Relevant bibliographies by topics / Prion amyloidogenesis

Academic literature on the topic 'Prion amyloidogenesis'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Prion amyloidogenesis"

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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, and Ryo Honda. "α-Synuclein chaperone suppresses nucleation and amyloidogenesis of prion protein." Biochemical and Biophysical Research Communications 521, no. 1 (January 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, Carmine Mancone, S. Principe, M. A. Di Bari, P. Parchi, and M. Pocchiari. "Prion protein allotype profiling by mass spectrometry." Pure and Applied Chemistry 75, no. 2-3 (January 1, 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 pathological conversion. These analyses are complicated by the heterogeneity and the insolubility of the prion amyloid extracted from affected brains, which have been obviated by extensive digestion of extracted fractions and analysis of peptide fragment composition. We have developed an optimized protocol of liquid chromatography/mass spectrometry (LC/MS) that can reliably map PrP peptides in digested fractions with a low PrPSc/contaminants ratio. This approach has been successfully applied to the analysis of amyloidogenesis in experimentally infected PrP-heterozygous laboratory animals.
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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 (February 16, 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 (December 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 (August 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 (October 22, 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, where His residues are protonated, the PLD is disordered and flexible, except for a partially populated α-helix spanning residues 55–60, and binds RNA oligos, but not divalent cations. At pH 7, in contrast, His residues are predominantly neutral, and the Q/H segments adopt minor populations of helical structure, show decreased mobility and start to self-associate. At pH 7, the His residues do not bind RNA or Ca2+, but do bind Zn2+, which promotes further association. These findings represent a remarkable case of structural plasticity, based on which an updated model for Orb2A functional amyloidogenesis is suggested.
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Yamashita, Satoshi, Yuji O. Kamatari, Ryo Honda, Ayumi Niwa, Hiroyuki Tomiata, Akira Hara, and Kazuo Kuwata. "Monomeric α-synuclein (αS) inhibits amyloidogenesis of human prion protein (hPrP) by forming a stable αS-hPrP hetero-dimer." Prion 15, no. 1 (January 1, 2021): 37–43. http://dx.doi.org/10.1080/19336896.2021.1910176.

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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 (January 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 monomeric protein that interacts with various ligands and hormones, aiding in their transport, distribution, metabolism in the circulatory system, and also plays a vital role in extracellular fluid volume stabilization. Under certain in vitro conditions, HSA has been reported to undergo conformational changes leading to fibril formation and hence acts as a suitable model for studying amyloidogenesis. In this review, we have explored the effects of various nanoparticles on HSA aggregation and their mechanism of action. The study will throw light on the mechanistic details of nanoparticle-mediated amyloid modulation, which will help in the development of effective therapeutics against amyloidosis.
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Zhang, Wei, Minghui Zhang, Qin Wu, and Jingshan Shi. "Dendrobium nobile Lindl. Alkaloids Ameliorate Aβ25-35-Induced Synaptic Deficits by Targeting Wnt/β-Catenin Pathway in Alzheimer’s Disease Models." Journal of Alzheimer's Disease 86, no. 1 (March 8, 2022): 297–313. http://dx.doi.org/10.3233/jad-215433.

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Background: Dendrobium nobile Lindl. alkaloids (DNLA) are effective in ameliorating cognitive deficit in SAMP8, AβPP/PS1, and LPS-induced AD animal models, and prevented Aβ-induced synaptic degeneration in cultured hippocampal neurons. However, the underlying mechanisms remain unexplored. Objective: This study investigated the protective effects of DNLA on synaptic damage in an Aβ25-35-induced rat AD model, in primary cortical neuron cultures, and in PC12 cells transfected with human AβPP695, focusing on the Wnt/β-catenin pathway. Methods: Sprague-Dawley rats received a single Aβ25-35 injection (10μg) into the bilateral hippocampi. DNLA (40 and 80 mg/kg/d) was intragastrically administrated 7 days prior to Aβ injection and continued for 28 days. The spatial learning and memory, synaptic morphology, synapse-related proteins, and Wnt signaling components GSK3β and β-catenin phosphorylation were evaluated. Rat primary cortical neuron cultures and AβPP695-PC12 cells were used to evaluate axonal mitochondria distribution, reactive oxygen species production, amyloidogenesis, and Wnt pathway in the protection. Results: DNLA ameliorated Aβ-induced cognitive impairment, increased the number of synapses, elevated the postsynaptic density thickness and expression of synapsin and PSD95 in the hippocampus, and suppressed Aβ-mediated GSK3β activity and the β-catenin phosphorylation. In primary neurons and AβPP695-PC12 cells, DNLA restored Aβ25-35 induced mitochondrial dysfunction and inhibited reactive oxygen species production and amyloidogenesis. Furthermore, the Wnt/β-catenin pathway inhibitor Dkk-1 blocked the effect of DNLA on the expression of Aβ1-42 and PSD95. Conclusion: DNLA rescued Aβ-mediated synaptic and mitochondrial injury and inhibited amyloidogenesis in vivo and in vitro, probably through the activation of Wnt/β-catenin signaling pathway to protect synaptic integrity.
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Dissertations / Theses on the topic "Prion amyloidogenesis"

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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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Abstract:
碩士
國立清華大學
化學系
92
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 modified peptide and the following amyloid fibril formation. Interestingly, this effect is sugar-specific. Introducing an �娗-GalNAc to Ser-135 of the prion peptide could suppress the fibrillization while adding a �涀-GlcNAc did not yield the same effect. In order to understand the origin of the effect, we performed a series glycosylations with these two sugars and another two non-native isomers �涀-GalNAc, and �娗-GlcNAc and compared their effects on the fibrillization of the prion peptide. We found that the anomeric position is the origin of the inhibition. Either �娗-GalNAc or �娗-GlcNAc has more prominent effect on the conformational energy of the peptide and inhibits the assembly of the peptide to form amyloid. The NMR results showed that the region of Ser-135 and Arg-136 plays the critical point for amyloidogenesis. We also compared the influence of glycosylation and phosphorylation on fibrillization.
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Book chapters on the topic "Prion amyloidogenesis"

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Cardone, Franco, and Maurizio Pocchiari. "Amyloidogenesis in Transmissible Spongiform Encephalopathies." In Prions and Brain Diseases in Animals and Humans, 245–52. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1896-3_24.

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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, 125–80. Elsevier, 2006. http://dx.doi.org/10.1016/s0065-3233(06)73005-4.

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