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Littérature scientifique sur le sujet « Antiamyloidogenic »

Auteur : Grafiati

Publié le 9 mars 2023

Mis à jour le 31 juillet 2025

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Articles de revues sur le sujet "Antiamyloidogenic"

Benseny-Cases, Núria, Oxana Klementieva, and Josep Cladera. "Dendrimers antiamyloidogenic potential in neurodegenerative diseases." New J. Chem. 36, no. 2 (2012): 211–16. http://dx.doi.org/10.1039/c1nj20469f.

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Chauhan, Ved, Lina Ji, and Abha Chauhan. "P1-442: Antiamyloidogenic properties of gelsolin." Alzheimer's & Dementia 4 (July 2008): T349. http://dx.doi.org/10.1016/j.jalz.2008.05.1024.

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Bermejo-Bescós, Paloma, Sagrario Martín-Aragón, Karim L. Jiménez-Aliaga, et al. "In vitro antiamyloidogenic properties of 1,4-naphthoquinones." Biochemical and Biophysical Research Communications 400, no. 1 (2010): 169–74. http://dx.doi.org/10.1016/j.bbrc.2010.08.038.

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Yu, Kun-Hua, and Cheng-I. Lee. "Quercetin Disaggregates Prion Fibrils and Decreases Fibril-Induced Cytotoxicity and Oxidative Stress." Pharmaceutics 12, no. 11 (2020): 1081. http://dx.doi.org/10.3390/pharmaceutics12111081.

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Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases caused by misfolding and aggregation of prion protein (PrP). Previous studies have demonstrated that quercetin can disaggregate some amyloid fibrils, such as amyloid β peptide (Aβ) and α-synuclein. However, the disaggregating ability is unclear in PrP fibrils. In this study, we examined the amyloid fibril-disaggregating activity of quercetin on mouse prion protein (moPrP) and characterized quercetin-bound moPrP fibrils by imaging, proteinase resistance, hemolysis assay, cell viability, and cellular oxidative

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Khaengkhan, Parinda, Yuki Nishikaze, Tetsuhiro Niidome, et al. "Identification of an antiamyloidogenic substance from mulberry leaves." NeuroReport 20, no. 13 (2009): 1214–18. http://dx.doi.org/10.1097/wnr.0b013e32832fa645.

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Benseny-Cases, Nuria, Oxana Klementieva, and Josep Cladera. "ChemInform Abstract: Dendrimers Antiamyloidogenic Potential in Neurodegenerative Diseases." ChemInform 43, no. 22 (2012): no. http://dx.doi.org/10.1002/chin.201222233.

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Pandini, Giuseppe, Vincenza Pace, Agata Copani, Sebastiano Squatrito, Danilo Milardi, and Riccardo Vigneri. "Insulin Has Multiple Antiamyloidogenic Effects on Human Neuronal Cells." Endocrinology 154, no. 1 (2013): 375–87. http://dx.doi.org/10.1210/en.2012-1661.

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Alzheimer’s disease is increased in diabetic patients. A defective insulin activity on the brain has been hypothesized to contribute to the neuronal cell dysregulation leading to AD, but the mechanism is not clear. We analyzed the effect of insulin on several molecular steps of amyloid precursor protein (APP) processing and β-amyloid (Aβ) intracellular accumulation in a panel of human neuronal cells and in human embryonic kidney 293 cells overexpressing APP-695. The data indicate that insulin, via its own receptor and the phosphatidylinositol-3-kinase/AKT pathway, influences APP phosphorylatio

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Fortin, Jessica S., and Marie-Odile Benoit-Biancamano. "Inhibition of islet amyloid polypeptide aggregation and associated cytotoxicity by nonsteroidal anti-inflammatory drugs." Canadian Journal of Physiology and Pharmacology 94, no. 1 (2016): 35–48. http://dx.doi.org/10.1139/cjpp-2015-0117.

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Nonsteroidal anti-inflammatory drugs (NSAIDs) constitute an important pharmacotherapeutic class that, over the past decade, have expanded in application to a panoply of medical conditions. They have been tested for neurodegenerative diseases such as Alzheimer’s to reduce inflammation and also in the attempt to abrogate amyloid deposition. However, the use of NSAIDs as aggregation inhibitors has not been extensively studied in pancreatic amyloid deposition. Pancreatic amyloidosis involves the misfolding of islet amyloid polypeptide (IAPP) and contributes to the progression of type-2 diabetes in

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Chemerovski-Glikman, Marina, Michal Richman та Shai Rahimipour. "Structure-based study of antiamyloidogenic cyclic d,l-α-peptides". Tetrahedron 70, № 42 (2014): 7639–44. http://dx.doi.org/10.1016/j.tet.2014.07.097.

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Zhao, Zijian, Ling Zhu, Haiyun Li та ін. "Antiamyloidogenic Activity of Aβ42-Binding Peptoid in Modulating Amyloid Oligomerization". Small 13, № 1 (2016): 1602857. http://dx.doi.org/10.1002/smll.201602857.

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Thèses sur le sujet "Antiamyloidogenic"

VISENTIN, CRISTINA. "Use of a technological platform to screening in vitro and in vivo anti-amyloidogenic drugs able to prevent early neurodegenerative process." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2017. http://hdl.handle.net/10281/158278.

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Amyloidoses are protein misfolding diseases caused by deposition of fibrillar proteins in target organs. Nowadays, most of them are still incurable and their relevance to public health system is growing, especially as a consequence of population aging. Spinocerebellar ataxia type 3 is a member of this group of pathologies and its causative agent is ataxin-3 (ATX3). This is consists of a globular N-terminal (JD), followed by a flexible tail carrying a poly-glutamine (polyQ) tract. An expanded polyQ tract triggers the aggregation. In this work, I have investigated the capability of tetracycline

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Chapitres de livres sur le sujet "Antiamyloidogenic"

"Antiamyloidogenic Effect of Dates Grown in Oman with Reference to Their Possible Protection against Alzheimer’s Disease." In Dates. CRC Press, 2012. http://dx.doi.org/10.1201/b11874-33.

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