.

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Scheinost, Johanna C., Grant E. Boldt, and Paul Wentworth. "Protein Misfolding and Disease." In Chemical Biology, 379–400. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2012. http://dx.doi.org/10.1002/9781118435762.ch19.

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Pennuto, Maria, and Kenneth H. Fischbeck. "Therapeutic Prospects for Polyglutamine Disease." In Protein Misfolding Diseases, 887–902. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch40.

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Wetzel, Ronald. "Misfolding and Aggregation in Huntington Disease and Other Expanded Polyglutamine Repeat Diseases." In Protein Misfolding Diseases, 305–24. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch14.

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Sim, Valerie L., and Byron Caughey. "Prion Disease Therapy: Trials and Tribulations." In Protein Misfolding Diseases, 259–303. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch13.

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Wang, Yongting, and Jonathan A. King. "Cataract as a Protein-Aggregation Disease." In Protein Misfolding Diseases, 487–515. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch22.

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Roberts, Blaine R., and Ashley I. Bush. "Role of Metals in Alzheimer Disease." In Protein Misfolding Diseases, 543–58. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch24.

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Chakrabarty, Paramita, Pritam Das, and Todd E. Golde. "Current and Future Therapies for Alzheimer Disease." In Protein Misfolding Diseases, 711–74. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch34.

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Price, Donald L., Alena V. Savonenko, Tong Li, Michael K. Lee, and Philip C. Wong. "Alzheimer Disease: Protein Misfolding, Model Systems, and Experimental Therapeutics." In Protein Misfolding Diseases, 231–58. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch12.

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Balch, William E., Ineke Braakman, Jeff Brodsky, Raymond Frizzell, William Guggino, Gergely L. Lukacs, Christopher Penland, et al. "Folding Biology of Cystic Fibrosis: A Consortium-Based Approach to Disease." In Protein Misfolding Diseases, 425–52. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch19.

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Conference papers on the topic "Misfolding disease"

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Collar, Giovanna Carello, Marco Antônio De Bastiani, and Eduardo R. Zimmer. "HUNTINGTON’S DISEASE AND EARLYONSET ALZHEIMER’S DISEASE SHARE A TRANSCRIPTOMIC SIGNATURE." In XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda082.

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Background: Neurodegenerative diseases share progressive loss of neurons and protein misfolding, which ultimately culminates in dementia; many diseases have been identified as causes of early-onset dementia (< 65 years of age) such as Huntington’s disease (HD) and early-onset Alzheimer’s disease (EOAD). Importantly, disease-specific genetic mutations have already been identified for HD and EOAD. Thus, one could suggest that the molecular link between these diseases may arise from alterations at the transcriptomic level, which is yet to be determined. Objective: We aimed at identifying transcriptome similarities between HD and EOAD. Methods: We collected data of the postmortem cerebral cortex from 1 HD and 6 AD microarray studies in the Gene Expression Omnibus. Of note, only subjects with age at death under 65 were selected (HD: n = 158, controls: n = 158; EOAD: n = 65, controls: n = 266). Differential expression and functional enrichment analyses were performed. Results: We identified 1,260 differentially expressed genes and 675 enriched gene ontology terms between HD and EOAD. Conclusion: Our results demonstrate a transcriptomic signature shared by HD and EOAD. Unveiling the similarities between these diseases at the transcriptomic level could advance our knowledge about pathogenesis and may help to develop therapeutic strategies targeting early-onset dementias.
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Bellotti, Vittorio, and Monica Stoppini. "Nanotechnology drives a paradigm shift on protein misfolding diseases and amyloidosis." In THEORY AND APPLICATIONS IN COMPUTATIONAL CHEMISTRY: THE FIRST DECADE OF THE SECOND MILLENNIUM: International Congress TACC-2012. AIP, 2012. http://dx.doi.org/10.1063/1.4730667.

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Hammarström, Per, Mikael Lindgren, and K. Peter R. Nilsson. "Luminescent conjugated oligothiophenes: optical dyes for revealing pathological hallmarks of protein misfolding diseases." In SPIE Photonic Devices + Applications, edited by Ruth Shinar and Ioannis Kymissis. SPIE, 2010. http://dx.doi.org/10.1117/12.859808.

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Elbashir, Israa, Aisha Aisha Nasser J. M. Al-Saei, Paul Thornalley, and Naila Rabbani. "Evaluation of antiviral activity of Manuka honey against SARS-CoV-2." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2021. http://dx.doi.org/10.29117/quarfe.2021.0113.

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Background and aims: In 2020 a global pandemic was declared caused by the severe acute respiratory syndrome coronavirus (SARS-CoV-2). The pandemic is still ongoing and continues to cause considerable mortality and morbidity world-wide and new variants of the virus are emerging. Rapid development and rollout of vaccines for SARS-CoV-2 is in progress to counter the pandemic but has been tempered by the emergence of new SARS-CoV-2 variants, many of which exhibit reduced vaccine effectiveness. To date there is no approved antiviral treatment for coronavirus disease 2019 (COVID-19). Several studies have shown that Manuka honey has virucidal/antiviral effect. Methylglyoxal (MG), a bioactive component in Manuka honey, has antiviral activity in vitro. MG may modify arginine residues in the functional domains of viral spike and nucleocapsid proteins, resulting in loss of charge, protein misfolding and inactivation. The aim of this study was to characterize the antiviral activity of Manuka honey against SARS-CoV-2 in vitro Materials and methods: Wild-type SARS-CoV-2 with titers of multiplicities of infection (MOI) 0.1 and 0.05 were incubated with 2-fold serial dilutions of 250+ Manuka honey (equivalent to 250 to 31 µM) in infection medium (Dulbecco's Modified Eagle Medium + 2% fetal bovine serum + 100 units/ml penicillin + 100 µg/ml streptomycin) for 3 h. Manuka honey treated and untreated control SARS-CoV-2 was incubated with confluent cultures of Vero cells in vitro for 1 h, cultures washed with phosphate-buffered saline and incubated in fresh infection medium at 37°C for 4 - 5 days until 70% of virus control cells displayed cytopathic effect. We also studied the effect of scavenging MG in Manuka Honey with aminoguanidine (AG; 500 µM) on virucidal activity. The antiviral activity of MG was judged by median tissue culture infectious dose (TCID50) assays. Data analysis was by logistic regression. TCID50 (mean ± SD) was deduced by interpolation. Results: Diluted Manuka honey inhibited SARS-CoV-2 replication in Vero cells. SARS-CoV-2 was incubated in diluted Manuka honey in medium at 37°C for 3 h before adding to Vero cells. Manuka honey dilutions down to 125 µM MG equivalents completely inhibited cytopathic effect of SARS-CoV-2 whereas 31.25 µM and 62.5 µM MG equivalents had limited effect. Logistic regression and interpolation of the cytopathic effect indicated that the TCID50 = 72 ± 2 µM MG equivalents for MOI of 0.1. Prior scavenging of MG by addition of AG resulted in virus replication levels equivalent to those seen in the virus control without AG. Conclusion: Manuka honey has antiviral activity against SARS-CoV-2 when incubated with the virus in cell-free media at no greater than ca. 40-fold dilutions of 250+ grade. Anti-viral activity was inhibited by AG, consistent with the anti-viral effect being mediated by MG. Manuka honey dilutions in MG equivalents had similar antiviral effect compared to authentic MG, also consistent with MG content of Manuka honey mediating the antiviral effect. Whilst Manuka honey may inactivate SARS-CoV-2 in cell-free culture medium, its antiviral activity in vivo for other than topical application may be limited because of the rapid metabolism of MG by the glyoxalase system and limited bioavailability of oral MG.
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