Статті в журналах з теми "Prion conversion"
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Jones, Rachel. "Blocking prion conversion." Nature Reviews Neuroscience 2, no. 9 (September 2001): 605. http://dx.doi.org/10.1038/35090100.
Повний текст джерелаZhou, Z., and G. Xiao. "Conformational conversion of prion protein in prion diseases." Acta Biochimica et Biophysica Sinica 45, no. 6 (April 11, 2013): 465–76. http://dx.doi.org/10.1093/abbs/gmt027.
Повний текст джерелаHara, Hideyuki, and Suehiro Sakaguchi. "Virus Infection, Genetic Mutations, and Prion Infection in Prion Protein Conversion." International Journal of Molecular Sciences 22, no. 22 (November 18, 2021): 12439. http://dx.doi.org/10.3390/ijms222212439.
Повний текст джерелаRigter, Alan, Jan Priem, Drophatie Timmers-Parohi, Jan PM Langeveld, Fred G. van Zijderveld, and Alex Bossers. "Prion protein self-peptides modulate prion interactions and conversion." BMC Biochemistry 10, no. 1 (2009): 29. http://dx.doi.org/10.1186/1471-2091-10-29.
Повний текст джерелаShen, Liang, and Hong-Fang Ji. "Conformational conversion and prion disease." Nature Reviews Molecular Cell Biology 12, no. 4 (March 23, 2011): 273. http://dx.doi.org/10.1038/nrm3007-c1.
Повний текст джерелаSupattapone, Surachai. "Prion protein conversion in vitro." Journal of Molecular Medicine 82, no. 6 (June 1, 2004): 348–56. http://dx.doi.org/10.1007/s00109-004-0534-3.
Повний текст джерелаDeleault, Nathan R., Ralf W. Lucassen, and Surachai Supattapone. "RNA molecules stimulate prion protein conversion." Nature 425, no. 6959 (October 2003): 717–20. http://dx.doi.org/10.1038/nature01979.
Повний текст джерелаApostol, Marcin I., and Witold K. Surewicz. "Structural Underpinnings of Prion Protein Conversion." Journal of Biological Chemistry 286, no. 21 (May 20, 2011): le7. http://dx.doi.org/10.1074/jbc.l110.213926.
Повний текст джерелаKang, Hae-Eun, Youngwon Mo, Raihah Abd Rahim, Hye-Mi Lee, and Chongsuk Ryou. "Prion Diagnosis: Application of Real-Time Quaking-Induced Conversion." BioMed Research International 2017 (2017): 1–8. http://dx.doi.org/10.1155/2017/5413936.
Повний текст джерелаEngelke, Anna D., Anika Gonsberg, Simrika Thapa, Sebastian Jung, Sarah Ulbrich, Ralf Seidel, Shaon Basu, et al. "Dimerization of the cellular prion protein inhibits propagation of scrapie prions." Journal of Biological Chemistry 293, no. 21 (April 10, 2018): 8020–31. http://dx.doi.org/10.1074/jbc.ra117.000990.
Повний текст джерелаDavenport, Kristen A., Davin M. Henderson, Candace K. Mathiason, and Edward A. Hoover. "Assessment of the PrP c Amino-Terminal Domain in Prion Species Barriers." Journal of Virology 90, no. 23 (September 21, 2016): 10752–61. http://dx.doi.org/10.1128/jvi.01121-16.
Повний текст джерелаTahir, Waqas, Basant Abdulrahman, Dalia H. Abdelaziz, Simrika Thapa, Rupali Walia, and Hermann M. Schätzl. "An astrocyte cell line that differentially propagates murine prions." Journal of Biological Chemistry 295, no. 33 (June 19, 2020): 11572–83. http://dx.doi.org/10.1074/jbc.ra120.012596.
Повний текст джерелаFernández, María Rosario, Cristina Batlle, Marcos Gil-García, and Salvador Ventura. "Amyloid cores in prion domains: Key regulators for prion conformational conversion." Prion 11, no. 1 (January 2, 2017): 31–39. http://dx.doi.org/10.1080/19336896.2017.1282020.
Повний текст джерелаLegname, Giuseppe. "Copper coordination modulates prion conversion and infectivity in mammalian prion proteins." Prion 17, no. 1 (January 3, 2023): 1–6. http://dx.doi.org/10.1080/19336896.2022.2163835.
Повний текст джерелаUchiyama, Keiji, Hironori Miyata, Yoshitaka Yamaguchi, Morikazu Imamura, Mariya Okazaki, Agriani Dini Pasiana, Junji Chida, et al. "Strain-Dependent Prion Infection in Mice Expressing Prion Protein with Deletion of Central Residues 91–106." International Journal of Molecular Sciences 21, no. 19 (October 1, 2020): 7260. http://dx.doi.org/10.3390/ijms21197260.
Повний текст джерелаDavenport, Kristen A., Davin M. Henderson, Jifeng Bian, Glenn C. Telling, Candace K. Mathiason, and Edward A. Hoover. "Insights into Chronic Wasting Disease and Bovine Spongiform Encephalopathy Species Barriers by Use of Real-Time Conversion." Journal of Virology 89, no. 18 (July 8, 2015): 9524–31. http://dx.doi.org/10.1128/jvi.01439-15.
Повний текст джерелаPoggiolini, Ilaria, Daniela Saverioni, and Piero Parchi. "Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions." International Journal of Cell Biology 2013 (2013): 1–24. http://dx.doi.org/10.1155/2013/910314.
Повний текст джерелаHara, Hideyuki, and Suehiro Sakaguchi. "N-Terminal Regions of Prion Protein: Functions and Roles in Prion Diseases." International Journal of Molecular Sciences 21, no. 17 (August 28, 2020): 6233. http://dx.doi.org/10.3390/ijms21176233.
Повний текст джерелаThapa, Simrika, Basant Abdulrahman, Dalia H. Abdelaziz, Li Lu, Manel Ben Aissa, and Hermann M. Schatzl. "Overexpression of quality control proteins reduces prion conversion in prion-infected cells." Journal of Biological Chemistry 293, no. 41 (August 28, 2018): 16069–82. http://dx.doi.org/10.1074/jbc.ra118.002754.
Повний текст джерелаKazlauskaite, Jurate, and Teresa JT Pinheiro. "Binding of prion proteins to lipid membranes and implications for prion conversion." Biochemical Society Transactions 30, no. 3 (June 1, 2002): A95. http://dx.doi.org/10.1042/bst030a095b.
Повний текст джерелаSanghera, Narinder, and Teresa J. T. Pinheiro. "Binding of prion protein to lipid membranes and implications for prion conversion." Journal of Molecular Biology 315, no. 5 (February 2002): 1241–56. http://dx.doi.org/10.1006/jmbi.2001.5322.
Повний текст джерелаSaleem, Fozia, Trent C. Bjorndahl, Carol L. Ladner, Rolando Perez-Pineiro, Burim N. Ametaj, and David S. Wishart. "Lipopolysaccharide induced conversion of recombinant prion protein." Prion 8, no. 2 (March 2014): 221–32. http://dx.doi.org/10.4161/pri.28939.
Повний текст джерелаGill, Andrew C., Sonya Agarwal, Teresa J. T. Pinheiro, and James F. Graham. "Structural requirements for efficient prion protein conversion." Prion 4, no. 4 (October 2010): 235–43. http://dx.doi.org/10.4161/pri.4.4.13394.
Повний текст джерелаCarter, John, Audrius Zukas, Cathrin Bruederle, Audrius A. Zukas, Cathrin E. Bruederle, and John Mark Carter. "Sonication Induced Intermediate in Prion Protein Conversion." Protein & Peptide Letters 15, no. 2 (February 1, 2008): 206–11. http://dx.doi.org/10.2174/092986608783489517.
Повний текст джерелаTuite, Mick F., and Tricia R. Serio. "Conformational conversion and prion disease: authors' reply." Nature Reviews Molecular Cell Biology 12, no. 4 (March 23, 2011): 273. http://dx.doi.org/10.1038/nrm3007-c2.
Повний текст джерелаWang, Fei, Xinhe Wang, and Jiyan Ma. "Conversion of bacterially expressed recombinant prion protein." Methods 53, no. 3 (March 2011): 208–13. http://dx.doi.org/10.1016/j.ymeth.2010.12.013.
Повний текст джерелаBaral, Pravas, Mridula Swayampakula, Manoj Rout, Leo Spyracopoulos, Adriano Aguzzi, and Michael James. "Structural Basis of Prion Protein Conformation Conversion Inhibition." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C812. http://dx.doi.org/10.1107/s2053273314091876.
Повний текст джерелаBarria, Marcelo A., Adriana Libori, Gordon Mitchell, and Mark W. Head. "Susceptibility of Human Prion Protein to Conversion by Chronic Wasting Disease Prions." Emerging Infectious Diseases 24, no. 8 (August 2018): 1482–89. http://dx.doi.org/10.3201/eid2408.161888.
Повний текст джерелаCaughey, Byron. "Prion protein interconversions†." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 356, no. 1406 (February 28, 2001): 197–202. http://dx.doi.org/10.1098/rstb.2000.0765.
Повний текст джерелаRigter, Alan, and Alex Bossers. "Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion." Journal of General Virology 86, no. 9 (September 1, 2005): 2627–34. http://dx.doi.org/10.1099/vir.0.80901-0.
Повний текст джерелаAtarashi, Ryuichiro, Valerie L. Sim, Noriyuki Nishida, Byron Caughey, and Shigeru Katamine. "Prion Strain-Dependent Differences in Conversion of Mutant Prion Proteins in Cell Culture." Journal of Virology 80, no. 16 (August 15, 2006): 7854–62. http://dx.doi.org/10.1128/jvi.00424-06.
Повний текст джерелаMa, Jiyan, Jingjing Zhang, and Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers." Viruses 14, no. 9 (August 31, 2022): 1940. http://dx.doi.org/10.3390/v14091940.
Повний текст джерелаKrauss, Sybille, and Ina Vorberg. "PrionsEx Vivo: What Cell Culture Models Tell Us about Infectious Proteins." International Journal of Cell Biology 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/704546.
Повний текст джерелаAtarashi, Ryuichiro, Roger A. Moore, Valerie L. Sim, Andrew G. Hughson, David W. Dorward, Henry A. Onwubiko, Suzette A. Priola, and Byron Caughey. "Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein." Nature Methods 4, no. 8 (July 22, 2007): 645–50. http://dx.doi.org/10.1038/nmeth1066.
Повний текст джерелаdo Carmo Ferreira, Natália, and Byron Caughey. "Cell-free prion protein conversion assays in screening for anti-prion drug candidates." Current Opinion in Pharmacology 44 (February 2019): 1–7. http://dx.doi.org/10.1016/j.coph.2018.10.001.
Повний текст джерелаKang, Hae-Eun, Jifeng Bian, Sarah J. Kane, Sehun Kim, Vanessa Selwyn, Jenna Crowell, Jason C. Bartz, and Glenn C. Telling. "Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination." Journal of Biological Chemistry 295, no. 30 (June 8, 2020): 10420–33. http://dx.doi.org/10.1074/jbc.ra120.012796.
Повний текст джерелаMcMahon, Hilary E. M. "Prion processing: a double-edged sword?" Biochemical Society Transactions 40, no. 4 (July 20, 2012): 735–38. http://dx.doi.org/10.1042/bst20120031.
Повний текст джерелаLegname, Giuseppe. "Early structural features in mammalian prion conformation conversion." Prion 6, no. 1 (January 2012): 37–39. http://dx.doi.org/10.4161/pri.6.1.18425.
Повний текст джерелаSpagnolli, Giovanni, Marta Rigoli, Simone Orioli, Alejandro M. Sevillano, Pietro Faccioli, Holger Wille, Emiliano Biasini, and Jesús R. Requena. "Full atomistic model of prion structure and conversion." PLOS Pathogens 15, no. 7 (July 11, 2019): e1007864. http://dx.doi.org/10.1371/journal.ppat.1007864.
Повний текст джерелаKudryavtseva, Sofia S., Aleksandra K. Melnikova, Vladimir I. Muronetz, and Yulia Yu Stroylova. "Methylglyoxal modification hinders amyloid conversion of prion protein." Mendeleev Communications 28, no. 3 (May 2018): 314–16. http://dx.doi.org/10.1016/j.mencom.2018.05.029.
Повний текст джерелаHead, Mark W., and James W. Ironside. "Inhibition of prion-protein conversion: a therapeutic tool?" Trends in Microbiology 8, no. 1 (January 2000): 6–8. http://dx.doi.org/10.1016/s0966-842x(99)01656-x.
Повний текст джерелаKuwata, K., N. Nishida, T. Matsumoto, Y. O. Kamatari, J. Hosokawa-Muto, K. Kodama, H. K. Nakamura, et al. "Hot spots in prion protein for pathogenic conversion." Proceedings of the National Academy of Sciences 104, no. 29 (July 6, 2007): 11921–26. http://dx.doi.org/10.1073/pnas.0702671104.
Повний текст джерелаHooper, Nigel M. "Glypican-1 facilitates prion conversion in lipid rafts." Journal of Neurochemistry 116, no. 5 (February 9, 2011): 721–25. http://dx.doi.org/10.1111/j.1471-4159.2010.06936.x.
Повний текст джерелаMarijanovic, Zrinka, Anna Caputo, Vincenza Campana, and Chiara Zurzolo. "Identification of an Intracellular Site of Prion Conversion." PLoS Pathogens 5, no. 5 (May 8, 2009): e1000426. http://dx.doi.org/10.1371/journal.ppat.1000426.
Повний текст джерелаCaughey, B., and G. S. Baron. "Factors affecting interactions between prion protein isoforms." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 565–69. http://dx.doi.org/10.1042/bst0300565.
Повний текст джерелаOrge, Leonor, Carla Lima, Carla Machado, Paula Tavares, Paula Mendonça, Paulo Carvalho, João Silva, et al. "Neuropathology of Animal Prion Diseases." Biomolecules 11, no. 3 (March 21, 2021): 466. http://dx.doi.org/10.3390/biom11030466.
Повний текст джерелаHarris, David A. "Cellular Biology of Prion Diseases." Clinical Microbiology Reviews 12, no. 3 (July 1, 1999): 429–44. http://dx.doi.org/10.1128/cmr.12.3.429.
Повний текст джерелаDelmouly, Karine, Maxime Belondrade, Danielle Casanova, Ollivier Milhavet, and Sylvain Lehmann. "HEPES inhibits the conversion of prion protein in cell culture." Journal of General Virology 92, no. 5 (May 1, 2011): 1244–50. http://dx.doi.org/10.1099/vir.0.027334-0.
Повний текст джерелаChoi, Jin-Kyu, Ignazio Cali, Krystyna Surewicz, Qingzhong Kong, Pierluigi Gambetti, and Witold K. Surewicz. "Amyloid fibrils from the N-terminal prion protein fragment are infectious." Proceedings of the National Academy of Sciences 113, no. 48 (November 14, 2016): 13851–56. http://dx.doi.org/10.1073/pnas.1610716113.
Повний текст джерелаHannaoui, Samia, Sara Amidian, Yo Ching Cheng, Camilo Duque Velásquez, Lyudmyla Dorosh, Sampson Law, Glenn Telling, et al. "Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency." PLOS Pathogens 13, no. 8 (August 11, 2017): e1006553. http://dx.doi.org/10.1371/journal.ppat.1006553.
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