Artículos de revistas sobre el tema "Amyloid Fibril Inhibition"
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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 completoMeier, Juris J., Rakez Kayed, Chia-Yu Lin, Tatyana Gurlo, Leena Haataja, Sajith Jayasinghe, Ralf Langen, Charles G. Glabe y Peter C. Butler. "Inhibition of human IAPP fibril formation does not prevent β-cell death: evidence for distinct actions of oligomers and fibrils of human IAPP". American Journal of Physiology-Endocrinology and Metabolism 291, n.º 6 (diciembre de 2006): E1317—E1324. http://dx.doi.org/10.1152/ajpendo.00082.2006.
Texto completoXu, Sherry C. S., Josephine G. LoRicco, Anthony C. Bishop, Nathan A. James, Welby H. Huynh, Scott A. McCallum, Nadia R. Roan y George I. Makhatadze. "Sequence-independent recognition of the amyloid structural motif by GFP protein family". Proceedings of the National Academy of Sciences 117, n.º 36 (24 de agosto de 2020): 22122–27. http://dx.doi.org/10.1073/pnas.2001457117.
Texto completoPatil, Sharadrao M. y Andrei T. Alexandrescu. "Charge-Based Inhibitors of Amylin Fibrillization and Toxicity". Journal of Diabetes Research 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/946037.
Texto completoPepys, M. B. "Pathogenesis, diagnosis and treatment of systemic amyloidosis". Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 356, n.º 1406 (28 de febrero de 2001): 203–11. http://dx.doi.org/10.1098/rstb.2000.0766.
Texto completoGupta, Neha, Sameer Quazi, Saurabh Kumar Jha, Mohammad Khursheed Siddiqi, Kanika Verma, Swapnil Sharma, Rizwan Hassan Khan y Sameer Suresh Bhagyawant. "Chickpea Peptide: A Nutraceutical Molecule Corroborating Neurodegenerative and ACE-I Inhibition". Nutrients 14, n.º 22 (14 de noviembre de 2022): 4824. http://dx.doi.org/10.3390/nu14224824.
Texto completoHoepfner, Jeannine, Mandy Kleinsorge, Oliver Papp, Susanne Alfken, Robin Heiringhoff, Andreas Pich, Vanessa Sauer et al. "In vitro modelling of familial amyloidotic polyneuropathy allows quantitative detection of transthyretin amyloid fibril-like structures in hepatic derivatives of patient-specific induced pluripotent stem cells". Biological Chemistry 398, n.º 8 (26 de julio de 2017): 939–54. http://dx.doi.org/10.1515/hsz-2016-0258.
Texto completoPalmal, Sharbari, Amit Ranjan Maity, Brijesh Kumar Singh, Sreetama Basu, Nihar R. Jana y Nikhil R. Jana. "Inhibition of Amyloid Fibril Growth and Dissolution of Amyloid Fibrils by Curcumin-Gold Nanoparticles". Chemistry - A European Journal 20, n.º 20 (1 de abril de 2014): 6184–91. http://dx.doi.org/10.1002/chem.201400079.
Texto completoShvadchak, Volodymyr V., Kseniia Afitska y Dmytro A. Yushchenko. "Inhibition of α-Synuclein Amyloid Fibril Elongation by Blocking Fibril Ends". Angewandte Chemie 130, n.º 20 (16 de abril de 2018): 5792–96. http://dx.doi.org/10.1002/ange.201801071.
Texto completoShvadchak, Volodymyr V., Kseniia Afitska y Dmytro A. Yushchenko. "Inhibition of α-Synuclein Amyloid Fibril Elongation by Blocking Fibril Ends". Angewandte Chemie International Edition 57, n.º 20 (16 de abril de 2018): 5690–94. http://dx.doi.org/10.1002/anie.201801071.
Texto completoShvadchak, Volodymyr V., Kseniia Afitska, Anna Fucikova y Dmytro A. Yushchenko. "Inhibition of A-Synuclein Amyloid Fibril Elongation by Blocking Fibril Ends". Biophysical Journal 116, n.º 3 (febrero de 2019): 491a. http://dx.doi.org/10.1016/j.bpj.2018.11.2650.
Texto completoShinde, Meenakshi N., Nilotpal Barooah, Achikanath C. Bhasikuttan y Jyotirmayee Mohanty. "Inhibition and disintegration of insulin amyloid fibrils: a facile supramolecular strategy with p-sulfonatocalixarenes". Chemical Communications 52, n.º 14 (2016): 2992–95. http://dx.doi.org/10.1039/c5cc10159j.
Texto completoDoig, A. J., E. Hughes, R. M. Burke, T. J. Su, R. K. Heenan y J. Lu. "Inhibition of toxicity and protofibril formation in the amyloid-β peptide β(25–35) using N-Methylated derivatives". Biochemical Society Transactions 30, n.º 4 (1 de agosto de 2002): 537–42. http://dx.doi.org/10.1042/bst0300537.
Texto completoFolmert, Kristin, Malgorzata Broncel, Hans v. Berlepsch, Christopher Hans Ullrich, Mary-Ann Siegert y Beate Koksch. "Inhibition of peptide aggregation by means of enzymatic phosphorylation". Beilstein Journal of Organic Chemistry 12 (18 de noviembre de 2016): 2462–70. http://dx.doi.org/10.3762/bjoc.12.240.
Texto completoMichaels, Thomas C. T., Andela Šarić, Georg Meisl, Gabriella T. Heller, Samo Curk, Paolo Arosio, Sara Linse, Christopher M. Dobson, Michele Vendruscolo y Tuomas P. J. Knowles. "Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors". Proceedings of the National Academy of Sciences 117, n.º 39 (14 de septiembre de 2020): 24251–57. http://dx.doi.org/10.1073/pnas.2006684117.
Texto completoLiu, Yanqin, Michael Graetz, Lam Ho y Tara L. Pukala. "Ion Mobility—Mass Spectrometry-Based Screening for Inhibition of α-Synuclein Aggregation". European Journal of Mass Spectrometry 21, n.º 3 (junio de 2015): 255–64. http://dx.doi.org/10.1255/ejms.1359.
Texto completoJAIKARAN, Emma T. A. S., Melanie R. NILSSON y Anne CLARK. "Pancreatic beta-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation". Biochemical Journal 377, n.º 3 (1 de febrero de 2004): 709–16. http://dx.doi.org/10.1042/bj20030852.
Texto completoObasse, Idira, Mark Taylor, Nigel J. Fullwood y David Allsop. "Development of proteolytically stable N-methylated peptide inhibitors of aggregation of the amylin peptide implicated in type 2 diabetes". Interface Focus 7, n.º 6 (20 de octubre de 2017): 20160127. http://dx.doi.org/10.1098/rsfs.2016.0127.
Texto completoHassan, N., M. L. Cordero, R. Sierpe, M. Almada, J. Juárez, M. Valdez, A. Riveros et al. "Peptide functionalized magneto-plasmonic nanoparticles obtained by microfluidics for inhibition of β-amyloid aggregation". Journal of Materials Chemistry B 6, n.º 31 (2018): 5091–99. http://dx.doi.org/10.1039/c8tb00206a.
Texto completoKitagawa, Keisuke, Yohei Misumi, Mitsuharu Ueda, Yuya Hayashi, Masayoshi Tasaki, Konen Obayashi, Taro Yamashita, Hirofumi Jono, Hidetoshi Arima y Yukio Ando. "Inhibition of insulin amyloid fibril formation by cyclodextrins". Amyloid 22, n.º 3 (3 de julio de 2015): 181–86. http://dx.doi.org/10.3109/13506129.2015.1064818.
Texto completoMartins, Pedro M. "True and apparent inhibition of amyloid fibril formation". Prion 7, n.º 2 (marzo de 2013): 136–39. http://dx.doi.org/10.4161/pri.23111.
Texto completoGazit, Ehud. "Mechanisms of amyloid fibril self-assembly and inhibition". FEBS Journal 272, n.º 23 (10 de noviembre de 2005): 5971–78. http://dx.doi.org/10.1111/j.1742-4658.2005.05022.x.
Texto completoPappolla, M., P. Bozner, C. Soto, M. Zagorski, H. Shao, B. Frangione y J. Ghiso. "Inhibition of Alzheimer's Beta (Aβ) Amyloid Fibril Formation". Emerging Therapeutic Targets 1, n.º 1 (enero de 1997): 77–80. http://dx.doi.org/10.1517/14728222.1.1.77.
Texto completoScheidt, Tom, Urszula Łapińska, Janet R. Kumita, Daniel R. Whiten, David Klenerman, Mark R. Wilson, Samuel I. A. Cohen et al. "Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates". Science Advances 5, n.º 4 (abril de 2019): eaau3112. http://dx.doi.org/10.1126/sciadv.aau3112.
Texto completoSuzuki, Takanobu, Yukiko Hori, Taka Sawazaki, Yusuke Shimizu, Yu Nemoto, Atsuhiko Taniguchi, Shuta Ozawa, Youhei Sohma, Motomu Kanai y Taisuke Tomita. "Photo-oxygenation inhibits tau amyloid formation". Chemical Communications 55, n.º 44 (2019): 6165–68. http://dx.doi.org/10.1039/c9cc01728c.
Texto completoStańczykiewicz, Bartłomiej, Tomasz M. Goszczyński, Paweł Migdał, Marta Piksa, Krzysztof Pawlik, Jakub Gburek, Krzysztof Gołąb, Bogusława Konopska y Agnieszka Zabłocka. "Effect of Ovocystatin on Amyloid β 1-42 Aggregation—In Vitro Studies". International Journal of Molecular Sciences 24, n.º 6 (12 de marzo de 2023): 5433. http://dx.doi.org/10.3390/ijms24065433.
Texto completoTon, Van-Khue, Monica Mukherjee y Daniel P. Judge. "Transthyretin Cardiac Amyloidosis: Pathogenesis, Treatments, and Emerging Role in Heart Failure with Preserved Ejection Fraction". Clinical Medicine Insights: Cardiology 8s1 (enero de 2014): CMC.S15719. http://dx.doi.org/10.4137/cmc.s15719.
Texto completoKhatua, Deb Kumar y Mintu Halder. "Distinctively complete inhibition of fibrillation of serum albumins by methotrexate in vitro: experimental and modelling studies to understand the tuning of protein misfolding-related aggregations". New Journal of Chemistry 43, n.º 48 (2019): 18983–87. http://dx.doi.org/10.1039/c9nj05128g.
Texto completoBai, Cuiqin, Dongdong Lin, Yuxiang Mo, Jiangtao Lei, Yunxiang Sun, Luogang Xie, Xinju Yang y Guanghong Wei. "Influence of fullerenol on hIAPP aggregation: amyloid inhibition and mechanistic aspects". Physical Chemistry Chemical Physics 21, n.º 7 (2019): 4022–31. http://dx.doi.org/10.1039/c8cp07501h.
Texto completoHe, Lei, Xuesong Wang, Dengsen Zhu, Cong Zhao y Weihong Du. "Methionine oxidation of amyloid peptides by peroxovanadium complexes: inhibition of fibril formation through a distinct mechanism". Metallomics 7, n.º 12 (2015): 1562–72. http://dx.doi.org/10.1039/c5mt00133a.
Texto completoMorgan, Gareth J. "Barriers to Small Molecule Drug Discovery for Systemic Amyloidosis". Molecules 26, n.º 12 (11 de junio de 2021): 3571. http://dx.doi.org/10.3390/molecules26123571.
Texto completoAdsi, Hanaa, Shon A. Levkovich, Elvira Haimov, Topaz Kreiser, Massimiliano Meli, Hamutal Engel, Luba Simhaev et al. "Chemical Chaperones Modulate the Formation of Metabolite Assemblies". International Journal of Molecular Sciences 22, n.º 17 (25 de agosto de 2021): 9172. http://dx.doi.org/10.3390/ijms22179172.
Texto completoBan, Tadato, Masaru Hoshino, Satoshi Takahashi, Daizo Hamada, Kazuhiro Hasegawa, Hironobu Naiki y Yuji Goto. "Direct Observation of Aβ Amyloid Fibril Growth and Inhibition". Journal of Molecular Biology 344, n.º 3 (noviembre de 2004): 757–67. http://dx.doi.org/10.1016/j.jmb.2004.09.078.
Texto completoZhang, Wenjie, Andrew J. Christofferson, Quinn A. Besford, Joseph J. Richardson, Junling Guo, Yi Ju, Kristian Kempe, Irene Yarovsky y Frank Caruso. "Metal-dependent inhibition of amyloid fibril formation: synergistic effects of cobalt–tannic acid networks". Nanoscale 11, n.º 4 (2019): 1921–28. http://dx.doi.org/10.1039/c8nr09221d.
Texto completoTavanti, Francesco, Alfonso Pedone y Maria Cristina Menziani. "Insights into the Effect of Curcumin and (–)-Epigallocatechin-3-Gallate on the Aggregation of Aβ(1–40) Monomers by Means of Molecular Dynamics". International Journal of Molecular Sciences 21, n.º 15 (30 de julio de 2020): 5462. http://dx.doi.org/10.3390/ijms21155462.
Texto completoWang, Steven S. S., Ya-Ting Chen y Shang-Wei Chou. "Inhibition of amyloid fibril formation of β-amyloid peptides via the amphiphilic surfactants". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1741, n.º 3 (septiembre de 2005): 307–13. http://dx.doi.org/10.1016/j.bbadis.2005.05.004.
Texto completoSharafdini, Raziyeh y Hamid Mosaddeghi. "Inhibition of Insulin Amyloid Fibrillation by Salvianolic Acids and Calix[n]arenes: Molecular Docking Insight". Journal of Computational Biophysics and Chemistry 20, n.º 05 (agosto de 2021): 539–55. http://dx.doi.org/10.1142/s2737416521500332.
Texto completoZHANG, Bao-Hong, Guo-Sheng HU, Deng-Sen ZHU, Wen-Ji WANG, Ge-Hui GONG y Wei-Hong DU. "Inhibition of Prion Amyloid Peptide Fibril Formation by Peroxovanadium Complexes". Acta Physico-Chimica Sinica 32, n.º 7 (2016): 1810–18. http://dx.doi.org/10.3866/pku.whxb201604145.
Texto completoTodorova, Nevena, Levi Yeung, Andrew Hung y Irene Yarovsky. ""Janus" Cyclic Peptides: A New Approach to Amyloid Fibril Inhibition?" PLoS ONE 8, n.º 2 (20 de febrero de 2013): e57437. http://dx.doi.org/10.1371/journal.pone.0057437.
Texto completoOzawa, Daisaku, Kazuhiro Hasegawa, Young-Ho Lee, Kazumasa Sakurai, Kotaro Yanagi, Tadakazu Ookoshi, Yuji Goto y Hironobu Naiki. "Inhibition of β2-Microglobulin Amyloid Fibril Formation by α2-Macroglobulin". Journal of Biological Chemistry 286, n.º 11 (7 de enero de 2011): 9668–76. http://dx.doi.org/10.1074/jbc.m110.167965.
Texto completoCohen, Tomer, Anat Frydman-Marom, Meirav Rechter y Ehud Gazit. "Inhibition of Amyloid Fibril Formation and Cytotoxicity by Hydroxyindole Derivatives†". Biochemistry 45, n.º 15 (abril de 2006): 4727–35. http://dx.doi.org/10.1021/bi051525c.
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