Literatura académica sobre el tema "Α-synuclein aggregation"
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Artículos de revistas sobre el tema "Α-synuclein aggregation"
Surguchov, Andrei y Alexei Surguchev. "Synucleins: New Data on Misfolding, Aggregation and Role in Diseases". Biomedicines 10, n.º 12 (13 de diciembre de 2022): 3241. http://dx.doi.org/10.3390/biomedicines10123241.
Texto completoHam, Sangwoo, Seung Pil Yun, Hyojung Kim, Donghoon Kim, Bo Am Seo, Heejeong Kim, Jeong-Yong Shin et al. "Amyloid-like oligomerization of AIMP2 contributes to α-synuclein interaction and Lewy-like inclusion". Science Translational Medicine 12, n.º 569 (11 de noviembre de 2020): eaax0091. http://dx.doi.org/10.1126/scitranslmed.aax0091.
Texto completoGalvagnion, Céline, James W. P. Brown, Myriam M. Ouberai, Patrick Flagmeier, Michele Vendruscolo, Alexander K. Buell, Emma Sparr y Christopher M. Dobson. "Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein". Proceedings of the National Academy of Sciences 113, n.º 26 (13 de junio de 2016): 7065–70. http://dx.doi.org/10.1073/pnas.1601899113.
Texto completoHashimoto, Makoto, Edward Rockenstein, Michael Mante, Margaret Mallory y Eliezer Masliah. "β-Synuclein Inhibits α-Synuclein Aggregation". Neuron 32, n.º 2 (octubre de 2001): 213–23. http://dx.doi.org/10.1016/s0896-6273(01)00462-7.
Texto completoANDREKOPOULOS, Christopher, Hao ZHANG, Joy JOSEPH, Shasi KALIVENDI y B. KALYANARAMAN. "Bicarbonate enhances alpha-synuclein oligomerization and nitration: intermediacy of carbonate radical anion and nitrogen dioxide radical". Biochemical Journal 378, n.º 2 (1 de marzo de 2004): 435–47. http://dx.doi.org/10.1042/bj20031466.
Texto completoRott, Ruth, Raymonde Szargel, Vered Shani, Haya Hamza, Mor Savyon, Fatimah Abd Elghani, Rina Bandopadhyay y Simone Engelender. "SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation". Proceedings of the National Academy of Sciences 114, n.º 50 (27 de noviembre de 2017): 13176–81. http://dx.doi.org/10.1073/pnas.1704351114.
Texto completoEstaun-Panzano, Juan, Marie-Laure Arotcarena y Erwan Bezard. "Monitoring α-synuclein aggregation". Neurobiology of Disease 176 (enero de 2023): 105966. http://dx.doi.org/10.1016/j.nbd.2022.105966.
Texto completoCaló, Laura, Eric Hidari, Michal Wegrzynowicz, Jeffrey W. Dalley, Bernard L. Schneider, Martyna Podgajna, Oleg Anichtchik, Emma Carlson, David Klenerman y Maria Grazia Spillantini. "CSPα reduces aggregates and rescues striatal dopamine release in α-synuclein transgenic mice". Brain 144, n.º 6 (24 de marzo de 2021): 1661–69. http://dx.doi.org/10.1093/brain/awab076.
Texto completoJENSEN, Poul H., Peter HØJRUP, Henrik HAGER, Morten S. NIELSEN, Linda JACOBSEN, Ole F. OLESEN, Jørgen GLIEMANN y Ross JAKES. "Binding of Aβ to α- and β-synucleins: identification of segments in α-synuclein/NAC precursor that bind Aβ and NAC". Biochemical Journal 323, n.º 2 (15 de abril de 1997): 539–46. http://dx.doi.org/10.1042/bj3230539.
Texto completoKrumova, Petranka, Erik Meulmeester, Manuel Garrido, Marilyn Tirard, He-Hsuan Hsiao, Guillaume Bossis, Henning Urlaub et al. "Sumoylation inhibits α-synuclein aggregation and toxicity". Journal of Cell Biology 194, n.º 1 (11 de julio de 2011): 49–60. http://dx.doi.org/10.1083/jcb.201010117.
Texto completoTesis sobre el tema "Α-synuclein aggregation"
Oliveira, Márcia Santos. "Modulation of α-synuclein aggregation and toxicity". Master's thesis, Faculdade de Ciências e Tecnologia, 2013. http://hdl.handle.net/10362/11195.
Texto completoIt is widely known that α-synuclein (aSyn) is an amyloidogenic protein prone to aggregation. This protein is found in specific inclusions named Lewy bodies in the surviving neurons of Parkinsons’s disease patients and other synucleinopathy brains. This aggregation process is greatly affected by different post-translational modifications, such as phosphorylation, acetylation, and glycation. Lately it was shown that aSyn oligomeric species are more toxic than the inclusion bodies. Heat shock proteins (HSPs) are molecular chaperones able to modulate the folding and refolding of proteins. Its overexpression in Parkinson’s disease models reduces and prevents aSyn aggregation. As the reduction of aSyn aggregation can lead to an eventual accumulation of oligomeric species which may cause cell damage, the main goal of this work is to better understand the role of HSPs in aSyn oligomer formation, clarifying which are the aSyn resulting species formed in the presence of HSPs. Moreover, as glycation is suggested to accelerate abnormal protein deposition, we aimed to investigate how HSPs interfere with the oligomerization process of glycated aSyn. In this study Hsp70 seemed to induce recombinant aSyn oligomerization, generating higher molecular weight species with no associated toxicity. On the other hand, Hsp27 reduced aSyn oligomerization in vitro possibly by inducing the formation of non-reactive small oligomers. MGO glycation increased protein aggregation and cell death. Interestingly, Hsp27 overexpression reversed glycated aSyn aggregation and its associated toxicity. These results demonstrate the importance of HSPs modulation as a possible target of Parkinson’s disease therapeutics.
Waudby, Christopher Andrew. "Structural and biophysical studies of α-synuclein and protein aggregation". Thesis, University of Cambridge, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.611252.
Texto completoPiroska, Marian-Leonard. "Engineering artificial biomolecular condensates to study the aggregation of α-Synuclein". Electronic Thesis or Diss., Sorbonne université, 2023. https://accesdistant.sorbonne-universite.fr/login?url=https://theses-intra.sorbonne-universite.fr/2023SORUS542.pdf.
Texto completoNeurodegenerative diseases, such as Alzheimer's, Parkinson's, and Huntington's disease, are incurable illnesses characterized by the progressive degeneration of neurons, leading to cognitive and motor deficits in affected individuals. The development of effective treatments is currently limited by our incomplete understanding of the underlying mechanisms that drive disease initiation and progression. One prevailing characteristic observed in the tissues affected by neurodegenerative diseases is the presence of aggregated proteins, which have become hallmarks of diseases such as Parkinson’s and Alzheimer’s. Thus, the aggregation process is believed to play a pivotal role in disease pathogenesis. However, the specific mechanisms underlying the transition of soluble proteins to their aggregated state remain elusive. Recent research has proposed phase separation (PS) as a critical intermediate step in the formation of protein aggregates. PS is a physical phenomenon wherein certain proteins undergo a phase transition, forming distinct liquid-like droplets within the cellular environment. Biomolecular condensates are involved in various physiological cellular processes, but are also increasingly believed to be subject to aberrant behaviours that can trigger pathological conditions. Although promising, studying the role of PS in the context of neurodegenerative diseases is a challenging task, due to the intricate composition of cellular condensates. They consist of tens to hundreds of different biomolecules, including proteins, nucleic acids, and lipids, creating a complex milieu that demands innovative research approaches. To improve the study of LLPS in the context of neurodegenerative diseases, we have developed a method for the controlled formation and dissolution of biomolecular condensates enriched in proteins involved in pathological aggregation. First, we created condensates containing α-synuclein (α-Syn), the main pathological factor in Parkinson’s disease and other pathologies. α-Syn is known as a prion-like protein, meaning that its aggregates spreads from cell to cell and template the aggregation of soluble cytosolic α-Syn, promoting the progression of the disease. However, little is known about this phenomenon with respect to the condensed state of the protein. To simulate this phenomenon, we exposed cells expressing our α-Syn condensates to preformed α-Syn aggregates in fibrillar form. We observed that fibrils triggered the transition of condensates from their liquid-like state to an aggregated form with solid-like properties and exhibiting biochemical markers characteristic of amyloids. This allowed us to propose a model where the condensed phase of α-Syn speeds up the propagation of pathological aggregates, by providing a pool of concentrated protein that can undergo more easily an amyloid transition via the prion-like pathway. Subsequently, we have built artificial condensates enriched in α-Syn together with synapsin. In neurons, α-Syn and synapsin interact at the presynaptic termini, where they play an important role in the release of neurotransmitters by controlling the clustering, trafficking and release of membrane-enclosed neurotransmitter containers called synaptic vesicles. In our setting α-Syn/synapsin condensates were also subject to a liquid-to-solid transition mediated by α-Syn fibrils
Rcom-H'cheo-Gauthier, Alexandre Nay. "The Protective Effect of Calbindin-D28K on a-Synuclein Aggregation in α- Synucleinopathies". Thesis, Griffith University, 2016. http://hdl.handle.net/10072/368168.
Texto completoThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Medical Science
Griffith Health
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Peduzzo, Alessia [Verfasser]. "Mechanistic insights into α-synuclein aggregation: from fibril stability to surface nucleation / Alessia Peduzzo". Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2019. http://d-nb.info/1201881978/34.
Texto completoRivers, Robert Clay. "Biophysical analysis of the aggregation behaviour and structural properties of α- and β-synuclein". Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612821.
Texto completoCheruvara, Harish. "Intracellular peptide library screening to derive inhibitors of Parkinson's disease associated α-synuclein aggregation". Thesis, University of Essex, 2015. http://repository.essex.ac.uk/16040/.
Texto completoFillon, Gwenaëlle. "Pathologies associated to α-synuclein aggregation in primary culture models of multiple system atrophy". Paris 6, 2006. http://www.theses.fr/2006PA066030.
Texto completoRoman, Andrei. "Tau protein aggregation and α-synuclein dysfunction : development of new in vitro and in vivo models to study neurodegenerative diseases". Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0281.
Texto completoThe histopathological hallmarks of the most common neurodegenerative diseases – Alzheimer’s disease and Parkinson’s disease are neurofibrillary tangles formed by tau protein and Lewy bodies inclusions formed by aggregated α-synuclein. The formation and accumulation of these proteins into inclusions cause functional disruptions of the cytoskeleton and leads to neuronal degeneration. The precise mechanisms of tau and synuclein misfolding and aggregation leading to those cellulare incluses, even though very studied, are not fully understood neither for tau protein nor for α-synuclein.Here we have addressed this question using both in vitro and in vivo models. Investigating tau aggregation in vitro, we have found a reversible self-assembly of tau, which depends on temperature and is induced by zinc ions, which is different from the tau aggregation in the presence of aggregation-inducers such as heparin. This process could be implicated in the first steps of tau pathological aggregation. In a second part, we have developed a mouse model for studying the α-synuclein dysfunction. We have shown that α- synuclein is directly involved in the embryonic development of the specific regions of the nervous system, and that it has modulating effect only on the populations of dopaminergic neurons of substantia nigra, which are affected in Parkinson’s disease.Results obtained in our studies of two proteins that undergo pathogenic aggregation and form intracellular inclusions contributed to understanding of molecular and cellular processes associated with neuronal degeneration, which is important for the development of new disease-modifying therapies of neurodegenerative disorders
APRILE, FRANCESCO ANTONIO. "Extrinsic factors affecting amyloid aggregation". Doctoral thesis, Università degli Studi di Milano-Bicocca, 2012. http://hdl.handle.net/10281/27834.
Texto completoLibros sobre el tema "Α-synuclein aggregation"
Rongve, Arvid y Dag Aarsland. Dementia with Lewy bodies and Parkinson’s disease dementia. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199644957.003.0035.
Texto completoCapítulos de libros sobre el tema "Α-synuclein aggregation"
Paleologou, Katerina E. y Omar M. A. El-Agnaf. "α-Synuclein Aggregation and Modulating Factors". En Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease, 109–64. Dordrecht: Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5416-4_6.
Texto completoMoosa, Mahdi Muhammad, Josephine C. Ferreon y Allan Chris M. Ferreon. "Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation". En Methods in Molecular Biology, 221–33. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9124-2_17.
Texto completoGromiha, M. Michael, S. Biswal, A. M. Thangakani, S. Kumar, G. J. Masilamoni y D. Velmurugan. "Role of Protein Aggregation and Interactions between α-Synuclein and Calbindin in Parkinson’s Disease". En Intelligent Computing Theories and Technology, 677–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-39482-9_78.
Texto completoBentea, Lucian, Peter Csaba Ölveczky y Eduard Bentea. "Using Probabilistic Strategies to Formalize and Compare α-Synuclein Aggregation and Propagation under Different Scenarios". En Computational Methods in Systems Biology, 92–105. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40708-6_8.
Texto completoKumar Chatterjee, Swapan, Snigdha Saha y Shahin Muhammed T.K. "COVID-19 and Its Impact on Onset and Progression of Parkinson’s and Cognitive Dysfunction". En COVID-19 Pandemic, Mental Health and Neuroscience - New Scenarios for Understanding and Treatment [Working Title]. IntechOpen, 2023. http://dx.doi.org/10.5772/intechopen.105667.
Texto completoPolverino de Laureto, Patrizia, Luana Palazzi y Laura Acquasaliente. "Polyphenols as Potential Therapeutic Drugs in Neurodegeneration". En Neuroprotection - New Approaches and Prospects. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.89575.
Texto completoEl-Mansoury, Bilal, Omar El Hiba, Mustapha Agnaou, Arumugam Radhakrishan Jayakumar, Abdelaati El Khiat, Kholoud Kahim, Samira Boulbaroud et al. "Neuropathology of Parkinson's Disease". En Experimental and Clinical Evidence of the Neuropathology of Parkinson’s Disease, 82–101. IGI Global, 2023. http://dx.doi.org/10.4018/978-1-6684-5156-4.ch006.
Texto completoBala, Sapna, Anamika Misra, Upinder Kaur y Sankha Shubhra Chakrabarti. "Resveratrol: A Novel Drug for the Management of Neurodegenerative Disorders". En Traditional Medicine for Neuronal Health, 230–51. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815040197123010015.
Texto completoBell, Rosie, Michele Vendruscolo y Janet R. Kumita. "Probing the effects of N-terminal acetylation on α-synuclein structure, aggregation and cytotoxicity". En Methods in Enzymology. Elsevier, 2023. http://dx.doi.org/10.1016/bs.mie.2022.09.003.
Texto completoJaved, Hayate y Shreesh Ojha. "Therapeutic Potential of Baicalein in Parkinson’s Disease: Focus on Inhibition of α-Synuclein Oligomerization and Aggregation". En Synucleins - Biochemistry and Role in Diseases. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.83589.
Texto completoActas de conferencias sobre el tema "Α-synuclein aggregation"
Dietrich, Heidelinde R. C., Richard L. van den Doel, Wolfgang Hoyer, Wim van Oel, Guus Liqui Lung, Yuval Garini, Thomas Jovin y Ian T. Young. "Adaptation of nanoarrays for the study of α-synuclein aggregation: preliminary results". En Biomedical Optics 2005, editado por Dan V. Nicolau, Joerg Enderlein, Robert C. Leif, Daniel L. Farkas y Ramesh Raghavachari. SPIE, 2005. http://dx.doi.org/10.1117/12.587493.
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