Relevant bibliographies by topics / Self-assembly - Misfolded Protein

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Academic literature on the topic 'Self-assembly - Misfolded Protein'

Author: Grafiati
Published: 7 September 2023

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Journal articles on the topic "Self-assembly - Misfolded Protein"

1

Krasnoslobodtsev, A., B.-H. Kim, and Y. Lyubchenko. "Nanoimaging for Protein Misfolding Diseases. Critical Role of Misfolded Dimers in the Amyloid Self-Assembly." Microscopy and Microanalysis 17, S2 (2011): 170–71. http://dx.doi.org/10.1017/s1431927611001723.

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2

Pinotsi, Dorothea, Claire H. Michel, Alexander K. Buell та ін. "Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons". Proceedings of the National Academy of Sciences 113, № 14 (2016): 3815–19. http://dx.doi.org/10.1073/pnas.1516546113.

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New strategies for visualizing self-assembly processes at the nanoscale give deep insights into the molecular origins of disease. An example is the self-assembly of misfolded proteins into amyloid fibrils, which is related to a range of neurodegenerative disorders, such as Parkinson's and Alzheimer's diseases. Here, we probe the links between the mechanism of α-synuclein (AS) aggregation and its associated toxicity by using optical nanoscopy directly in a neuronal cell culture model of Parkinson’s disease. Using superresolution microscopy, we show that protein fibrils are taken up by neuronal
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3

Barreca, Maria, Nunzio Iraci, Silvia Biggi, Violetta Cecchetti, and Emiliano Biasini. "Pharmacological Agents Targeting the Cellular Prion Protein." Pathogens 7, no. 1 (2018): 27. http://dx.doi.org/10.3390/pathogens7010027.

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Prion diseases are associated with the conversion of the cellular prion protein (PrPC), a glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded conformer (the scrapie form of PrP, or PrPSc) that accumulates in brain tissues of affected individuals. PrPSc is a self-catalytic protein assembly capable of recruiting native conformers of PrPC, and causing their rearrangement into new PrPSc molecules. Several previous attempts to identify therapeutic agents against prion diseases have targeted PrPSc, and a number of compounds have shown potent anti-prion effects in
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4

Adsi, Hanaa, Shon A. Levkovich, Elvira Haimov, et al. "Chemical Chaperones Modulate the Formation of Metabolite Assemblies." International Journal of Molecular Sciences 22, no. 17 (2021): 9172. http://dx.doi.org/10.3390/ijms22179172.

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The formation of amyloid-like structures by metabolites is associated with several inborn errors of metabolism (IEMs). These structures display most of the biological, chemical and physical properties of protein amyloids. However, the molecular interactions underlying the assembly remain elusive, and so far, no modulating therapeutic agents are available for clinical use. Chemical chaperones are known to inhibit protein and peptide amyloid formation and stabilize misfolded enzymes. Here, we provide an in-depth characterization of the inhibitory effect of osmolytes and hydrophobic chemical chap
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5

Sharma, Vandna, and Kalyan Sundar Ghosh. "Inhibition of Amyloid Fibrillation by Small Molecules and Nanomaterials: Strategic Development of Pharmaceuticals Against Amyloidosis." Protein & Peptide Letters 26, no. 5 (2019): 315–23. http://dx.doi.org/10.2174/0929866526666190307164944.

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Amyloid fibrils are a special class of self-assembled protein molecules, which exhibit various toxic effects in cells. Different physiological disorders such as Alzheimer’s, Parkinson’s, Huntington’s diseases, etc. happen due to amyloid formation and lack of proper cellular mechanism for the removal of fibrils. Therefore, inhibition of amyloid fibrillation will find immense applications to combat the diseases associated with amyloidosis. The development of therapeutics against amyloidosis is definitely challenging and numerous strategies have been followed to find out anti-amyloidogenic molecu
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6

Knowles, Tuomas P. J., Duncan A. White, Christopher M. Dobson, and Mark E. Welland. "Quantitative approaches for characterising fibrillar protein nanostructures." MRS Proceedings 1274 (2010). http://dx.doi.org/10.1557/proc-1274-qq04-05.

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AbstractPolypeptide sequences have an inherent tendency to self-assemble into filamentous nanostructures commonly known as amyloid fibrils. Such self-assembly is used in nature to generate a variety of functional materials ranging from protective coatings in bacteria to catalytic scaffolds in mammals. The aberrant self-assembly of misfolded peptides and proteins is also, however, implicated in a range of disease states including neurodegenerative conditions such as Alzheimer's and Parkinson's diseases. It is increasingly evident that the intrinsic material properties of these structures are cr
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7

Kusmierczyk, Andrew R., and Mark Hochstrasser. "Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis." Biological Chemistry 389, no. 9 (2008). http://dx.doi.org/10.1515/bc.2008.130.

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Abstract The 26S proteasome is the key eukaryotic protease responsible for the degradation of intracellular proteins. Protein degradation by the 26S proteasome plays important roles in numerous cellular processes, including the cell cycle, differentiation, apoptosis, and the removal of damaged or misfolded proteins. How this 2.5-MDa complex, composed of at least 32 different polypeptides, is assembled in the first place is not well understood. However, it has become evident that this complicated task is facilitated by a framework of protein factors that chaperone the nascent proteasome through
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8

Zhang, Yuqi, Yanyan Zhu, Haiyan Yue, Qingjie Zhao, and Huiyu Li. "Exploring the misfolding and self-assembly mechanism of TTR (105–115) peptides by all-atom molecular dynamics simulation." Frontiers in Molecular Biosciences 9 (August 31, 2022). http://dx.doi.org/10.3389/fmolb.2022.982276.

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Pathological aggregation of essentially dissociative Transthyretin (TTR) monomers protein, driven by misfolded and self-interaction, is connected with Amyloid Transthyretin amyloidosis (ATTR) disease. The TTR monomers protein contains several fragments that tend to self-aggregate, such as residue 105–115 sequence [TTR (105–115)]. However, the misfolding and aggregation mechanisms of TTR are still unknown. In this study, we explored the misfolding and self-assembly of TTR (105–115) peptides by all-atom molecular dynamics simulation. Our results indicated that the conformation of the two-peptide
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9

Igel, Angélique, Basile Fornara, Human Rezaei, and Vincent Béringue. "Prion assemblies: structural heterogeneity, mechanisms of formation, and role in species barrier." Cell and Tissue Research, November 18, 2022. http://dx.doi.org/10.1007/s00441-022-03700-2.

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AbstractPrions are proteinaceous pathogens responsible for a wide range of neurodegenerative diseases in animal and human. Prions are formed from misfolded, ß-sheet rich, and aggregated conformers (PrPSc) of the host-encoded prion protein (PrPC). Prion replication stems from the capacity of PrPSc to self-replicate by templating PrPC conversion and polymerization. The question then arises about the molecular mechanisms of prion replication, host invasion, and capacity to contaminate other species. Studying these mechanisms has gained in recent years further complexity with evidence that PrPSc i
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10

Igel-Egalon, Angélique, Florent Laferrière, Mohammed Moudjou, et al. "Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway." Communications Biology 2, no. 1 (2019). http://dx.doi.org/10.1038/s42003-019-0608-y.

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Abstract The dynamics of aggregation and structural diversification of misfolded, host-encoded proteins in neurodegenerative diseases are poorly understood. In many of these disorders, including Alzheimer’s, Parkinson’s and prion diseases, the misfolded proteins are self-organized into conformationally distinct assemblies or strains. The existence of intrastrain structural heterogeneity is increasingly recognized. However, the underlying processes of emergence and coevolution of structurally distinct assemblies are not mechanistically understood. Here, we show that early prion replication gene
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