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Journal articles on the topic 'Prion amyloidogenesis'

Author: Grafiati

Published: 6 September 2023

Last updated: 31 July 2025

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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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2

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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3

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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4

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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5

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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6

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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7

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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9

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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10

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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11

Zhang, Wei, Minghui Zhang, Qin Wu та 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, № 1 (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 injectio

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12

Sanders, Anna, C. Jeremy Craven, Lee D. Higgins, et al. "Cystatin forms a Tetramer through Structural Rearrangement of Domain-swapped Dimers prior to Amyloidogenesis." Journal of Molecular Biology 336, no. 1 (2004): 165–78. http://dx.doi.org/10.1016/j.jmb.2003.12.011.

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13

Galkin, Alexey P., and Evgeniy I. Sysoev. "Stress Response Is the Main Trigger of Sporadic Amyloidoses." International Journal of Molecular Sciences 22, no. 8 (2021): 4092. http://dx.doi.org/10.3390/ijms22084092.

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Amyloidoses are a group of diseases associated with the formation of pathological protein fibrils with cross-β structures. Approximately 5–10% of the cases of these diseases are determined by amyloidogenic mutations, as well as by transmission of infectious amyloids (prions) between organisms. The most common group of so-called sporadic amyloidoses is associated with abnormal aggregation of wild-type proteins. Some sporadic amyloidoses are known to be induced only against the background of certain pathologies, but in some cases the cause of amyloidosis is unclear. It is assumed that these dise

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14

Vashist, Shilpa, Mimi Cushman, and James Shorter. "Applying Hsp104 to protein-misfolding disordersThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 1 (2010): 1–13. http://dx.doi.org/10.1139/o09-121.

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Hsp104, a hexameric AAA+ ATPase found in yeast, transduces energy from cycles of ATP binding and hydrolysis to resolve disordered protein aggregates and cross-β amyloid conformers. These disaggregation activities are often co-ordinated by the Hsp70 chaperone system and confer considerable selective advantages. First, renaturation of aggregated conformers by Hsp104 is critical for yeast survival after various environmental stresses. Second, amyloid remodeling by Hsp104 enables yeast to exploit multifarious prions as a reservoir of beneficial and heritable phenotypic variation. Curiously, althou

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15

Huang, Alexis S., Benjamin C. K. Tong, Aston J. Wu, et al. "Rectifying Attenuated Store-Operated Calcium Entry as a Therapeutic Approach for Alzheimer’s Disease." Current Alzheimer Research 17, no. 12 (2021): 1072–87. http://dx.doi.org/10.2174/1567205018666210119150613.

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: Alzheimer’s disease (AD) is the most common neurodegenerative disorder. Although the pathological hallmarks of AD have been identified, the derived therapies cannot effectively slow down or stop disease progression; hence, it is likely that other pathogenic mechanisms are involved in AD pathogenesis. Intracellular calcium (Ca2+) dyshomeostasis has been consistently observed in AD patients and numerous AD models and may emerge prior to the development of amyloid plaques and neurofibrillary tangles. Thus, intracellular Ca2+ disruptions are believed to play an important role in AD development a

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16

Dookhy, Joshi, Cathy McHale, Sean Kennelly, et al. "127 Modifiable Cardiovascular Risk Profile in People with Mild Cognitive Symptoms Attending a Memory Service - an Opportunity to Promote Brain Health." Age and Ageing 48, Supplement_3 (2019): iii17—iii65. http://dx.doi.org/10.1093/ageing/afz103.75.

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Abstract Background Current evidence strongly implicates the burden of vascular risk factors (VRF) in the development of stroke, cognitive decline and dementia. This effect is mediated through several mechanisms, including amyloidogenesis, chronic neuroinflamation, cerebral perfusion and white-matter changes. Vascular risk profiling is well-embedded in stroke and cardiac services, but less so in memory services. Methods A review of established modifiable VRF (hypercholesterolemia, Body Mass Index (BMI), hypertension, HbA1c, smoking and alcohol habits) of people with mild cognitive complaints (

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17

Stępkowski, Dariusz, and Juliusz Bieniaś. "Nature of cross-seeding barriers of amyloidogenesis." Acta Biochimica Polonica 59, no. 2 (2012). http://dx.doi.org/10.18388/abp.2012_2156.

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The epidemics of bovine spongiform encephalopathy (BSE) several decades ago and present epidemics of chronic wasting disease (CWD) among cervids posed a threat of cross-species infections to humans or other animals. Therefore, the question as to the molecular nature of the species barriers to transmissibility of prion diseases is very important. We approached this problem theoretically, first developing a model of template-monomer interaction based on logical and topological grounds and on experimental data about cross-seeding of PrP 23-144 protein orthologs. Further, we propose that the stren

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18

Schininà, M. E., Bruno Maras, Franco Cardone, et al. "Prion protein allotype profiling by mass spectrometry." October 13, 2007. https://doi.org/10.1351/pac200375020317.

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Abstract 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

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19

Yoon, Soljee, Hye Yun Kim, Sohui Park, et al. "Drug Discovery and Screening Tool Development for Tauopathies by Focusing on Pathogenic Tau Repeat 3 Oligomers." Angewandte Chemie International Edition, September 24, 2024. http://dx.doi.org/10.1002/anie.202411942.

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Comprehending early amyloidogenesis is essential for the development of effective therapeutic strategies. In tauopathies like Alzheimer’s disease (AD), the abnormal accumulation of tau protein is initiated by pathological tau seeds. Mounting evidence implies that the microtubule binding domain, consisting of three to four repeats, plays a pivotal role in this process, yet the exact region driving the formation of pathogenic species needs to be further scrutinized. Here, we chemically synthesized individual tau repeats to identify those exhibiting pathogenic prion‐like characteristics. Notably,

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20

Yoon, Soljee, Hye Yun Kim, Sohui Park, et al. "Drug Discovery and Screening Tool Development for Tauopathies by Focusing on Pathogenic Tau Repeat 3 Oligomers." Angewandte Chemie, September 24, 2024. http://dx.doi.org/10.1002/ange.202411942.

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Comprehending early amyloidogenesis is essential for the development of effective therapeutic strategies. In tauopathies like Alzheimer’s disease (AD), the abnormal accumulation of tau protein is initiated by pathological tau seeds. Mounting evidence implies that the microtubule binding domain, consisting of three to four repeats, plays a pivotal role in this process, yet the exact region driving the formation of pathogenic species needs to be further scrutinized. Here, we chemically synthesized individual tau repeats to identify those exhibiting pathogenic prion‐like characteristics. Notably,

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21

Revilla-García, Aida, Cristina Fernández, María Moreno-del Álamo, Vivian de los Ríos, Ina M. Vorberg, and Rafael Giraldo. "Intercellular Transmission of a Synthetic Bacterial Cytotoxic Prion-Like Protein in Mammalian Cells." mBio 11, no. 2 (2020). http://dx.doi.org/10.1128/mbio.02937-19.

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ABSTRACT RepA is a bacterial protein that builds intracellular amyloid oligomers acting as inhibitory complexes of plasmid DNA replication. When carrying a mutation enhancing its amyloidogenesis (A31V), the N-terminal domain (WH1) generates cytosolic amyloid particles that are inheritable within a bacterial lineage. Such amyloids trigger in bacteria a lethal cascade reminiscent of mitochondrial impairment in human cells affected by neurodegeneration. To fulfill all the criteria to qualify as a prion-like protein, horizontal (intercellular) transmissibility remains to be demonstrated for RepA-W

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22

Bencs, Fruzsina, Loránd Románszki, Viktor Farkas, and András Perczel. "Structural Insights into Amyloid Polymorphism: The Impact of Glutamine to Norleucine Substitutions in GNNQQNY Aggregation." Chemistry – A European Journal, March 28, 2025. https://doi.org/10.1002/chem.202404255.

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Polypeptides can self‐assemble into highly organized amyloid structures through complex and poorly understood mechanisms. To better understand the key parameters governing amyloidogenesis, we investigated the aggregation of the Sup35 prion‐derived GNNQQNY sequence alongside two rationally designed mutants, glutamine to norleucine in position 4th or 5th, where selective removal of hydrogen bonding capacity reduces amyloid structural stability. Our findings reveal that β‐sheet arrays form rapidly as an initial step, followed by π‐π aromatic interactions between Tyr residues, which drive hierarch

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23

Bengoa-Vergniory, Nora, Elisavet Velentza-Almpani, Ana Maria Silva, et al. "Tau-proximity ligation assay reveals extensive previously undetected pathology prior to neurofibrillary tangles in preclinical Alzheimer’s disease." Acta Neuropathologica Communications 9, no. 1 (2021). http://dx.doi.org/10.1186/s40478-020-01117-y.

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Abstract Background Multimerization is a key process in prion-like disorders such as Alzheimer’s disease (AD), since it is a requirement for self-templating tau and beta-amyloid amyloidogenesis. AT8-immunohistochemistry for hyperphosphorylated tau is currently used for the diagnosis and staging of tau pathology. Given that tau–tau interactions can occur in the absence of hyperphosphorylation or other post-translational modifications (PTMs), the direct visualization of tau multimerization could uncover early pathological tau multimers. Methods Here, we used bimolecular fluorescent complementati

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24

Prosswimmer, Tatum, та Valerie Daggett. "The role of α-sheet structure in amyloidogenesis: characterization and implications". Open Biology 12, № 11 (2022). http://dx.doi.org/10.1098/rsob.220261.

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Amyloid diseases are linked to protein misfolding whereby the amyloidogenic protein undergoes a conformational change, aggregates and eventually forms amyloid fibrils. While the amyloid fibrils and plaques are hallmarks of these diseases, they typically form late in the disease process and do not correlate with disease. Instead, there is growing evidence that smaller, soluble toxic oligomers form prior and appear to be early triggers of the molecular pathology underlying these diseases. Nearly 20 years ago, we proposed the α-sheet hypothesis after discovering that the early conformational chan

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25

McMackin, Patrick, Joe Adam, Shannon Griffin, and Amir Hirsa. "Amyloidogenesis via interfacial shear in a containerless biochemical reactor aboard the International Space Station." npj Microgravity 8, no. 1 (2022). http://dx.doi.org/10.1038/s41526-022-00227-2.

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AbstractFluid interfaces significantly influence the dynamics of protein solutions, effects that can be isolated by performing experiments in microgravity, greatly reducing the amount of solid boundaries present, allowing air-liquid interfaces to become dominant. This investigation examined the effects of protein concentration on interfacial shear-induced fibrillization of insulin in microgravity within a containerless biochemical reactor, the ring-sheared drop (RSD), aboard the international space station (ISS). Human insulin was used as a model amyloidogenic protein for studying protein kine

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26

Orlowski, Alex, Joseph Karippaparambil, Jean-Michel Paumier, et al. "Axonal organelle buildup from loss of AP-4 complex function causes exacerbation of amyloid plaque pathology and gliosis in Alzheimer’s disease mouse model." eneuro, December 4, 2024, ENEURO.0445–24.2024. https://doi.org/10.1523/eneuro.0445-24.2024.

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Lysosomes and related precursor organelles robustly build up in swollen axons that surround amyloid plaques and disrupted axonal lysosome transport has been implicated in worsening Alzheimer’s pathology. Our prior studies have revealed that loss of Adaptor protein-4 (AP-4) complex function, linked primarily to Spastic Paraplegia (HSP), leads to a similar build of lysosomes in structures we term “AP-4 dystrophies”. Surprisingly, these AP-4 dystrophies were also characterized by enrichment of components of APP processing machinery, β-site cleaving enzyme 1 (BACE1) and Presenilin 2. Our studies e

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27

van Hulst, KL, C. Oosterwijk, W. Born, et al. "Islet amyloid polypeptide/amylin messenger RNA and protein expression in human insulinomas in relation to amyloid formation." European Journal of Endocrinology, January 1, 1999, 69–78. http://dx.doi.org/10.1530/eje.0.1400069.

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OBJECTIVE: Islet amyloid polypeptide (IAPP), also named amylin, is the predominant protein component of amyloid deposits in human islet beta cell tumours of the pancreas (insulinomas). IAPP is co-produced with insulin by islet beta cells. We investigated IAPP expression in relation to insulin expression and to amyloid formation in eleven insulinomas. DESIGN AND METHODS: RNA and protein extracts were prepared from the same pieces of tumour tissue, and from specimens of two normal human pancreata. IAPP and insulin mRNA and peptide content were quantified using Northern blot analysis and radioimm

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28

Takashio, S., M. Morioka, A. Fujiyama, et al. "Clinical characteristics, patient selection and clinical outcomes of tafamidis treatment in transthyretin amyloidosis cardiomyopathy." European Heart Journal 43, Supplement_2 (2022). http://dx.doi.org/10.1093/eurheartj/ehac544.964.

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Abstract Background Tafamidis is a stabilizer of transthyretin, specifically designed to decrease or prevent amyloidogenesis, and improves prognosis in patients with transthyretin amyloid cardiomyopathy (ATTR-CM). However, clinical coarse, selection of appropriate patients and monitoring therapeutic effect of tafamidis remained unclear. Purpose The aim of this study was to clarify the patients' characteristics, clinical coarse, and clinical outcomes of tafamidis in patients with ATTR-CM and to evaluate prognostic factors and changes in clinical data over time. Methods We evaluated consecutive

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