Literatura académica sobre el tema "Prion amyloidogenesis"
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Artículos de revistas sobre el tema "Prion amyloidogenesis"
Kinoshita, Misaki, Yuxi Lin, Masatoshi Nakatsuji, Takashi Inui y Young-Ho Lee. "Kinetics and polymorphs of yeast prion Sup35NM amyloidogenesis". International Journal of Biological Macromolecules 102 (septiembre de 2017): 1241–49. http://dx.doi.org/10.1016/j.ijbiomac.2017.05.001.
Texto completoShirasaka, Maki, Kazuo Kuwata y Ryo Honda. "α-Synuclein chaperone suppresses nucleation and amyloidogenesis of prion protein". Biochemical and Biophysical Research Communications 521, n.º 1 (enero de 2020): 259–64. http://dx.doi.org/10.1016/j.bbrc.2019.10.120.
Texto completoSchininà, M. E., Bruno Maras, Franco Cardone, Carmine Mancone, S. Principe, M. A. Di Bari, P. Parchi y M. Pocchiari. "Prion protein allotype profiling by mass spectrometry". Pure and Applied Chemistry 75, n.º 2-3 (1 de enero de 2003): 317–23. http://dx.doi.org/10.1351/pac200375020317.
Texto completoSaiki, Masatoshi, Yuji Hidaka, Masayuki Nara y Hisayuki Morii. "Stem-Forming Regions That Are Essential for the Amyloidogenesis of Prion Proteins". Biochemistry 51, n.º 8 (16 de febrero de 2012): 1566–76. http://dx.doi.org/10.1021/bi201688r.
Texto completoTcherkasskaya, Olga, William Sanders, Veeradej Chynwat, Eugene A. Davidson y Cindy S. Orser. "The Role of Hydrophobic Interactions in Amyloidogenesis: Example of Prion-Related Polypeptides". Journal of Biomolecular Structure and Dynamics 21, n.º 3 (diciembre de 2003): 353–65. http://dx.doi.org/10.1080/07391102.2003.10506931.
Texto completoBerthelot, Karine, Sophie Lecomte, Julie Géan, Françoise Immel y Christophe Cullin. "A Yeast Toxic Mutant of HET-s(218-289) Prion Displays Alternative Intermediates of Amyloidogenesis". Biophysical Journal 99, n.º 4 (agosto de 2010): 1239–46. http://dx.doi.org/10.1016/j.bpj.2010.06.015.
Texto completoOroz, Javier, Sara S. Félix, Eurico J. Cabrita y Douglas V. Laurents. "Structural transitions in Orb2 prion-like domain relevant for functional aggregation in memory consolidation". Journal of Biological Chemistry 295, n.º 52 (22 de octubre de 2020): 18122–33. http://dx.doi.org/10.1074/jbc.ra120.015211.
Texto completoYamashita, Satoshi, Yuji O. Kamatari, Ryo Honda, Ayumi Niwa, Hiroyuki Tomiata, Akira Hara y Kazuo Kuwata. "Monomeric α-synuclein (αS) inhibits amyloidogenesis of human prion protein (hPrP) by forming a stable αS-hPrP hetero-dimer." Prion 15, n.º 1 (1 de enero de 2021): 37–43. http://dx.doi.org/10.1080/19336896.2021.1910176.
Texto completoParamasivam, Santhosh, Kavita Kundal y Nandini Sarkar. "Human Serum Albumin Aggregation and its Modulation Using Nanoparticles: A Review". Protein & Peptide Letters 29, n.º 1 (enero de 2022): 11–21. http://dx.doi.org/10.2174/0929866528666211125104600.
Texto completoZhang, Wei, Minghui Zhang, Qin Wu y 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, n.º 1 (8 de marzo de 2022): 297–313. http://dx.doi.org/10.3233/jad-215433.
Texto completoTesis sobre el tema "Prion amyloidogenesis"
Srivastava, Ankit. "Investigation on endogenous and synthetic modulators of prion amyloidogenesis". Thesis, 2017. http://localhost:8080/xmlui/handle/12345678/7428.
Texto completoChai-Chi, Ho y 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.
Texto completo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.
Capítulos de libros sobre el tema "Prion amyloidogenesis"
Cardone, Franco y Maurizio Pocchiari. "Amyloidogenesis in Transmissible Spongiform Encephalopathies". En 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.
Texto completoBaxa, Ulrich, Todd Cassese, Andrey V. Kajava y Alasdair C. Steven. "Structure, Function, and Amyloidogenesis of Fungal Prions: Filament Polymorphism and Prion Variants". En Advances in Protein Chemistry, 125–80. Elsevier, 2006. http://dx.doi.org/10.1016/s0065-3233(06)73005-4.
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