Artículos de revistas sobre el tema "Α-synuclein aggregation"
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Surguchov, Andrei y Alexei Surguchev. "Synucleins: New Data on Misfolding, Aggregation and Role in Diseases". Biomedicines 10, n.º 12 (13 de diciembre de 2022): 3241. http://dx.doi.org/10.3390/biomedicines10123241.
Texto completoHam, Sangwoo, Seung Pil Yun, Hyojung Kim, Donghoon Kim, Bo Am Seo, Heejeong Kim, Jeong-Yong Shin et al. "Amyloid-like oligomerization of AIMP2 contributes to α-synuclein interaction and Lewy-like inclusion". Science Translational Medicine 12, n.º 569 (11 de noviembre de 2020): eaax0091. http://dx.doi.org/10.1126/scitranslmed.aax0091.
Texto completoGalvagnion, Céline, James W. P. Brown, Myriam M. Ouberai, Patrick Flagmeier, Michele Vendruscolo, Alexander K. Buell, Emma Sparr y Christopher M. Dobson. "Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein". Proceedings of the National Academy of Sciences 113, n.º 26 (13 de junio de 2016): 7065–70. http://dx.doi.org/10.1073/pnas.1601899113.
Texto completoHashimoto, Makoto, Edward Rockenstein, Michael Mante, Margaret Mallory y Eliezer Masliah. "β-Synuclein Inhibits α-Synuclein Aggregation". Neuron 32, n.º 2 (octubre de 2001): 213–23. http://dx.doi.org/10.1016/s0896-6273(01)00462-7.
Texto completoANDREKOPOULOS, Christopher, Hao ZHANG, Joy JOSEPH, Shasi KALIVENDI y B. KALYANARAMAN. "Bicarbonate enhances alpha-synuclein oligomerization and nitration: intermediacy of carbonate radical anion and nitrogen dioxide radical". Biochemical Journal 378, n.º 2 (1 de marzo de 2004): 435–47. http://dx.doi.org/10.1042/bj20031466.
Texto completoRott, Ruth, Raymonde Szargel, Vered Shani, Haya Hamza, Mor Savyon, Fatimah Abd Elghani, Rina Bandopadhyay y Simone Engelender. "SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation". Proceedings of the National Academy of Sciences 114, n.º 50 (27 de noviembre de 2017): 13176–81. http://dx.doi.org/10.1073/pnas.1704351114.
Texto completoEstaun-Panzano, Juan, Marie-Laure Arotcarena y Erwan Bezard. "Monitoring α-synuclein aggregation". Neurobiology of Disease 176 (enero de 2023): 105966. http://dx.doi.org/10.1016/j.nbd.2022.105966.
Texto completoCaló, Laura, Eric Hidari, Michal Wegrzynowicz, Jeffrey W. Dalley, Bernard L. Schneider, Martyna Podgajna, Oleg Anichtchik, Emma Carlson, David Klenerman y Maria Grazia Spillantini. "CSPα reduces aggregates and rescues striatal dopamine release in α-synuclein transgenic mice". Brain 144, n.º 6 (24 de marzo de 2021): 1661–69. http://dx.doi.org/10.1093/brain/awab076.
Texto completoJENSEN, Poul H., Peter HØJRUP, Henrik HAGER, Morten S. NIELSEN, Linda JACOBSEN, Ole F. OLESEN, Jørgen GLIEMANN y Ross JAKES. "Binding of Aβ to α- and β-synucleins: identification of segments in α-synuclein/NAC precursor that bind Aβ and NAC". Biochemical Journal 323, n.º 2 (15 de abril de 1997): 539–46. http://dx.doi.org/10.1042/bj3230539.
Texto completoKrumova, Petranka, Erik Meulmeester, Manuel Garrido, Marilyn Tirard, He-Hsuan Hsiao, Guillaume Bossis, Henning Urlaub et al. "Sumoylation inhibits α-synuclein aggregation and toxicity". Journal of Cell Biology 194, n.º 1 (11 de julio de 2011): 49–60. http://dx.doi.org/10.1083/jcb.201010117.
Texto completoTaguchi, Yumiko V., Erica L. Gorenberg, Maria Nagy, Drake Thrasher, Wayne A. Fenton, Laura Volpicelli-Daley, Arthur L. Horwich y Sreeganga S. Chandra. "Hsp110 mitigates α-synuclein pathology in vivo". Proceedings of the National Academy of Sciences 116, n.º 48 (4 de noviembre de 2019): 24310–16. http://dx.doi.org/10.1073/pnas.1903268116.
Texto completoChia, Sean, Patrick Flagmeier, Johnny Habchi, Veronica Lattanzi, Sara Linse, Christopher M. Dobson, Tuomas P. J. Knowles y Michele Vendruscolo. "Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates". Proceedings of the National Academy of Sciences 114, n.º 30 (11 de julio de 2017): 8005–10. http://dx.doi.org/10.1073/pnas.1700239114.
Texto completoLoureiro, Joana Angélica, Stéphanie Andrade, Lies Goderis, Ruben Gomez-Gutierrez, Claudio Soto, Rodrigo Morales y Maria Carmo Pereira. "(De)stabilization of Alpha-Synuclein Fibrillary Aggregation by Charged and Uncharged Surfactants". International Journal of Molecular Sciences 22, n.º 22 (19 de noviembre de 2021): 12509. http://dx.doi.org/10.3390/ijms222212509.
Texto completoShan, Frank Y., Kar-Ming Fung, Tarek Zieneldien, Janice Kim, Chuanhai Cao y Jason H. Huang. "Examining the Toxicity of α-Synuclein in Neurodegenerative Disorders". Life 11, n.º 11 (22 de octubre de 2021): 1126. http://dx.doi.org/10.3390/life11111126.
Texto completoVajhøj, Charlotte, Benjamin Schmid, Ania Alik, Ronald Melki, Karina Fog, Bjørn Holst y Tina Charlotte Stummann. "Establishment of a human induced pluripotent stem cell neuronal model for identification of modulators of A53T α-synuclein levels and aggregation". PLOS ONE 16, n.º 12 (21 de diciembre de 2021): e0261536. http://dx.doi.org/10.1371/journal.pone.0261536.
Texto completoKoopman, Herjan, Simon Jackson, Oleg Anichtchik y Camille Carroll. "LPS INDUCES AGGREGATION OF α-SYNUCLEIN IN MONOCYTES". Journal of Neurology, Neurosurgery & Psychiatry 86, n.º 11 (14 de octubre de 2015): e4.188-e4. http://dx.doi.org/10.1136/jnnp-2015-312379.93.
Texto completoIkeda, Aya, Kenya Nishioka, Hongrui Meng, Masashi Takanashi, Iwao Hasegawa, Tsuyoshi Inoshita, Kahori Shiba-Fukushima et al. "Mutations in CHCHD2 cause α-synuclein aggregation". Human Molecular Genetics 28, n.º 23 (10 de octubre de 2019): 3895–911. http://dx.doi.org/10.1093/hmg/ddz241.
Texto completoGuo, Min, Jian Wang, Yanxin Zhao, Yiwei Feng, Sida Han, Qiang Dong, Mei Cui y Kim Tieu. "Microglial exosomes facilitate α-synuclein transmission in Parkinson’s disease". Brain 143, n.º 5 (1 de mayo de 2020): 1476–97. http://dx.doi.org/10.1093/brain/awaa090.
Texto completoGaspar, Ricardo, Georg Meisl, Alexander K. Buell, Laurence Young, Clemens F. Kaminski, Tuomas P. J. Knowles, Emma Sparr y Sara Linse. "Acceleration of α-synuclein aggregation". Amyloid 24, sup1 (16 de marzo de 2017): 20–21. http://dx.doi.org/10.1080/13506129.2017.1292904.
Texto completoGiehm, Lise, Nikolai Lorenzen y Daniel E. Otzen. "Assays for α-synuclein aggregation". Methods 53, n.º 3 (marzo de 2011): 295–305. http://dx.doi.org/10.1016/j.ymeth.2010.12.008.
Texto completoChen, Merry, Julie Vincent, Alexis Ezeanii, Saurabh Wakade, Shobha Yerigenahally y Danielle E. Mor. "Heparan sulfate proteoglycans mediate prion-like α-synuclein toxicity in Parkinson’s in vivo models". Life Science Alliance 5, n.º 11 (5 de julio de 2022): e202201366. http://dx.doi.org/10.26508/lsa.202201366.
Texto completode Boni, Laura, Aurelia Hays Watson, Ludovica Zaccagnini, Amber Wallis, Kristina Zhelcheska, Nora Kim, John Sanderson et al. "Brain region-specific susceptibility of Lewy body pathology in synucleinopathies is governed by α-synuclein conformations". Acta Neuropathologica 143, n.º 4 (9 de febrero de 2022): 453–69. http://dx.doi.org/10.1007/s00401-022-02406-7.
Texto completoMurvai, Nikoletta, Gabriella Gellen, András Micsonai, Gitta Schlosser y József Kardos. "Cross-Linked α-Synuclein as Inhibitor of Amyloid Formation". International Journal of Molecular Sciences 24, n.º 17 (29 de agosto de 2023): 13403. http://dx.doi.org/10.3390/ijms241713403.
Texto completoWen, Tianzhi, Jian Chen, Wenqian Zhang y Jiyan Pang. "Design, Synthesis and Biological Evaluation of α-Synuclein Proteolysis-Targeting Chimeras". Molecules 28, n.º 11 (31 de mayo de 2023): 4458. http://dx.doi.org/10.3390/molecules28114458.
Texto completoLevine, Paul M., Ana Galesic, Aaron T. Balana, Anne-Laure Mahul-Mellier, Mariana X. Navarro, Cesar A. De Leon, Hilal A. Lashuel y Matthew R. Pratt. "α-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson’s disease". Proceedings of the National Academy of Sciences 116, n.º 5 (16 de enero de 2019): 1511–19. http://dx.doi.org/10.1073/pnas.1808845116.
Texto completoWon, Seok Joon, Rebecca Fong, Nicholas Butler, Jennifer Sanchez, Yiguan Zhang, Candance Wong, Olive Tambou Nzoutchoum, Annie Huynh, June Pan y Raymond A. Swanson. "Neuronal Oxidative Stress Promotes α-Synuclein Aggregation In Vivo". Antioxidants 11, n.º 12 (15 de diciembre de 2022): 2466. http://dx.doi.org/10.3390/antiox11122466.
Texto completoPujols, Jordi, Samuel Peña-Díaz, Diana F. Lázaro, Francesca Peccati, Francisca Pinheiro, Danilo González, Anita Carija et al. "Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons". Proceedings of the National Academy of Sciences 115, n.º 41 (24 de septiembre de 2018): 10481–86. http://dx.doi.org/10.1073/pnas.1804198115.
Texto completoMorgan, Sophie A., Isabelle Lavenir, Juan Fan, Masami Masuda-Suzukake, Daniela Passarella, Michael A. DeTure, Dennis W. Dickson, Bernardino Ghetti y Michel Goedert. "α-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species". Journal of Biological Chemistry 295, n.º 19 (24 de marzo de 2020): 6652–64. http://dx.doi.org/10.1074/jbc.ra119.012179.
Texto completoHartlage-Rübsamen, Maike, Alexandra Bluhm, Sandra Moceri, Lisa Machner, Janett Köppen, Mathias Schenk, Isabel Hilbrich et al. "A glutaminyl cyclase-catalyzed α-synuclein modification identified in human synucleinopathies". Acta Neuropathologica 142, n.º 3 (26 de julio de 2021): 399–421. http://dx.doi.org/10.1007/s00401-021-02349-5.
Texto completoPerni, Michele, Céline Galvagnion, Alexander Maltsev, Georg Meisl, Martin B. D. Müller, Pavan K. Challa, Julius B. Kirkegaard et al. "A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity". Proceedings of the National Academy of Sciences 114, n.º 6 (17 de enero de 2017): E1009—E1017. http://dx.doi.org/10.1073/pnas.1610586114.
Texto completoEl-Agnaf, Omar M. A. y G. Brent Irvine. "Aggregation and properties of α‒synuclein and related proteins". Spectroscopy 15, n.º 3,4 (2001): 141–50. http://dx.doi.org/10.1155/2001/939274.
Texto completoPalazzi, Luana, Benedetta Fongaro, Manuela Leri, Laura Acquasaliente, Massimo Stefani, Monica Bucciantini y Patrizia Polverino de Laureto. "Structural Features and Toxicity of α-Synuclein Oligomers Grown in the Presence of DOPAC". International Journal of Molecular Sciences 22, n.º 11 (2 de junio de 2021): 6008. http://dx.doi.org/10.3390/ijms22116008.
Texto completoHlushchuk, Irena, Justyna Barut, Mikko Airavaara, Kelvin Luk, Andrii Domanskyi y Piotr Chmielarz. "Cell Culture Media, Unlike the Presence of Insulin, Affect α-Synuclein Aggregation in Dopaminergic Neurons". Biomolecules 12, n.º 4 (9 de abril de 2022): 563. http://dx.doi.org/10.3390/biom12040563.
Texto completoToleikis, Zigmantas, Mantas Ziaunys, Lina Baranauskiene, Vytautas Petrauskas, Kristaps Jaudzems y Vytautas Smirnovas. "S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation". International Journal of Molecular Sciences 22, n.º 15 (26 de julio de 2021): 7972. http://dx.doi.org/10.3390/ijms22157972.
Texto completoBluhm, Alexandra, Sarah Schrempel, Stephan von von Hörsten, Anja Schulze y Steffen Roßner. "Proteolytic α-Synuclein Cleavage in Health and Disease". International Journal of Molecular Sciences 22, n.º 11 (21 de mayo de 2021): 5450. http://dx.doi.org/10.3390/ijms22115450.
Texto completoAntonschmidt, Leif, Rıza Dervişoğlu, Vrinda Sant, Kumar Tekwani Movellan, Ingo Mey, Dietmar Riedel, Claudia Steinem, Stefan Becker, Loren B. Andreas y Christian Griesinger. "Insights into the molecular mechanism of amyloid filament formation: Segmental folding of α-synuclein on lipid membranes". Science Advances 7, n.º 20 (mayo de 2021): eabg2174. http://dx.doi.org/10.1126/sciadv.abg2174.
Texto completoMa, Qiu-Lan, Piu Chan, Mitsunobu Yoshii y Kenji Uéda. "α-Synuclein aggregation and neurodegenerative diseases". Journal of Alzheimer's Disease 5, n.º 2 (22 de abril de 2003): 139–48. http://dx.doi.org/10.3233/jad-2003-5208.
Texto completoCrunkhorn, Sarah. "Rescuing α-synuclein aggregation in PD". Nature Reviews Drug Discovery 21, n.º 1 (2 de diciembre de 2021): 20. http://dx.doi.org/10.1038/d41573-021-00201-9.
Texto completoLundvig, Ditte, Evo Lindersson y Poul Henning Jensen. "Pathogenic effects of α-synuclein aggregation". Molecular Brain Research 134, n.º 1 (marzo de 2005): 3–17. http://dx.doi.org/10.1016/j.molbrainres.2004.09.001.
Texto completoGhosh, Dhiman, Surabhi Mehra, Shruti Sahay, Pradeep K. Singh y Samir K. Maji. "α-synuclein aggregation and its modulation". International Journal of Biological Macromolecules 100 (julio de 2017): 37–54. http://dx.doi.org/10.1016/j.ijbiomac.2016.10.021.
Texto completoAfitska, Kseniia, Anna Fucikova, Volodymyr V. Shvadchak y Dmytro A. Yushchenko. "α-Synuclein aggregation at low concentrations". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1867, n.º 7-8 (julio de 2019): 701–9. http://dx.doi.org/10.1016/j.bbapap.2019.05.003.
Texto completoPandey, Neeraj, Jeffrey Strider, William C. Nolan, Sherry X. Yan y James E. Galvin. "Curcumin inhibits aggregation of α-synuclein". Acta Neuropathologica 115, n.º 4 (10 de enero de 2008): 479–89. http://dx.doi.org/10.1007/s00401-007-0332-4.
Texto completoTakano, Mariko, Erika Tashiro, Akira Kitamura, Hiroshi Maita, Sanae M. M. Iguchi-Ariga, Masataka Kinjo y Hiroyoshi Ariga. "Prefoldin prevents aggregation of α-synuclein". Brain Research 1542 (enero de 2014): 186–94. http://dx.doi.org/10.1016/j.brainres.2013.10.034.
Texto completoGao, Huiling, Hehong Sun, Nan Yan, Pu Zhao, He Xu, Wei Zheng, Xiaoyu Zhang, Tao Wang, Chuang Guo y Manli Zhong. "ATP13A2 Declines Zinc-Induced Accumulation of α-Synuclein in a Parkinson’s Disease Model". International Journal of Molecular Sciences 23, n.º 14 (21 de julio de 2022): 8035. http://dx.doi.org/10.3390/ijms23148035.
Texto completoVentura, Salvador y Francisca Pinheiro. "Inducing α-synuclein compaction: a new strategy for inhibiting α-synuclein aggregation?" Neural Regeneration Research 14, n.º 11 (2019): 1897. http://dx.doi.org/10.4103/1673-5374.259608.
Texto completoScheibe, Christian, Christiaan Karreman, Stefan Schildknecht, Marcel Leist y Karin Hauser. "Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation". Biomolecules 11, n.º 8 (21 de julio de 2021): 1067. http://dx.doi.org/10.3390/biom11081067.
Texto completoChen, Chiung Mei, Chih-Hsin Lin, Yih-Ru Wu, Chien-Yu Yen, Yu-Ting Huang, Jia-Lan Lin, Chung-Yin Lin et al. "Lactulose and Melibiose Inhibit α-Synuclein Aggregation and Up-Regulate Autophagy to Reduce Neuronal Vulnerability". Cells 9, n.º 5 (16 de mayo de 2020): 1230. http://dx.doi.org/10.3390/cells9051230.
Texto completoZhou, Wenbo, Chunmei Long, Anthony Fink y Vladimir Uversky. "Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro". Open Life Sciences 5, n.º 1 (1 de febrero de 2010): 11–20. http://dx.doi.org/10.2478/s11535-009-0071-8.
Texto completoPaleologou, K. E., G. B. Irvine y O. M. A. El-Agnaf. "α-Synuclein aggregation in neurodegenerative diseases and its inhibition as a potential therapeutic strategy". Biochemical Society Transactions 33, n.º 5 (26 de octubre de 2005): 1106–10. http://dx.doi.org/10.1042/bst0331106.
Texto completoKo, Eun Ae, Hyun Jin Min y Jeon-Soo Shin. "Interaction of High Mobility Group Box-1 (HMGB1) with α-synuclein and its aggregation (172.28)". Journal of Immunology 188, n.º 1_Supplement (1 de mayo de 2012): 172.28. http://dx.doi.org/10.4049/jimmunol.188.supp.172.28.
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