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Relevant bibliographies by topics / Prion amyloidogenesis

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Journal articles
Dissertations / Theses
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Academic literature on the topic 'Prion amyloidogenesis'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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Journal articles on the topic "Prion amyloidogenesis"

1

Kinoshita, Misaki, Yuxi Lin, Masatoshi Nakatsuji, Takashi Inui, and Young-Ho Lee. "Kinetics and polymorphs of yeast prion Sup35NM amyloidogenesis." International Journal of Biological Macromolecules 102 (September 2017): 1241–49. http://dx.doi.org/10.1016/j.ijbiomac.2017.05.001.

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Shirasaka, Maki, Kazuo Kuwata та Ryo Honda. "α-Synuclein chaperone suppresses nucleation and amyloidogenesis of prion protein". Biochemical and Biophysical Research Communications 521, № 1 (2020): 259–64. http://dx.doi.org/10.1016/j.bbrc.2019.10.120.

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Schininà, M. E., Bruno Maras, Franco Cardone, et al. "Prion protein allotype profiling by mass spectrometry." Pure and Applied Chemistry 75, no. 2-3 (2003): 317–23. http://dx.doi.org/10.1351/pac200375020317.

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Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative pathologies characterized by the formation in the central nervous system of the amyloid protein PrPSc, which derives from a cellular precursor called PrPc. Epidemiological and laboratory studies have shown that in species where the PrPc gene is polymorphic, the genotype composition is an important factor for the development of the disease. Identification of PrPSc allotypes accumulated in the brain during the disease proved valuable to investigate whether these polymorphisms are critical for the patho

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Saiki, Masatoshi, Yuji Hidaka, Masayuki Nara, and Hisayuki Morii. "Stem-Forming Regions That Are Essential for the Amyloidogenesis of Prion Proteins." Biochemistry 51, no. 8 (2012): 1566–76. http://dx.doi.org/10.1021/bi201688r.

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Tcherkasskaya, Olga, William Sanders, Veeradej Chynwat, Eugene A. Davidson, and Cindy S. Orser. "The Role of Hydrophobic Interactions in Amyloidogenesis: Example of Prion-Related Polypeptides." Journal of Biomolecular Structure and Dynamics 21, no. 3 (2003): 353–65. http://dx.doi.org/10.1080/07391102.2003.10506931.

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Berthelot, Karine, Sophie Lecomte, Julie Géan, Françoise Immel, and Christophe Cullin. "A Yeast Toxic Mutant of HET-s(218-289) Prion Displays Alternative Intermediates of Amyloidogenesis." Biophysical Journal 99, no. 4 (2010): 1239–46. http://dx.doi.org/10.1016/j.bpj.2010.06.015.

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Oroz, Javier, Sara S. Félix, Eurico J. Cabrita, and Douglas V. Laurents. "Structural transitions in Orb2 prion-like domain relevant for functional aggregation in memory consolidation." Journal of Biological Chemistry 295, no. 52 (2020): 18122–33. http://dx.doi.org/10.1074/jbc.ra120.015211.

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The recent structural elucidation of ex vivo Drosophila Orb2 fibrils revealed a novel amyloid formed by interdigitated Gln and His residue side chains belonging to the prion-like domain. However, atomic-level details on the conformational transitions associated with memory consolidation remain unknown. Here, we have characterized the nascent conformation and dynamics of the prion-like domain (PLD) of Orb2A using a nonconventional liquid-state NMR spectroscopy strategy based on 13C detection to afford an essentially complete set of 13Cα, 13Cβ, 1Hα, and backbone 13CO and 15N assignments. At pH 4

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Yamashita, Satoshi, Yuji O. Kamatari, Ryo Honda та ін. "Monomeric α-synuclein (αS) inhibits amyloidogenesis of human prion protein (hPrP) by forming a stable αS-hPrP hetero-dimer." Prion 15, № 1 (2021): 37–43. http://dx.doi.org/10.1080/19336896.2021.1910176.

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Kalmouni, Mona, Yujeong Oh, Wael Alata, and Mazin Magzoub. "Designed Cell-Penetrating Peptide Constructs for Inhibition of Pathogenic Protein Self-Assembly." Pharmaceutics 16, no. 11 (2024): 1443. http://dx.doi.org/10.3390/pharmaceutics16111443.

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Peptides possess a number of pharmacologically desirable properties, including greater chemical diversity than other biomolecule classes and the ability to selectively bind to specific targets with high potency, as well as biocompatibility, biodegradability, and ease and low cost of production. Consequently, there has been considerable interest in developing peptide-based therapeutics, including amyloid inhibitors. However, a major hindrance to the successful therapeutic application of peptides is their poor delivery to target tissues, cells or subcellular organelles. To overcome these issues,

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Paramasivam, Santhosh, Kavita Kundal, and Nandini Sarkar. "Human Serum Albumin Aggregation and its Modulation Using Nanoparticles: A Review." Protein & Peptide Letters 29, no. 1 (2022): 11–21. http://dx.doi.org/10.2174/0929866528666211125104600.

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: Amyloid fibrils are highly stable protein fibrillar aggregates believed to be involved in various neurodegenerative diseases, which include Alzheimer’s disease, Parkinson’s disease, and prion diseases. Inhibiting the aggregation process is a potential strategy to prevent diseases caused by amyloid formation. In this regard, nanoparticles have emerged as promising candidates owing to their unique physical/chemical properties of small size, large surface area, biocompatibility, biodegradability, non-toxicity, and ease of functionalization. Human Serum Albumin (HSA) is a soluble multidomain mon

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Dissertations / Theses on the topic "Prion amyloidogenesis"

1

Srivastava, Ankit. "Investigation on endogenous and synthetic modulators of prion amyloidogenesis." Thesis, 2017. http://localhost:8080/xmlui/handle/12345678/7428.

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Chai-Chi, Ho, and 何家齊. "Effects of Glycosylation and Phosphorylation on the Conformation and Amyloidogenesis of the Prion Protein." Thesis, 2004. http://ndltd.ncl.edu.tw/handle/75549986992499783731.

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碩士<br>國立清華大學<br>化學系<br>92<br>Prion disease is a neurodegenerative disorder. The prion formation, resulting from a structural conversion of the prion protein from the cellular form (PrPC) to the pathogenic isoform (PrPSc), is the culprit of the malady. A posttranslational process on the prion protein has been implicated in the prion formation during the development of prion disease. However, what the modification is and how the modification works remain elusive. It has been found that adding one single sugar on the prion peptide (sequence 108-144) can affect the structural conversion of the mod

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Book chapters on the topic "Prion amyloidogenesis"

1

Cardone, Franco, and Maurizio Pocchiari. "Amyloidogenesis in Transmissible Spongiform Encephalopathies." In Prions and Brain Diseases in Animals and Humans. Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1896-3_24.

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Jain Neha, Hammer Neal D., Wang Xuan, McGuffie Bryan A., and Chapman Matthew R. "Amyloid: Friend and Foe." In Advances in Alzheimer’s Disease. IOS Press, 2017. https://doi.org/10.3233/978-1-61499-706-1-297.

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Amyloidogenesis is the aggregation of soluble proteins into structurally conserved fibers. Amyloid fibers are distinguished by their resistance to proteinase K, tinctorial properties and &bgr;-sheet-rich secondary structure. Amyloid formation is a hallmark of many human diseases including Alzheimer's, Huntington's and the prion diseases. Therefore, understanding amyloidogenesis will provide insights into the development of therapeutics that target these debilitating diseases. A new class of &lsquo;functional&rsquo; amyloids promises a unique glimpse at how nature has harnessed the

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Baxa, Ulrich, Todd Cassese, Andrey V. Kajava, and Alasdair C. Steven. "Structure, Function, and Amyloidogenesis of Fungal Prions: Filament Polymorphism and Prion Variants." In Advances in Protein Chemistry. Elsevier, 2006. http://dx.doi.org/10.1016/s0065-3233(06)73005-4.

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