Статті в журналах з теми "Cellular prion protein physiological function, Myelin"
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Nuvolone, Mario, Mario Hermann, Silvia Sorce, Giancarlo Russo, Cinzia Tiberi, Petra Schwarz, Eric Minikel, Despina Sanoudou, Pawel Pelczar, and Adriano Aguzzi. "Strictly co-isogenic C57BL/6J-Prnp−/− mice: A rigorous resource for prion science." Journal of Experimental Medicine 213, no. 3 (February 29, 2016): 313–27. http://dx.doi.org/10.1084/jem.20151610.
Повний текст джерелаMartins, V. R., A. F. Mercadante, A. L. B. Cabral, A. R. O. Freitas, and R. M. R. P. S. Castro. "Insights into the physiological function of cellular prion protein." Brazilian Journal of Medical and Biological Research 34, no. 5 (May 2001): 585–95. http://dx.doi.org/10.1590/s0100-879x2001000500005.
Повний текст джерелаFranzmann, Titus M., Marcus Jahnel, Andrei Pozniakovsky, Julia Mahamid, Alex S. Holehouse, Elisabeth Nüske, Doris Richter, et al. "Phase separation of a yeast prion protein promotes cellular fitness." Science 359, no. 6371 (January 4, 2018): eaao5654. http://dx.doi.org/10.1126/science.aao5654.
Повний текст джерелаGo, Gyeongyun, and Sang Hun Lee. "The Cellular Prion Protein: A Promising Therapeutic Target for Cancer." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9208. http://dx.doi.org/10.3390/ijms21239208.
Повний текст джерелаWestergard, Laura, Heather M. Christensen, and David A. Harris. "The cellular prion protein (PrPC): Its physiological function and role in disease." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1772, no. 6 (June 2007): 629–44. http://dx.doi.org/10.1016/j.bbadis.2007.02.011.
Повний текст джерелаMiranzadeh Mahabadi, Hajar, and Changiz Taghibiglou. "Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction." International Journal of Molecular Sciences 21, no. 19 (September 25, 2020): 7058. http://dx.doi.org/10.3390/ijms21197058.
Повний текст джерелаAguzzi, Adriano, and Anna Maria Calella. "Prions: Protein Aggregation and Infectious Diseases." Physiological Reviews 89, no. 4 (October 2009): 1105–52. http://dx.doi.org/10.1152/physrev.00006.2009.
Повний текст джерелаHenzi, Anna, and Adriano Aguzzi. "The prion protein is not required for peripheral nerve de- and remyelination after crush injury." PLOS ONE 16, no. 1 (January 22, 2021): e0245944. http://dx.doi.org/10.1371/journal.pone.0245944.
Повний текст джерелаLorca, Ramón A., Lorena Varela-Nallar, Nibaldo C. Inestrosa, and J. Pablo Huidobro-Toro. "The Cellular Prion Protein Prevents Copper-Induced Inhibition of P2X4Receptors." International Journal of Alzheimer's Disease 2011 (2011): 1–6. http://dx.doi.org/10.4061/2011/706576.
Повний текст джерелаYoon, Sungtae, Gyeongyun Go, Yeomin Yoon, Jiho Lim, Gaeun Lee, and Sanghun Lee. "Harnessing the Physiological Functions of Cellular Prion Protein in the Kidneys: Applications for Treating Renal Diseases." Biomolecules 11, no. 6 (May 22, 2021): 784. http://dx.doi.org/10.3390/biom11060784.
Повний текст джерелаKovač, Valerija, and Vladka Čurin Šerbec. "Prion Protein: The Molecule of Many Forms and Faces." International Journal of Molecular Sciences 23, no. 3 (January 22, 2022): 1232. http://dx.doi.org/10.3390/ijms23031232.
Повний текст джерелаCaldarulo, Enrico, Alessandro Barducci, Kurt Wüthrich та Michele Parrinello. "Prion protein β2–α2 loop conformational landscape". Proceedings of the National Academy of Sciences 114, № 36 (21 серпня 2017): 9617–22. http://dx.doi.org/10.1073/pnas.1712155114.
Повний текст джерелаKhosravani, Houman, Yunfeng Zhang, Shigeki Tsutsui, Shahid Hameed, Christophe Altier, Jawed Hamid, Lina Chen, et al. "Prion protein attenuates excitotoxicity by inhibiting NMDA receptors." Journal of Cell Biology 181, no. 3 (April 28, 2008): 551–65. http://dx.doi.org/10.1083/jcb.200711002.
Повний текст джерелаPrado, Mariana Brandão, Maria Isabel Melo Escobar, Rodrigo Nunes Alves, Bárbara Paranhos Coelho, Camila Felix de Lima Fernandes, Jacqueline Marcia Boccacino, Rebeca Piatniczka Iglesia, and Marilene Hohmuth Lopes. "Prion Protein at the Leading Edge: Its Role in Cell Motility." International Journal of Molecular Sciences 21, no. 18 (September 12, 2020): 6677. http://dx.doi.org/10.3390/ijms21186677.
Повний текст джерелаVarela-Nallar, Lorena, Enrique M. Toledo, Luis F. Larrondo, Ana L. B. Cabral, Vilma R. Martins, and Nibaldo C. Inestrosa. "Induction of cellular prion protein gene expression by copper in neurons." American Journal of Physiology-Cell Physiology 290, no. 1 (January 2006): C271—C281. http://dx.doi.org/10.1152/ajpcell.00160.2005.
Повний текст джерелаDondapati, Divya Teja, Pradeep Reddy Cingaram, Ferhan Ayaydin, Antal Nyeste, Andor Kanyó, Ervin Welker, and Elfrieda Fodor. "Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin." Membranes 11, no. 12 (December 13, 2021): 978. http://dx.doi.org/10.3390/membranes11120978.
Повний текст джерелаKhosravani, Houman, Yunfeng Zhang, Shigeki Tsutsui, Shahid Hameed, Jawed Hamid, Christophe Altier, Frank R. Jirik, and Gerald W. Zamponi. "Modulation of NMDA receptors by prion proteins." Clinical & Investigative Medicine 30, no. 4 (August 1, 2007): 85. http://dx.doi.org/10.25011/cim.v30i4.2859.
Повний текст джерелаKhosravani, H., Y. Zhang, S. Tsutsui, S. Hameed, C. Altier, J. Hamid, L. Chen, et al. "LACK OF CELLULAR PRION PROTEIN UNMASKS NMDA NR2D SUBUNIT RECEPTOR FUNCTION WITH CONSEQUENCES TOWARD SYNAPTIC TRANSMISSION AND EXCITOTOXICITY." Clinical & Investigative Medicine 31, no. 4 (August 1, 2008): 14. http://dx.doi.org/10.25011/cim.v31i4.4811.
Повний текст джерелаD’Alessio, Stefania, Stefanía Thorgeirsdóttir, Igor Kraev, Karl Skírnisson, and Sigrun Lange. "Post-Translational Protein Deimination Signatures in Plasma and Plasma EVs of Reindeer (Rangifer tarandus)." Biology 10, no. 3 (March 13, 2021): 222. http://dx.doi.org/10.3390/biology10030222.
Повний текст джерелаGonzalez-Gronow, Mario, and Salvatore Vincent Pizzo. "Physiological Roles of the Autoantibodies to the 78-Kilodalton Glucose-Regulated Protein (GRP78) in Cancer and Autoimmune Diseases." Biomedicines 10, no. 6 (May 24, 2022): 1222. http://dx.doi.org/10.3390/biomedicines10061222.
Повний текст джерелаHolada, Karel, Jan Simak, and Jaroslav G. Vostal. "The Post-Transfusion Recovery and Survival of Red Blood Cells in Mice Is Affected by the Expression of Cellular Prion Protein." Blood 108, no. 11 (November 16, 2006): 959. http://dx.doi.org/10.1182/blood.v108.11.959.959.
Повний текст джерелаNoori, Leila, Kamila Filip, Zohreh Nazmara, Simin Mahakizadeh, Gholamreza Hassanzadeh, Celeste Caruso Caruso Bavisotto, Fabio Bucchieri, et al. "Contribution of Extracellular Vesicles and Molecular Chaperones in Age-Related Neurodegenerative Disorders of the CNS." International Journal of Molecular Sciences 24, no. 2 (January 4, 2023): 927. http://dx.doi.org/10.3390/ijms24020927.
Повний текст джерелаCarlston, Colleen, Robin Weinmann, Natalia Stec, Simona Abbatemarco, Francoise Schwager, Jing Wang, Huiwu Ouyang, Collin Y. Ewald, Monica Gotta, and Christopher M. Hammell. "PQN-59 antagonizes microRNA-mediated repression during post-embryonic temporal patterning and modulates translation and stress granule formation in C. elegans." PLOS Genetics 17, no. 11 (November 22, 2021): e1009599. http://dx.doi.org/10.1371/journal.pgen.1009599.
Повний текст джерелаSoukup, Alexandra, Kirby D. Johnson, Daniel J. Conn, Evgenia Shishkova, Koichi Ricardo Katsumura, Peng Liu, Erik A. Ranheim, et al. "GATA2-Dependent Developmental and Regenerative Networks." Blood 134, Supplement_1 (November 13, 2019): 1182. http://dx.doi.org/10.1182/blood-2019-126875.
Повний текст джерелаTsutsui, Shigeki, Megan Morgan, Hugo Tedford, Haitao You, Gerald W. Zamponi та Peter K. Stys. "Copper ions, prion protein and Aβ modulate Ca levels in central nervous system myelin in an NMDA receptor-dependent manner". Molecular Brain 15, № 1 (26 липня 2022). http://dx.doi.org/10.1186/s13041-022-00955-2.
Повний текст джерелаDidonna, Alessandro. "Prion protein and its role in signal transduction." Cellular and Molecular Biology Letters 18, no. 2 (January 1, 2013). http://dx.doi.org/10.2478/s11658-013-0085-0.
Повний текст джерелаSchneider, Benoit, Anne Baudry, Mathéa Pietri, Aurélie Alleaume-Butaux, Chloé Bizingre, Pierre Nioche, Odile Kellermann, and Jean-Marie Launay. "The Cellular Prion Protein—ROCK Connection: Contribution to Neuronal Homeostasis and Neurodegenerative Diseases." Frontiers in Cellular Neuroscience 15 (April 12, 2021). http://dx.doi.org/10.3389/fncel.2021.660683.
Повний текст джерелаGielnik, Maciej, Michał Taube, Lilia Zhukova, Igor Zhukov, Sebastian K. T. S. Wärmländer, Željko Svedružić, Wojciech M. Kwiatek, Astrid Gräslund, and Maciej Kozak. "Zn(II) binding causes interdomain changes in the structure and flexibility of the human prion protein." Scientific Reports 11, no. 1 (November 4, 2021). http://dx.doi.org/10.1038/s41598-021-00495-0.
Повний текст джерелаMatamoros-Angles, A., A. Hervera, J. Soriano, E. Martí, P. Carulla, F. Llorens, M. Nuvolone, et al. "Analysis of co-isogenic prion protein deficient mice reveals behavioral deficits, learning impairment, and enhanced hippocampal excitability." BMC Biology 20, no. 1 (January 13, 2022). http://dx.doi.org/10.1186/s12915-021-01203-0.
Повний текст джерелаBosch, Assumpció, and Raúl Estévez. "Megalencephalic Leukoencephalopathy: Insights Into Pathophysiology and Perspectives for Therapy." Frontiers in Cellular Neuroscience 14 (January 22, 2021). http://dx.doi.org/10.3389/fncel.2020.627887.
Повний текст джерелаCorraliza-Gomez, Miriam, Beatriz Bendito, David Sandonis-Camarero, Jorge Mondejar-Duran, Miguel Villa, Marta Poncela, Jorge Valero, Diego Sanchez, and Maria D. Ganfornina. "Dual role of Apolipoprotein D as long-term instructive factor and acute signal conditioning microglial secretory and phagocytic responses." Frontiers in Cellular Neuroscience 17 (January 26, 2023). http://dx.doi.org/10.3389/fncel.2023.1112930.
Повний текст джерелаBaena-Montes, Jara M., Sahar Avazzadeh та Leo R. Quinlan. "α-synuclein pathogenesis in hiPSC models of Parkinson’s disease". Neuronal Signaling 5, № 2 (червень 2021). http://dx.doi.org/10.1042/ns20210021.
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