Littérature scientifique sur le sujet « Α-synuclein aggregation »
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Articles de revues sur le sujet "Α-synuclein aggregation"
Surguchov, Andrei, et Alexei Surguchev. « Synucleins : New Data on Misfolding, Aggregation and Role in Diseases ». Biomedicines 10, no 12 (13 décembre 2022) : 3241. http://dx.doi.org/10.3390/biomedicines10123241.
Texte intégralHam, 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, no 569 (11 novembre 2020) : eaax0091. http://dx.doi.org/10.1126/scitranslmed.aax0091.
Texte intégralGalvagnion, Céline, James W. P. Brown, Myriam M. Ouberai, Patrick Flagmeier, Michele Vendruscolo, Alexander K. Buell, Emma Sparr et 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, no 26 (13 juin 2016) : 7065–70. http://dx.doi.org/10.1073/pnas.1601899113.
Texte intégralHashimoto, Makoto, Edward Rockenstein, Michael Mante, Margaret Mallory et Eliezer Masliah. « β-Synuclein Inhibits α-Synuclein Aggregation ». Neuron 32, no 2 (octobre 2001) : 213–23. http://dx.doi.org/10.1016/s0896-6273(01)00462-7.
Texte intégralANDREKOPOULOS, Christopher, Hao ZHANG, Joy JOSEPH, Shasi KALIVENDI et B. KALYANARAMAN. « Bicarbonate enhances alpha-synuclein oligomerization and nitration : intermediacy of carbonate radical anion and nitrogen dioxide radical ». Biochemical Journal 378, no 2 (1 mars 2004) : 435–47. http://dx.doi.org/10.1042/bj20031466.
Texte intégralRott, Ruth, Raymonde Szargel, Vered Shani, Haya Hamza, Mor Savyon, Fatimah Abd Elghani, Rina Bandopadhyay et Simone Engelender. « SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation ». Proceedings of the National Academy of Sciences 114, no 50 (27 novembre 2017) : 13176–81. http://dx.doi.org/10.1073/pnas.1704351114.
Texte intégralEstaun-Panzano, Juan, Marie-Laure Arotcarena et Erwan Bezard. « Monitoring α-synuclein aggregation ». Neurobiology of Disease 176 (janvier 2023) : 105966. http://dx.doi.org/10.1016/j.nbd.2022.105966.
Texte intégralCaló, Laura, Eric Hidari, Michal Wegrzynowicz, Jeffrey W. Dalley, Bernard L. Schneider, Martyna Podgajna, Oleg Anichtchik, Emma Carlson, David Klenerman et Maria Grazia Spillantini. « CSPα reduces aggregates and rescues striatal dopamine release in α-synuclein transgenic mice ». Brain 144, no 6 (24 mars 2021) : 1661–69. http://dx.doi.org/10.1093/brain/awab076.
Texte intégralJENSEN, Poul H., Peter HØJRUP, Henrik HAGER, Morten S. NIELSEN, Linda JACOBSEN, Ole F. OLESEN, Jørgen GLIEMANN et 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, no 2 (15 avril 1997) : 539–46. http://dx.doi.org/10.1042/bj3230539.
Texte intégralKrumova, 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, no 1 (11 juillet 2011) : 49–60. http://dx.doi.org/10.1083/jcb.201010117.
Texte intégralThèses sur le sujet "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.
Texte intégralIt 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.
Texte intégralPiroska, 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.
Texte intégralNeurodegenerative 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.
Texte intégralThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Medical Science
Griffith Health
Full Text
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.
Texte intégralRivers, 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.
Texte intégralCheruvara, 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/.
Texte intégralFillon, Gwenaëlle. « Pathologies associated to α-synuclein aggregation in primary culture models of multiple system atrophy ». Paris 6, 2006. http://www.theses.fr/2006PA066030.
Texte intégralRoman, 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.
Texte intégralThe 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.
Texte intégralLivres sur le sujet "Α-synuclein aggregation"
Rongve, Arvid, et 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.
Texte intégralChapitres de livres sur le sujet "Α-synuclein aggregation"
Paleologou, Katerina E., et Omar M. A. El-Agnaf. « α-Synuclein Aggregation and Modulating Factors ». Dans 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.
Texte intégralMoosa, Mahdi Muhammad, Josephine C. Ferreon et Allan Chris M. Ferreon. « Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation ». Dans 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.
Texte intégralGromiha, M. Michael, S. Biswal, A. M. Thangakani, S. Kumar, G. J. Masilamoni et D. Velmurugan. « Role of Protein Aggregation and Interactions between α-Synuclein and Calbindin in Parkinson’s Disease ». Dans 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.
Texte intégralBentea, Lucian, Peter Csaba Ölveczky et Eduard Bentea. « Using Probabilistic Strategies to Formalize and Compare α-Synuclein Aggregation and Propagation under Different Scenarios ». Dans 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.
Texte intégralKumar Chatterjee, Swapan, Snigdha Saha et Shahin Muhammed T.K. « COVID-19 and Its Impact on Onset and Progression of Parkinson’s and Cognitive Dysfunction ». Dans 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.
Texte intégralPolverino de Laureto, Patrizia, Luana Palazzi et Laura Acquasaliente. « Polyphenols as Potential Therapeutic Drugs in Neurodegeneration ». Dans Neuroprotection - New Approaches and Prospects. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.89575.
Texte intégralEl-Mansoury, Bilal, Omar El Hiba, Mustapha Agnaou, Arumugam Radhakrishan Jayakumar, Abdelaati El Khiat, Kholoud Kahim, Samira Boulbaroud et al. « Neuropathology of Parkinson's Disease ». Dans 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.
Texte intégralBala, Sapna, Anamika Misra, Upinder Kaur et Sankha Shubhra Chakrabarti. « Resveratrol : A Novel Drug for the Management of Neurodegenerative Disorders ». Dans Traditional Medicine for Neuronal Health, 230–51. BENTHAM SCIENCE PUBLISHERS, 2023. http://dx.doi.org/10.2174/9789815040197123010015.
Texte intégralBell, Rosie, Michele Vendruscolo et Janet R. Kumita. « Probing the effects of N-terminal acetylation on α-synuclein structure, aggregation and cytotoxicity ». Dans Methods in Enzymology. Elsevier, 2023. http://dx.doi.org/10.1016/bs.mie.2022.09.003.
Texte intégralJaved, Hayate, et Shreesh Ojha. « Therapeutic Potential of Baicalein in Parkinson’s Disease : Focus on Inhibition of α-Synuclein Oligomerization and Aggregation ». Dans Synucleins - Biochemistry and Role in Diseases. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.83589.
Texte intégralActes de conférences sur le sujet "Α-synuclein aggregation"
Dietrich, Heidelinde R. C., Richard L. van den Doel, Wolfgang Hoyer, Wim van Oel, Guus Liqui Lung, Yuval Garini, Thomas Jovin et Ian T. Young. « Adaptation of nanoarrays for the study of α-synuclein aggregation : preliminary results ». Dans Biomedical Optics 2005, sous la direction de Dan V. Nicolau, Joerg Enderlein, Robert C. Leif, Daniel L. Farkas et Ramesh Raghavachari. SPIE, 2005. http://dx.doi.org/10.1117/12.587493.
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