Cell models of prion infection
Vet. Res., 39 4 (2008) 10
Published online: 2007-11-27
Articles citing this article
The Citing articles tool gives a list of articles citing the current article.
The citing articles come from EDP Sciences database, as well as other publishers participating in CrossRef Cited-by Linking Program. You can set up your personal account to receive an email alert each time this article is cited by a new article (see the menu on the right-hand side of the abstract page).
Cited article:
This article has been cited by the following article(s):
A Neuronal Cell Line Model for Studying Camel Prions
Basant Abdulrahman, Shabboo Rahimi Aqdam, Matteo Mosca, Hanaa Ahmed-Hassan, Melissa Razcon-Echeagaray, Lia Popa, Sabine Gilch, Baaissa Babelhadj, Gabriele Vaccari and Hermann M. SchätzlPathogens 15 (5) 472 (2026)
https://doi.org/10.3390/pathogens15050472
Bifunctional carbazole derivatives for simultaneous therapy and fluorescence imaging in prion disease murine cell models
Matteo Staderini, Silvia Vanni, Arianna Colini Baldeschi, Gabriele Giachin, Marco Zattoni, Luigi Celauro, Chiara Ferracin, Edoardo Bistaffa, Fabio Moda, Daniel I. Pérez, Ana Martínez, M. Antonia Martín, Olmo Martín-Cámara, Ángel Cores, Giulia Bianchini, Robert Kammerer, J. Carlos Menéndez, Giuseppe Legname and Maria Laura BolognesiEuropean Journal of Medicinal Chemistry 245 114923 (2023)
https://doi.org/10.1016/j.ejmech.2022.114923
Sensitive microscopic quantification of surface-bound prion infectivity for the assessment of surgical instrument decontamination procedures
T.J. Secker, R.C. Hervé and C.W. KeevilJournal of Hospital Infection 132 116 (2023)
https://doi.org/10.1016/j.jhin.2022.09.020
Competition for calnexin binding regulates secretion and turnover of misfolded GPI-anchored proteins
Amber M. Cheatham, Nishi Raj Sharma and Prasanna Satpute-KrishnanJournal of Cell Biology 222 (10) (2023)
https://doi.org/10.1083/jcb.202108160
Tackling prion diseases: a review of the patent landscape
Marco Zattoni and Giuseppe LegnameExpert Opinion on Therapeutic Patents 31 (12) 1097 (2021)
https://doi.org/10.1080/13543776.2021.1945033
Cellular models for discovering prion disease therapeutics: Progress and challenges
Saffire H. Krance, Russell Luke, Marc Shenouda, et al.Journal of Neurochemistry 153 (2) 150 (2020)
https://doi.org/10.1111/jnc.14956
(2020)
https://doi.org/10.1101/2020.04.01.019786
Prion infection, transmission, and cytopathology modeled in a low-biohazard human cell line
Merve Avar, Daniel Heinzer, Nicolas Steinke, et al.Life Science Alliance 3 (8) e202000814 (2020)
https://doi.org/10.26508/lsa.202000814
BMD42-2910, a Novel Benzoxazole Derivative, Shows a Potent Anti-prion Activity and Prolongs the Mean Survival in an Animal Model of Prion Disease
Jae Wook Hyeon, Ran Noh, Jiwon Choi, et al.Experimental Neurobiology 29 (1) 93 (2020)
https://doi.org/10.5607/en.2020.29.1.93
Engineering a murine cell line for the stable propagation of hamster prions
Matthew E.C. Bourkas, Hamza Arshad, Zaid A.M. Al-Azzawi, et al.Journal of Biological Chemistry 294 (13) 4911 (2019)
https://doi.org/10.1074/jbc.RA118.007135
A PRNP-Disrupted Human Neuroblastoma Cell Line and Its Stable Transformants Expressing Prion Protein Variants
Yuko Okemoto-Nakamura, Isei Tanida, Toshiyuki Yamaji, Kentaro Hanada and Ken’ichi HagiwaraBPB Reports 2 (5) 73 (2019)
https://doi.org/10.1248/bpbreports.2.5_73
Gene-edited murine cell lines for propagation of chronic wasting disease prions
Rupali Walia, Cheng Ching Ho, Chi Lee, Sabine Gilch and Hermann M. SchatzlScientific Reports 9 (1) (2019)
https://doi.org/10.1038/s41598-019-47629-z
A New Cell Model for Investigating Prion Strain Selection and Adaptation
Alexandra Philiastides, Juan Manuel Ribes, Daniel Chun-Mun Yip, Christian Schmidt, Iryna Benilova and Peter-Christian KlöhnViruses 11 (10) 888 (2019)
https://doi.org/10.3390/v11100888
Acute Neurotoxicity Models of Prion Disease
A. M. T. Islam, P. A. Adlard, D. I. Finkelstein, et al.ACS Chemical Neuroscience 9 (3) 431 (2018)
https://doi.org/10.1021/acschemneuro.7b00517
Cellular mechanisms responsible for cell-to-cell spreading of prions
Didier Vilette, Josquin Courte, Jean Michel Peyrin, et al.Cellular and Molecular Life Sciences 75 (14) 2557 (2018)
https://doi.org/10.1007/s00018-018-2823-y
A stretch of residues within the protease-resistant core is not necessary for prion structure and infectivity
Carola Munoz-Montesino, Christina Sizun, Mohammed Moudjou, et al.Prion 11 (1) 25 (2017)
https://doi.org/10.1080/19336896.2016.1274851
Exosomes and Microvesicles
Pascal Leblanc, Zaira E. Arellano-Anaya, Emilien Bernard, et al.Methods in Molecular Biology, Exosomes and Microvesicles 1545 153 (2017)
https://doi.org/10.1007/978-1-4939-6728-5_11
Prions
Zaira E. Arellano-Anaya, Alvina Huor, Pascal Leblanc, Olivier Andréoletti and Didier ViletteMethods in Molecular Biology, Prions 1658 95 (2017)
https://doi.org/10.1007/978-1-4939-7244-9_8
Biomedical Applications of Acridines
Jan Ježek, Jan Hlaváček and Jaroslav ŠebestíkProgress in Drug Research, Biomedical Applications of Acridines 72 99 (2017)
https://doi.org/10.1007/978-3-319-63953-6_6
A transfectant RK13 cell line permissive to classical caprine scrapie prion propagation
Rohana P. Dassanayake, Dongyue Zhuang, Thomas C. Truscott, et al.Prion 10 (2) 153 (2016)
https://doi.org/10.1080/19336896.2016.1166324
Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification
Mohammed Moudjou, Jérôme Chapuis, Mériem Mekrouti, et al.Scientific Reports 6 (1) (2016)
https://doi.org/10.1038/srep29116
Methods for Differentiating Prion Types in Food-Producing Animals
Kevin Gough, Helen Rees, Sarah Ives and Ben MaddisonBiology 4 (4) 785 (2015)
https://doi.org/10.3390/biology4040785
Synthetic prions and other human neurodegenerative proteinopathies
Nhat Tran Thanh Le, Joanna Narkiewicz, Suzana Aulić, et al.Virus Research 207 25 (2015)
https://doi.org/10.1016/j.virusres.2014.10.020
Approaches for discovering anti-prion compounds: lessons learned and challenges ahead
Maria Laura Bolognesi and Giuseppe LegnameExpert Opinion on Drug Discovery 10 (4) 389 (2015)
https://doi.org/10.1517/17460441.2015.1016498
Generation of a Persistently Infected MDBK Cell Line with Natural Bovine Spongiform Encephalopathy (BSE)
Dongseob Tark, Hyojin Kim, Michael H. Neale, et al.PLOS ONE 10 (2) e0115939 (2015)
https://doi.org/10.1371/journal.pone.0115939
hTERT-immortalized ovine microglia propagate natural scrapie isolates
Juan F. Muñoz-Gutiérrez, David A. Schneider, Timothy V. Baszler, et al.Virus Research 198 35 (2015)
https://doi.org/10.1016/j.virusres.2014.10.028
Discovery of Novel Anti-prion Compounds Using In Silico and In Vitro Approaches
Jae Wook Hyeon, Jiwon Choi, Su Yeon Kim, et al.Scientific Reports 5 (1) (2015)
https://doi.org/10.1038/srep14944
Prion strains are differentially released through the exosomal pathway
Zaira E. Arellano-Anaya, Alvina Huor, Pascal Leblanc, et al.Cellular and Molecular Life Sciences 72 (6) 1185 (2015)
https://doi.org/10.1007/s00018-014-1735-8
Prion disease tempo determined by host-dependent substrate reduction
Charles E. Mays, Chae Kim, Tracy Haldiman, et al.Journal of Clinical Investigation 124 (2) 847 (2014)
https://doi.org/10.1172/JCI72241
Assessing Proteinase K Resistance of Fish Prion Proteins in a Scrapie-Infected Mouse Neuroblastoma Cell Line
Evgenia Salta, Eirini Kanata, Christos Ouzounis, Sabine Gilch, Hermann Schätzl and Theodoros SklaviadisViruses 6 (11) 4398 (2014)
https://doi.org/10.3390/v6114398
Endoproteolytic processing of the mammalian prion glycoprotein family
Charles E. Mays, Janaky Coomaraswamy, Joel C. Watts, et al.The FEBS Journal 281 (3) 862 (2014)
https://doi.org/10.1111/febs.12654
Prion Protein Interaction with Soil Humic Substances: Environmental Implications
Gabriele Giachin, Joanna Narkiewicz, Denis Scaini, et al.PLoS ONE 9 (6) e100016 (2014)
https://doi.org/10.1371/journal.pone.0100016
Successes and Challenges in Phenotype-Based Lead Discovery for Prion Diseases
Sina Ghaemmaghami, Miranda Russo and Adam R. RensloJournal of Medicinal Chemistry 57 (16) 6919 (2014)
https://doi.org/10.1021/jm5001425
Prion Protein Accumulation in Lipid Rafts of Mouse Aging Brain
Federica Agostini, Carlos G. Dotti, Azucena Pérez-Cañamás, et al.PLoS ONE 8 (9) e74244 (2013)
https://doi.org/10.1371/journal.pone.0074244
Prion Propagation and Toxicity Occur In Vitro with Two-Phase Kinetics Specific to Strain and Neuronal Type
Samia Hannaoui, Layal Maatouk, Nicolas Privat, et al.Journal of Virology 87 (5) 2535 (2013)
https://doi.org/10.1128/JVI.03082-12
Alteration of cell responses to PrPSc in prolonged cell culture and its effect on transmission of PrPSc to neural cells
Abdelazim E. Elhelaly, Yasuo Inoshima and Naotaka IshiguroArchives of Virology 158 (3) 651 (2013)
https://doi.org/10.1007/s00705-012-1540-3
Towards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays
Susann Boerner, Katja Wagenführ, Martin L Daus, Achim Thomzig and Michael BeekesLaboratory Animals 47 (2) 106 (2013)
https://doi.org/10.1177/0023677213476856
Prion Pathogenesis Is Faithfully Reproduced in Cerebellar Organotypic Slice Cultures
Jeppe Falsig, Tiziana Sonati, Uli S. Herrmann, et al.PLoS Pathogens 8 (11) e1002985 (2012)
https://doi.org/10.1371/journal.ppat.1002985
Shadoo/PrP (Sprn0/0/Prnp0/0) double knockout mice
Nathalie Daude and David WestawayPrion 6 (5) 420 (2012)
https://doi.org/10.4161/pri.21867
Synthesis and Evaluation of 1‐Amino‐6‐halo‐β‐carbolines as Antimalarial and Antiprion Agents
Mark J. Thompson, Jennifer C. Louth, Susan M. Little, Matthew P. Jackson, Yohan Boursereau, Beining Chen and Iain ColdhamChemMedChem 7 (4) 578 (2012)
https://doi.org/10.1002/cmdc.201200002
Cytochalasin D enhances the accumulation of a protease‐resistant form of prion protein in ScN2a cells: involvement of PI3 kinase/Akt signalling pathway
Takato Takenouchi, Yoshifumi Iwamaru, Morikazu Imamura, et al.Cell Biology International 36 (12) 1223 (2012)
https://doi.org/10.1042/CBI20120329
Prion inhibition with multivalent PrPSc binding compounds
Charles E. Mays, Shaon Joy, Lei Li, Linghui Yu, Sacha Genovesi, Frederick G. West and David WestawayBiomaterials 33 (28) 6808 (2012)
https://doi.org/10.1016/j.biomaterials.2012.06.004
Inhibition of PrPScformation in scrapie infected N2a cells by 5,7,8-trimethyl-3,4-dihydro-2H-1,4-benzoxazine derivatives
Fani Koukouli, Ioannis Paspaltsis, Evgenia Salta, et al.Prion 6 (5) 470 (2012)
https://doi.org/10.4161/pri.21913
Joint Scientific Opinion on any possible epidemiological or molecular association between TSEs in animals and humans
EFSA Journal 9 (1) 1945 (2011)https://doi.org/10.2903/j.efsa.2011.1945
Mammalian prions
Jimmy Savistchenko, Zaira E. Arellano-Anaya, Olivier Andréoletti and Didier VilettePrion 5 (2) 84 (2011)
https://doi.org/10.4161/pri.5.2.16096
Discovery of 6-substituted indole-3-glyoxylamides as lead antiprion agents with enhanced cell line activity, improved microsomal stability and low toxicity
Mark J. Thompson, Jennifer C. Louth, Steven Ferrara, et al.European Journal of Medicinal Chemistry 46 (9) 4125 (2011)
https://doi.org/10.1016/j.ejmech.2011.06.013
A Simple, Versatile and Sensitive Cell-Based Assay for Prions from Various Species
Zaira E. Arellano-Anaya, Jimmy Savistchenko, Jacinthe Mathey, et al.PLoS ONE 6 (5) e20563 (2011)
https://doi.org/10.1371/journal.pone.0020563
Spongiform degeneration induced by neuropathogenic murine coronavirus infection
Hiromi Kashiwazaki, Risa Nomura, Shutoku Matsuyama, Fumihiro Taguchi and Rihito WatanabePathology International 61 (4) 184 (2011)
https://doi.org/10.1111/j.1440-1827.2010.02639.x
Recovery of Small Infectious PrPres Aggregates from Prion-infected Cultured Cells
Zaira E. Arellano Anaya, Jimmy Savistchenko, Véronique Massonneau, et al.Journal of Biological Chemistry 286 (10) 8141 (2011)
https://doi.org/10.1074/jbc.M110.165233
Structure–Activity Relationship Refinement and Further Assessment of Indole‐3‐glyoxylamides as a Lead Series against Prion Disease
Mark J. Thompson, Jennifer C. Louth, Steven Ferrara, Fiona J. Sorrell, Benjamin J. Irving, Edward J. Cochrane, Anthony J. H. M. Meijer and Beining ChenChemMedChem 6 (1) 115 (2011)
https://doi.org/10.1002/cmdc.201000383
Fukuoka‐1 strain of transmissible spongiform encephalopathy agent infects murine bone marrow–derived cells with features of mesenchymal stem cells
Larisa Cervenakova, Sergey Akimov, Irina Vasilyeva, et al.Transfusion 51 (8) 1755 (2011)
https://doi.org/10.1111/j.1537-2995.2010.03041.x
Infection of Cell Lines with Experimental and Natural Ovine Scrapie Agents
Michael H. Neale, Susan J. Mountjoy, Jane C. Edwards, et al.Journal of Virology 84 (5) 2444 (2010)
https://doi.org/10.1128/JVI.01855-09
Conservation of a Glycine-rich Region in the Prion Protein Is Required for Uptake of Prion Infectivity
Christopher F. Harrison, Victoria A. Lawson, Bradley M. Coleman, et al.Journal of Biological Chemistry 285 (26) 20213 (2010)
https://doi.org/10.1074/jbc.M109.093310
Inducible expression of chimpanzee prion protein (PrP) in murine PrP knock-out cells
Lars Heinig, Daniel A. Mueller, Sanja Ramljak, Edgar Holznagel and Andreas W. StukeProtein Expression and Purification 70 (2) 129 (2010)
https://doi.org/10.1016/j.pep.2009.09.015
Improved 2,4‐Diarylthiazole‐Based Antiprion Agents: Switching the Sense of the Amide Group at C5 Leads to an Increase in Potency
Mark J. Thompson, Jennifer C. Louth, Gemma K. Greenwood, Fiona J. Sorrell, Sandra G. Knight, Nathan B. P. Adams and Beining ChenChemMedChem 5 (9) 1476 (2010)
https://doi.org/10.1002/cmdc.201000217
Redox Control of Prion and Disease Pathogenesis
Neena Singh, Ajay Singh, Dola Das and Maradumane L. MohanAntioxidants & Redox Signaling 12 (11) 1271 (2010)
https://doi.org/10.1089/ars.2009.2628
Synthesis of Conjugates of 6-Aminophenanthridine and Guanabenz, Two Structurally Unrelated Prion Inhibitors, for the Determination of Their Cellular Targets by Affinity Chromatography
Fabienne Gug, Nassima Oumata, Déborah Tribouillard-Tanvier, et al.Bioconjugate Chemistry 21 (2) 279 (2010)
https://doi.org/10.1021/bc900314n
Prion infection of differentiated neurospheres
Maria Eugenia Herva, Aroa Relaño-Ginés, Ana Villa and Juan María TorresJournal of Neuroscience Methods 188 (2) 270 (2010)
https://doi.org/10.1016/j.jneumeth.2010.02.022
Bovine spongiform encephalopathy
Jane L. Harman and Christopher J. SilvaJournal of the American Veterinary Medical Association 234 (1) 59 (2009)
https://doi.org/10.2460/javma.234.1.59
Encyclopedia of Microbiology
W. BodemerEncyclopedia of Microbiology 689 (2009)
https://doi.org/10.1016/B978-012373944-5.00200-5
Design, Synthesis, and Structure−Activity Relationship of Indole-3-glyoxylamide Libraries Possessing Highly Potent Activity in a Cell Line Model of Prion Disease
Mark J. Thompson, Vinciane Borsenberger, Jennifer C. Louth, Katie E. Judd and Beining ChenJournal of Medicinal Chemistry 52 (23) 7503 (2009)
https://doi.org/10.1021/jm900920x
Identification of an Intracellular Site of Prion Conversion
Zrinka Marijanovic, Anna Caputo, Vincenza Campana, Chiara Zurzolo and Neil MabbottPLoS Pathogens 5 (5) e1000426 (2009)
https://doi.org/10.1371/journal.ppat.1000426
Genetic heterogeneity versus molecular analysis of prion susceptibility in neuroblasma N2a sublines
Stéphanie Chasseigneaux, Manuela Pastore, Janice Britton-Davidian, et al.Archives of Virology 153 (9) 1693 (2008)
https://doi.org/10.1007/s00705-008-0177-8
Persistent Propagation of Variant Creutzfeldt-Jakob Disease Agent in Murine Spleen Stromal Cell Culture with Features of Mesenchymal Stem Cells
Sergey Akimov, Oksana Yakovleva, Irina Vasilyeva, Carroll McKenzie and Larisa CervenakovaJournal of Virology 82 (21) 10959 (2008)
https://doi.org/10.1128/JVI.01085-08
A cell line infectible by prion strains from different species
M.-P. Courageot, N. Daude, R. Nonno, et al.Journal of General Virology 89 (1) 341 (2008)
https://doi.org/10.1099/vir.0.83344-0
Small-Ruminant Lentivirus Enhances PrP Sc Accumulation in Cultured Sheep Microglial Cells
James B. Stanton, Donald P. Knowles, Katherine I. O'Rourke, et al.Journal of Virology 82 (20) 9839 (2008)
https://doi.org/10.1128/JVI.01137-08
Antihypertensive Drug Guanabenz Is Active In Vivo against both Yeast and Mammalian Prions
Déborah Tribouillard-Tanvier, Vincent Béringue, Nathalie Desban, et al.PLoS ONE 3 (4) e1981 (2008)
https://doi.org/10.1371/journal.pone.0001981
Prions Impair Bioaminergic Functions through Serotonin- or Catecholamine-derived Neurotoxins in Neuronal Cells
Sophie Mouillet-Richard, Noriyuki Nishida, Elodie Pradines, et al.Journal of Biological Chemistry 283 (35) 23782 (2008)
https://doi.org/10.1074/jbc.M802433200
Cellular pathogenesis in prion diseases
Carole Crozet, Florence Beranger and Sylvain LehmannVeterinary Research 39 (4) 44 (2008)
https://doi.org/10.1051/vetres:2008021