Literatura académica sobre el tema "Amyloid Fibril Inhibition"
Crea una cita precisa en los estilos APA, MLA, Chicago, Harvard y otros
Consulte las listas temáticas de artículos, libros, tesis, actas de conferencias y otras fuentes académicas sobre el tema "Amyloid Fibril Inhibition".
Junto a cada fuente en la lista de referencias hay un botón "Agregar a la bibliografía". Pulsa este botón, y generaremos automáticamente la referencia bibliográfica para la obra elegida en el estilo de cita que necesites: APA, MLA, Harvard, Vancouver, Chicago, etc.
También puede descargar el texto completo de la publicación académica en formato pdf y leer en línea su resumen siempre que esté disponible en los metadatos.
Artículos de revistas sobre el tema "Amyloid Fibril Inhibition"
Šneideris, Tomas, Lina Baranauskienė, Jonathan G. Cannon, Rasa Rutkienė, Rolandas Meškys y Vytautas Smirnovas. "Looking for a generic inhibitor of amyloid-like fibril formation among flavone derivatives". PeerJ 3 (24 de septiembre de 2015): e1271. http://dx.doi.org/10.7717/peerj.1271.
Texto completoHOWLETT, David R., Amanda E. PERRY, Fiona GODFREY, Jane E. SWATTON, Kevin H. JENNINGS, Claus SPITZFADEN, Harry WADSWORTH, Stephen J. WOOD y Roger E. MARKWELL. "Inhibition of fibril formation in β-amyloid peptide by a novel series of benzofurans". Biochemical Journal 340, n.º 1 (10 de mayo de 1999): 283–89. http://dx.doi.org/10.1042/bj3400283.
Texto completoSaelices, Lorena, Kevin Chung, Ji H. Lee, Whitaker Cohn, Julian P. Whitelegge, Merrill D. Benson y David S. Eisenberg. "Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition". Proceedings of the National Academy of Sciences 115, n.º 29 (28 de junio de 2018): E6741—E6750. http://dx.doi.org/10.1073/pnas.1805131115.
Texto completoHasanbašić, Samra, Alma Jahić, Selma Berbić, Magda Tušek Žnidarič y Eva Žerovnik. "Inhibition of Protein Aggregation by Several Antioxidants". Oxidative Medicine and Cellular Longevity 2018 (2018): 1–12. http://dx.doi.org/10.1155/2018/8613209.
Texto completoSelig, Emily E., Courtney O. Zlatic, Dezerae Cox, Yee-Foong Mok, Paul R. Gooley, Heath Ecroyd y Michael D. W. Griffin. "N- and C-terminal regions of αB-crystallin and Hsp27 mediate inhibition of amyloid nucleation, fibril binding, and fibril disaggregation". Journal of Biological Chemistry 295, n.º 29 (16 de mayo de 2020): 9838–54. http://dx.doi.org/10.1074/jbc.ra120.012748.
Texto completoXun, Tianrong, Wenjuan Li, Jinquan Chen, Fei Yu, Wei Xu, Qian Wang, Ruizhe Yu et al. "ADS-J1 Inhibits Semen-Derived Amyloid Fibril Formation and Blocks Fibril-Mediated Enhancement of HIV-1 Infection". Antimicrobial Agents and Chemotherapy 59, n.º 9 (8 de junio de 2015): 5123–34. http://dx.doi.org/10.1128/aac.00385-15.
Texto completoAITKEN, Jacqueline F., Kerry M. LOOMES, Barbara KONARKOWSKA y Garth J. S. COOPER. "Suppression by polycyclic compounds of the conversion of human amylin into insoluble amyloid". Biochemical Journal 374, n.º 3 (15 de septiembre de 2003): 779–84. http://dx.doi.org/10.1042/bj20030422.
Texto completoOkumura, Hisashi y Satoru G. Itoh. "Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation". Molecules 27, n.º 8 (12 de abril de 2022): 2483. http://dx.doi.org/10.3390/molecules27082483.
Texto completoBhasikuttan, Achikanath C. y Jyotirmayee Mohanty. "Detection, inhibition and disintegration of amyloid fibrils: the role of optical probes and macrocyclic receptors". Chemical Communications 53, n.º 19 (2017): 2789–809. http://dx.doi.org/10.1039/c6cc08727b.
Texto completoSandhya A, Gomathi Kanayiram, Kiruthika L y Aafreen Afroz S. "Nigella Sativa : A Potential Inhibitor for Insulin Fibril Formation". International Journal of Research in Pharmaceutical Sciences 11, n.º 1 (23 de enero de 2020): 765–74. http://dx.doi.org/10.26452/ijrps.v11i1.1891.
Texto completoTesis sobre el tema "Amyloid Fibril Inhibition"
Young, Lydia Mary. "Defining the mechanism of small molecule inhibition of amyloid fibril formation using ion mobility spectrometry-mass spectrometry". Thesis, University of Leeds, 2015. http://etheses.whiterose.ac.uk/11887/.
Texto completoBoehringer, Régis. "Synthèse chimique de protéines pour l'étude structurale et fonctionnelle de fibres amyloïdes". Thesis, Strasbourg, 2018. http://www.theses.fr/2018STRAF001/document.
Texto completoAmyloid fibrils are associated with many human disorders including Alzheimer’s or Parkinson’s diseases. The formation of insoluble plaques is the result of protein misfolding and aggregation due to abnormal conformational isomerization of the involved protein. The structural and biological studies of amyloids are highly complex. In this thesis, we report on the development of different synthetic methodologies for the preparation of distinct amyloid fibril polymorphs as homogeneous samples for structural and biological studies. We also synthesized covalently-tethered oligomers composed of nine copies of an amyloidogenic peptide segment, where we were able to control the self-assembly of the structure by insertion of N-methylated amino-acids and to obtain monomeric oligomers mimicking a cross section of an amyloid fibril. We also report on the chiral recognition of L-peptides and L-proteins towards corresponding D-enantiomers during amyloid formation. Moreover, we studied various N-methylated peptide analogues to suppress amyloid growth. Overall, the results obtained in this thesis pave the way towards rational design of peptide-based inhibitors and diagnostics against amyloid propagation
Okada, Takuma. "Formation of toxic fibrils of Alzheimer's amyloid β-proteins mediated by GM1 ganglioside and its inhibition". 京都大学 (Kyoto University), 2008. http://hdl.handle.net/2433/137149.
Texto completoLunven, Laurent. "Synthèse et évaluation d'aurones sur des modèles de fibres de tau". Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAV007/document.
Texto completoThe fibrillation of the tau protein occurs in many neurodegenerative diseases, including Alzheimer’s disease, and leads to the formation of amyloid fibres called neurofibrillary tangles. Using organic molecules able to mark these fibres or inhibit their formation provides an interest both in diagnosis and therapy in Alzheimer’s disease. A series of aurones was synthesized and their ability to interfere with the fibrillation process was evaluated in vitro on models of tau fibres developed in this project. This work shows that polyhydroxylated aurones are able to act both as probes and as inhibitors of the fibrillation process. The ligation of these aurones with biomolecules or their radiolabelling has also been investigated
How, Su-Chun y 侯素君. "Inhibition of Amyloid Fibril Formation of Hen Egg White Lysozyme". Thesis, 2019. http://ndltd.ncl.edu.tw/handle/zeu3kb.
Texto completo國立臺灣大學
化學工程學研究所
107
Amyloid fibril formation serves as a key pathological feature of several different human degenerative diseases. Evidence suggests that mitigation/inhibition of amyloid fibril formation is considered a promising approach toward treating these diseases. However, as of now, there has been no effective small molecule available to cure amyloid diseases. The reasons why hen egg white lysozyme was used as the model protein in this research work are as follows: (1) hen egg white lysozyme is structurally homologous to human lysozyme, which is the protein associated with hereditary systemic amyloidosis, and (2) its fibrils were found to resemble the fibrillar species of human lysozyme. Investigation of amyloid fibril formation using hen egg white lysozyme can aid in a better understanding of the possible inhibition strategies for tackling amyloid aggregation. In our study, we used three kinds of small molecules including fast green FCF, methylene blue, and brilliant blue G. Both fast green FCF and brilliant blue G are triarylmethane dyes, fast green FCF is approved by the FDA as a food dye, while brilliant blue G has been shown to be safe with good blood–brain-barrier-permeability. Methylene blue, a compound belonging to the phenothiazinium family, has the potential to treat a variety of cancerous and non-cancerous diseases with low toxicity and minimal side effects. Furthermore, evidence demonstrates that methylene blue may be a promising molecules for the treatment of Alzheimer’s disease. Here, we examine the effects of fast green FCF, methylene blue and brilliant blue G on amyloid fibril formation derived from hen egg white lysozyme using a variety of spectroscopic techniques, such as intrinsic fluorescence, ANS fluorescence and ThT fluorescence assays, transmission electron microscopy, and circular dichroism spectroscopy. ThT fluorescence intensity results show that fast green FCF(25%) and brilliant blue G(32.8%) possess better inhibition efficacy than methylene blue (below 1:1.11,ThT intensity has no significant change). However, CD results reveal that fast green FCF and brilliant blue G affect hen egg white lysozyme differently. The addition of fast green FCF was observed to reduce the β-sheet secondary structure content associated with amyloid fibrillogenesis, which was not found in the case of brilliant blue G. Our results demonstrate that the addition of brilliant blue G is not able to suppress the amyloid fibril-forming propensity of lysozyme but only shorten the length of fibrillary species. Moreover, our SDS-PAGE results suggest that more native proteins are retained in the sample. In addition, our results further suggest that the observed inhibitory actions against amyloid fibril formation is mainly correlated with the interaction between the small molecules and protein hydrophobic sites. Given that both fast green FCF and brilliant blue G have sulfonate functional groups, the two molecules are able to electrostatically interact with the protein, thus further mitigating amyloid fibril formation. In addition, we surmise that the less negative charge and two additional methyl groups attached to the triphenylmethane structure might account for why the presence of brilliant blue G induces the formation of shorter fibrils, but can not suppress amyloid fibrillogenesis. Taken together, we conclude that small molecules’ inhibitory activity toward amyloid fibril formation is dependent upon the structure, size, and types of functional groups attached to them. We believe exploring the effects of small molecule on amyloid fibrillogenesis of lysozyme can contribute to the development of drugs for the treatment of amyloid diseases.
Actas de conferencias sobre el tema "Amyloid Fibril Inhibition"
Abioye, Raliat y Chibuike Udenigwe. "Inhibition of islet amyloid polypeptide fibril formation by natural polyphenols". En Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.601.
Texto completoAbioye, Raliat, Chibuike Udenigwe y Ogadimma Okagu. "Disaggregation of islet amyloid polypeptide fibrils as a potential anti-fibrillation mechanism of tetrapeptide TNGQ". En 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/szym9744.
Texto completoSoares, Izadora Fonseca Zaiden, João Nicoli Ferreira dos Santos y Lis Gomes Silva. "Dramatic cognitive improvement with acetylcholinesterase inhibitor in cerebral amyloid angiopathyrelated inflammation". En XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.578.
Texto completo