Cystatin F is a biomarker of prion pathogenesis in mice
Open accessAbstract
Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases. Experimental and epidemiological evidence point toward a protracted, clinically silent phase in prion diseases, yet there is no diagnostic test capable of identifying asymptomatic individuals incubating prions. In an effort to identify early biomarkers of prion diseases, we have compared global transcriptional profiles in brains from pre-symptomatic prion-infected mice and controls. We identified Cst7, which encodes cystatin F, as the most strongly upregulated transcript in this model. Early and robust upregulation of Cst7 mRNA levels and of its cognate protein was validated in additional mouse models of prion disease. Surprisingly, we found no significant increase in cystatin F levels in both cerebrospinal fluid or brain parenchyma of patients with Creutzfeldt-Jakob disease compared to Alzheimer's disease or non-demented controls. Our results validate cystatin F as a useful biomarker of early pathogenesis in experimental models of prion disease, and point to unexpected species-specific differences in the transcriptional responses to prion infections.
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In humans, CST7 is expressed in endothelial cells in addition to microglia and macrophages.
“In humans, CST7 is expressed in endothelial cells in addition to microglia and macrophages.36”
From Microglial <i>INPP5D</i> limits plaque formation and glial reactivity in the PSAPP mouse model of Alzheimer's disease (2023) · cites this paper as [36]
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Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A., & Speleman, F. (2002) · Genome Biology · doi:10.1186/gb-2002-3-7-research0034 · Cited by 20,038 · see citing works
Novel Proteinaceous Infectious Particles Cause Scrapie
Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,121 · see citing works
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875 · see citing works
Of Mice and Not Men: Differences between Mouse and Human Immunology
Mestas, J., & Hughes, C. C. W. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.5.2731 · Cited by 3,822 · see citing works
Genomic responses in mouse models poorly mimic human inflammatory diseases
Seok, J., Warren, H. S., Cuenca, A. G., Mindrinos, M. N., Baker, H. V., Xu, W., Richards, D. R., McDonald-Smith, G. P., Gao, H., Hennessy, L., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1222878110 · Cited by 3,005 · see citing works
Montine, T. J., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., Mirra, S. S., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0910-3 · Cited by 2,992 · cited 2× · see citing works
“Neuropathologic assessment of Alzheimer type brain pathology was made according to the NIA/AA criteria [7].”
BackgroundMethodZhang, Y., Sloan, S. A., Clarke, L. E., Caneda, C., Plaza, C. A., Blumenthal, P. D., Vogel, H., Steinberg, G. K., Edwards, M. S. B., Li, G., et al. (2016) · Neuron · doi:10.1016/j.neuron.2015.11.013 · Cited by 2,295 · see citing works
Gene regulation and DNA damage in the ageing human brain
Lu, T., Pan, Y., Kao, S.-Y., Li, C., Kohane, I., Chan, J., & Yankner, B. A. (2004) · Nature · doi:10.1038/nature02661 · Cited by 1,874 · see citing works
New tools for studying microglia in the mouse and human CNS
Bennett, M. L., Bennett, F. C., Liddelow, S. A., Ajami, B., Zamanian, J. L., Fernhoff, N. B., Mulinyawe, S. B., Bohlen, C. J., Adil, A., Tucker, A., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1525528113 · Cited by 1,804 · see citing works
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507 · see citing works
Molecular basis of phenotypic variability in sporadc creudeldt‐jakob disease
Parchi, P., Castellani, R., Capellari, S., Ghetti, B., Young, K., Chen, S. G., Farlow, M., Dickson, D. W., Sima, A. A. F., Trojanowski, J. Q., et al. (1996) · Annals of Neurology · doi:10.1002/ana.410390613 · Cited by 864 · see citing works
The Blood-Brain Barrier in Brain Homeostasis and Neurological Diseases
Weiss, N., Miller, F., Cazaubon, S., & Couraud, P.-O. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.022 · Cited by 731 · see citing works
Shmerling, D., Hegyi, I., Fischer, M., Blättler, T., Brandner, S., Götz, J., Rülicke, T., Flechsig, E., Cozzio, A., von Mering, C., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81572-x · Cited by 530 · see citing works
Self-citationPrions: Protein Aggregation and Infectious Diseases
Aguzzi, A., & Calella, A. M. (2009) · Physiological Reviews · doi:10.1152/physrev.00006.2009 · Cited by 502 · see citing works
Self-citationPathogenesis of bacterial meningitis: from bacteraemia to neuronal injury
Kim, K. S. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1103 · Cited by 431 · see citing works
Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping.
Janowski, R., Kozak, M., Jankowska, E., Grzonka, Z., GRUBB, A. O., Abrahamson, M., & Jaskólski, M. (2001) · Nature Structural Biology · doi:10.1038/86188 · Cited by 395 · see citing works
Insights into prion strains and neurotoxicity
Aguzzi, A., Heikenwälder, M. F., & Polymenidou, M. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2204 · Cited by 327 · see citing works
Self-citationDoh‐ura, K., Iwaki, T., & Caughey, B. W. (2000) · Journal of Virology · doi:10.1128/jvi.74.10.4894-4897.2000 · Cited by 323 · see citing works
Diedrich, J. F., Minnigan, H. J., Carp, R. I., Whitaker, J. N., Race, R., Frey, W. H., & Haase, A. T. (1991) · Journal of Virology · doi:10.1128/jvi.65.9.4759-4768.1991 · Cited by 295 · see citing works
A systems approach to prion disease
Hwang, D., Lee, I. Y., Yoo, H., Gehlenborg, N., Cho, J., Petritis, B., Baxter, D., Pitstick, R., Young, R., Spicer, D., et al. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.10 · Cited by 287 · see citing works
Smith, A. M., & Dragunow, M. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2013.12.001 · Cited by 256 · cited 1× · see citing works
“Multiple divergent molecular pathways in immune cells have been described, including for macrophages [55] and microglia [56].”
BackgroundParchi, P., de Boni, L., Saverioni, D., Cohen, M. L., Ferrer, I., Gambetti, P. L., Gelpí, E., Giaccone, G., Hauw, J., Höftberger, R., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1002-8 · Cited by 228 · see citing works
MUTATION IN CYSTATIN C GENE CAUSES HEREDITARY BRAIN HAEMORRHAGE
Palsdottir, A., Thorsteinsson, L., Olafsson, I., Abrahamson, M., Arnason, A., Grubb, A., & Jensson, O. (1988) · The Lancet · doi:10.1016/s0140-6736(88)90641-1 · Cited by 212 · see citing works
Becher, B., Durell, B. G., Miga, A. V., Hickey, W. F., & Noelle, R. J. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.8.967 · Cited by 210 · see citing works
Letter: The handicapped family.
Caplan, M. B., & Antonis, P. (1975) · PubMed · Cited by 194 · see citing works
Cystatin C inhibits amyloid-β deposition in Alzheimer's disease mouse models
Mi, W., Pawlik, M., Sastre, M., Jung, S. S., Radvinsky, D. S., Klein, A. M., Sommer, J., Schmidt, S. D., Nixon, R. A., Mathews, P. M., et al. (2007) · Nature Genetics · doi:10.1038/ng.2007.29 · Cited by 189 · see citing works
The POM Monoclonals: A Comprehensive Set of Antibodies to Non-Overlapping Prion Protein Epitopes
Polymenidou, M., Moos, R., Scott, M., Sigurdson, C. J., Shi, Y., Yajima, B., Hafner‐Bratkovič, I., Jerala, R., Hornemann, S., Kurt Wüthrich, A., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003872 · Cited by 181 · see citing works
Self-citationLevy, E., López-Otı́n, C., Ghiso, J. A., Geltner, D., & Frangione, B. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.5.1771 · Cited by 180 · see citing works
Isolation of human monoclonal antibodies by mammalian cell display
Beerli, R. R., Bauer, M., Buser, R. B., Gwerder, M., Muntwiler, S., Maurer, P., Saudan, P., & Bachmann, M. F. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805942105 · Cited by 175 · see citing works
Self-citationPreclinical Alzheimer's disease: diagnosis and prediction of progression
Chong, M. S., & Sahadevan, S. (2005) · The Lancet Neurology · doi:10.1016/s1474-4422(05)70168-x · Cited by 173 · see citing works
Unique inflammatory RNA profiles of microglia in Creutzfeldt–Jakob disease
Baker, C. A., & Manuelidis, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0237313100 · Cited by 165 · see citing works
Stoeck, K., Sánchez‐Juan, P., Gawinecka, J., Green, A. J. E., Ladogana, A., Pocchiari, M., Sánchez‐Valle, R., Mitrova, E., Sklaviadis, T., Kulczycki, J., et al. (2012) · Brain · doi:10.1093/brain/aws238 · Cited by 161 · see citing works
Self-citationCystatin F Is a Glycosylated Human Low Molecular Weight Cysteine Proteinase Inhibitor
Ni, J., Fernandez, M. A., Danielsson, L., Chillakuru, R. A., Zhang, J., GRUBB, A. O., Su, J. Y., Gentz, R., & Abrahamson, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.38.24797 · Cited by 156 · see citing works
Xiang, W., Windl, O., Wünsch, G., Dugas, M., Kohlmann, A., Dierkes, N., Westner, I. M., & Kretzschmar, H. A. (2004) · Journal of Virology · doi:10.1128/jvi.78.20.11051-11060.2004 · Cited by 150 · see citing works
Binding of cystatin C to Alzheimer’s amyloid β inhibits in vitro amyloid fibril formation
Sastre, M., Calero, M., Pawlik, M., Mathews, P. M., Kumar, A. R., Danilov, V., Schmidt, S. D., Nixon, R. A., Frangione, B., & Levy, E. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.11.006 · Cited by 148 · see citing works
The immunobiology of prion diseases
Aguzzi, A., Nuvolone, M., & Zhu, C. (2013) · Nature reviews. Immunology · doi:10.1038/nri3553 · Cited by 146 · see citing works
Self-citationBiobanking of CSF: International standardization to optimize biomarker development
Teunissen, C. E., Tumani, H., Engelborghs, S., & Mollenhauer, B. (2014) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2013.12.024 · Cited by 137 · see citing works
A neuroprotective role for microglia in prion diseases
Zhu, C., Herrmann, U. S., Falsig, J., Abakumova, I., Nuvolone, M., Schwarz, P., Frauenknecht, K., Rushing, E. J., & Aguzzi, A. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151000 · Cited by 134 · see citing works
Self-citationAdvanced tests for early and accurate diagnosis of Creutzfeldt–Jakob disease
Zanusso, G., Monaco, S., Pocchiari, M., & Caughey, B. W. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2016.65 · Cited by 129 · see citing works
Strictly co-isogenic C57BL/6J- Prnp −/− mice: A rigorous resource for prion science
Nuvolone, M., Hermann, M., Sorce, S., Russo, G., Tiberi, C., Schwarz, P., Minikel, E. V., Sanoudou, D., Pelczar, P., & Aguzzi, A. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151610 · Cited by 127 · see citing works
Self-citationSpecies differences in macrophage NO production are important
Schneemann, M., & Schoedon, G. (2002) · Nature Immunology · doi:10.1038/ni0202-102a · Cited by 124 · see citing works
Cystatin F is a cathepsin C‐directed protease inhibitor regulated by proteolysis
Hamilton, G., Colbert, J. D., Schuettelkopf, A. W., & Watts, C. K. W. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601979 · Cited by 120 · see citing works
Stilling, R. M., Benito, E., Barth, J., Gertig, M., Capece, V., Burckhardt, S., Bonn, S., & Fischer, A. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00373 · Cited by 111 · see citing works
Leukocystatin, A New Class II Cystatin Expressed Selectively by Hematopoietic Cells
Halfon, S., Ford, J., Foster, J., Dowling, L., Lucian, L. A., Sterling, M., Xu, Y., Weiss, M., Ikeda, M., Liggett, D., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16400 · Cited by 110 · see citing works
Gene expression profiling of scrapie-infected brain tissue
Riemer, C., Neidhold, S., Burwinkel, M., Schwarz, A., Schultz, J., Krätzschmar, J., Mönning, U., & Baier, M. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.124 · Cited by 108 · see citing works
Determination of reference genes for circadian studies in different tissues and mouse strains
Košir, R., Ačimovič, J., Goličnik, M., Perše, M., Majdič, G., Fink, M., & Rozman, D. (2010) · BMC Molecular Biology · doi:10.1186/1471-2199-11-60 · Cited by 94 · see citing works
Microglial Activation Varies in Different Models of Creutzfeldt-Jakob Disease
Baker, C. A., Lu, Z.-Y., Zaitsev, I., & Manuelidis, L. (1999) · Journal of Virology · doi:10.1128/jvi.73.6.5089-5097.1999 · Cited by 91 · see citing works
Kovács, G. G., Gelpí, E., Ströbel, T., Ricken, G., Nyengaard, J. R., Bernheimer, H., & Budka, H. (2007) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318093ecc7 · Cited by 79 · see citing works
Self-citationMolecular pathology, classification, and diagnosis of sporadic human prion disease variants.
Parchi, P., & Saverioni, D. (2012) · PubMed · Cited by 72 · see citing works
Subtype and Regional-Specific Neuroinflammation in Sporadic Creutzfeldt–Jakob Disease
Llorens, F., López-González, I., Thüne, K., Carmona, M., Zafar, S., Andréoletti, O., Zerr, I., & Ferrer, I. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00198 · Cited by 69 · see citing works
Ma, J.-M., Tanaka, K., Shimizu, T., Bernard, C., Kakita, A., Takahashi, H., Pfeiffer, S., & Ikenaka, K. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22567 · Cited by 67 · see citing works
SIRPα polymorphisms, but not the prion protein, control phagocytosis of apoptotic cells
Nuvolone, M., Kana, V., Hütter, G., Sakata, D., Mortin-Toth, S. M., Russo, G., Danska, J. S., & Aguzzi, A. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20131274 · Cited by 67 · see citing works
Self-citationThe Role of the NADPH Oxidase NOX2 in Prion Pathogenesis
Sorce, S., Nuvolone, M., Keller, A., Falsig, J., Varol, A., Schwarz, P., Bieri, M., Budka, H., & Aguzzi, A. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004531 · Cited by 62 · see citing works
Self-citationLuhr, K. M., Nordström, E. K., Löw, P., Ljunggren, H., Taraboulos, A., & Kristensson, K. (2004) · Journal of Virology · doi:10.1128/jvi.78.9.4776-4782.2004 · Cited by 51 · see citing works
Cystatin F Ensures Eosinophil Survival by Regulating Granule Biogenesis
Matthews, S. P., McMillan, S. J., Colbert, J. D., Lawrence, R. A., & Watts, C. K. W. (2016) · Immunity · doi:10.1016/j.immuni.2016.03.003 · Cited by 41 · see citing works
Xiang, W., Hummel, M., Mitteregger, G., Pace, C., Windl, O., Mansmann, U., & Kretzschmar, H. A. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04566.x · Cited by 41 · see citing works
Cathepsin B and L are involved in degradation of prions in GT1-1 neuronal cells
Luhr, K. M., Nordström, E. K., Löw, P., & Kristensson, K. (2004) · Neuroreport · doi:10.1097/01.wnr.0000134931.81690.34 · Cited by 41 · see citing works
Prion Pathogenesis in the Absence of NLRP3/ASC Inflammasomes
Nuvolone, M., Sorce, S., Schwarz, P., & Aguzzi, A. (2015) · PLOS ONE · doi:10.1371/journal.pone.0117208 · Cited by 39 · see citing works
Self-citationUp-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells
Zhang, Y., Spieß, E., Groschup, M. H., & Bürkle, A. (2003) · Journal of General Virology · doi:10.1099/vir.0.19153-0 · Cited by 36 · see citing works
Urinary α1-Antichymotrypsin: A Biomarker of Prion Infection
Miele, G., Seeger, H., Marino, D., Eberhard, R., Heikenwälder, M. F., Stoeck, K., Basagni, M., Knight, R., Green, A. J. E., Chianini, F., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003870 · Cited by 33 · see citing works
Self-citationA high-throughput alphavirus-based expression cloning system for mammalian cells
Koller, D., Ruedl, C., Loetscher, M., Vlach, J., Oehen, S., Oertle, K., Schirinzi, M., Deneuve, E., Moser, R., Köpf, M., et al. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-851 · Cited by 29 · see citing works
Morita, M., Hara, Y., Tamai, Y., Arakawa, H., & Nishimura, S. (2000) · Genomics · doi:10.1006/geno.2000.6237 · Cited by 28 · see citing works
Duan, W., Ran, H., Zhou, Z., He, Q., & Zheng, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052566 · Cited by 21 · see citing works
Expression Profiling Using Affymetrix GeneChip® Probe Arrays
Schinke-Braun, M., & Couget, J. A. (2007) · Methods in molecular biology · doi:10.1007/978-1-59745-030-0_2 · Cited by 14 · see citing works
Unaltered Prion Pathogenesis in a Mouse Model of High-Fat Diet-Induced Insulin Resistance
Zhu, C., Schwarz, P., Abakumova, I., & Aguzzi, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0144983 · Cited by 13 · see citing works
Self-citationVidal, E., Tortosa, R., Marco-Salazar, P., Fondevila, D., Rabanal, R. M., Torres, J. M., & Pumarola, M. B. (2012) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2012.05.004 · Cited by 5 · see citing works
Beasley, T. M., Holt, J. K., & Allison, D. B. (2005) · American Journal of PharmacoGenomics · doi:10.2165/00129785-200505030-00006 · Cited by 3 · see citing works
Flagged first, then by citations
1 of the 68 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Necroptosis and RIPK1-mediated neuroinflammation in CNS diseases
Yuan, J., Amin, P., & Ofengeim, D. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0093-1 · Cited by 967 · see citing works
Targeting RIPK1 for the treatment of human diseases
Degterev, A., Ofengeim, D., & Yuan, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901179116 · Cited by 411 · see citing works
RIPK1 mediates a disease-associated microglial response in Alzheimer’s disease
Ofengeim, D., Mazzitelli, S., Ito, Y., DeWitt, J. P., Mifflin, L., Zou, C., Das, S., Adiconis, X., Chen, H., Zhu, H., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1714175114 · Cited by 395 · see citing works
Automated Detection of Alzheimer’s Disease and Mild Cognitive Impairment Using Whole Brain MRI
Faisal, F. U. R., & Kwon, G. (2022) · IEEE Access · doi:10.1109/access.2022.3180073 · Cited by 94 · see citing works
Castranio, E. L., Hasel, P., Haure‐Mirande, J., Ramirez Jimenez, A. V., Hamilton, B. W., Kim, R. D., Glabe, C. G., Wang, M., Zhang, B., Gandy, S., et al. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.12821 · Cited by 74 · see citing works
Liu, Y., Sorce, S., Nuvolone, M., Domange, J., & Aguzzi, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-32712-8 · Cited by 53 · see citing works
Self-citationWang, H., Qi, W., Zou, C., Xie, Z., Zhang, M., Naito, M. G., Mifflin, L., Liu, Z., Najafov, A., Pan, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25157-7 · Cited by 52 · see citing works
Microglia control small vessel calcification via TREM2
Zarb, Y., Sridhar, S., Nassiri, S., Utz, S. G., Schaffenrath, J., Maheshwari, U., Rushing, E. J., Nilsson, K. P. R., Delorenzi, M., Colonna, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abc4898 · Cited by 44 · see citing works
Self-citationDaniels, M. J. D., Lefèvre, L., Szymkowiak, S., Drake, A., McCulloch, L. J., Tzioras, M., Barrington, J., Dando, O., He, X., Mohammad, M., et al. (2023) · eLife · doi:10.7554/elife.85279 · Cited by 28 · see citing works
RIPK1 promotes inflammation and β-amyloid accumulation in Alzheimer’s disease
Rubinsztein, D. C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715241114 · Cited by 23 · see citing works
Core transcriptional regulatory circuits in prion diseases
Kim, T., Lee, I., Cho, J.-H., Canine, B., Keller, A., Price, N. D., Hwang, D., Carlson, G. A., & Hood, L. (2020) · Molecular Brain · doi:10.1186/s13041-020-0551-3 · Cited by 20 · see citing works
Maniwa, K., Yano, S., Sheikh, A. M., Onoda, K., Mitaki, S., Isomura, M., Mishima, S., Yamaguchi, S., Nabika, T., & Nagai, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-61383-7 · Cited by 17 · see citing works
Cystatin F acts as a mediator of immune suppression in glioblastoma
Senjor, E., Nanut, M. P., Breznik, B., Mitrović, A., Mlakar, J., Rotter, A., Porčnik, A., Turnšek, T. L., & Kos, J. (2021) · Cellular Oncology · doi:10.1007/s13402-021-00618-9 · Cited by 16 · see citing works
Microglia contribute to polyG-dependent neurodegeneration in neuronal intranuclear inclusion disease
Zhong, S., Lian, Y., Zhou, B., Ren, R., Duan, L., Pan, Y., Gong, Y., Wu, X., Cheng, D., Zhang, P.-M., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02776-0 · Cited by 15 · see citing works
Prion pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling
Nuvolone, M., Paolucci, M., Sorce, S., Kana, V., Moos, R., Matozaki, T., & Aguzzi, A. (2017) · PLOS ONE · doi:10.1371/journal.pone.0177876 · Cited by 13 · see citing works
Self-citationPrion pathogenesis is unaltered in a mouse strain with a permeable blood-brain barrier
Keller, A., Nuvolone, M., Abakumova, I., Chincisan, A., Reimann, R., Avar, M., Heinzer, D., Hornemann, S., Wagner, J., Kirschenbaum, D., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007424 · Cited by 11 · see citing works
Self-citationSingle-Cell RNA-seq reveals transcriptomic modulation of Alzheimer’s disease by activated protein C
Fatmi, M. K., Wang, H., Slotabec, L. A., Wen, C., Seale, B. C., Zhao, B., & Li, J. (2024) · Aging · doi:10.18632/aging.205624 · Cited by 10 · see citing works
Gao, S., Chen, Z., Shi, J. R., Chen, Z., Yun, D., Li, X., Wu, X., & Sun, F. (2023) · The FASEB Journal · doi:10.1096/fj.202201862rr · Cited by 7 · see citing works
Cystatin F-a key player in central nervous system disease
Wang, Y.-T., Li, Q., Liu, J., Chen, C., Ding, H.-X., Zha, X., & Zhang, K. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03526-z · Cited by 5 · see citing works
Sheshe, S. M. (2018) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-5225-5282-6.ch017 · Cited by 4 · see citing works
Xu, S., Wang, Y., Han, C., Jiang, Y., Qin, Q., & Wei, S. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.09.003 · Cited by 3 · see citing works
Liu, Y., Sorce, S., Nuvolone, M., Domange, J., & Aguzzi, A. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/291401 · Cited by 3 · see citing works
Self-citationSheshe, S. M. (2020) · IGI Global eBooks · doi:10.4018/978-1-7998-3441-0.ch003 · Cited by 1 · see citing works
APOE genotype differentially modulates prion pathology in a mouse model
Lizińczyk, A. M., Pankiewicz, J. E., Cullina, W. L., Franco, L. A., Sullivan, P. M., & Sadowski, M. J. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02207-5
Hemonnot-Girard, A.-L. (2021) · theses.fr (ABES) · doi:10.70675/9c8a4775zd774z494ez9bbazf7566faefa8f
- Authors
- Nuvolone, M., Schmid, N., Miele, G., Sorce, S., Moos, R., Schori, C., Beerli, R. R., Bauer, M., Saudan, P., Dietmeier, K., Lachmann, I., Linnebank, M., Martin, R., Kallweit, U., Kana, V., Rushing, E. J., Budka, H., & Aguzzi, A.
- Affiliations
- University Hospital Zurich (CH)
- University of Bern (CH)
- Corresponding author
- Aguzzi, Adriano
- ORCID
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2017-02-08
- Volume
- 12
- Issue
- 2
- Pages
- e0171923
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC5298286
- OpenAlex
- W2586358468
- Cited by
- 25
- References
- 68
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 4 · 2020: 3 · 2019: 1 · 2018: 5 · 2017: 3
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, cc-by)
- BORIS (University Library Bern) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Zurich Open Repository and Archive (University of Zurich) (submittedVersion, cc-by-nc-nd)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- European Commission
- SystemsX.ch
- FP7 Ideas: European Research Council (250356)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Keywords
- cystatin F, prion disease, prion pathogenesis, biomarkers, cellular prion protein, scrapie, Creutzfeldt-Jakob disease, pre-symptomatic infection, gene expression profiling, cerebrospinal fluid, species differences, mouse model
- MeSH terms
- Animals, Brain, Enzyme-Linked Immunosorbent Assay, Humans, Immunohistochemistry, Male, RNA, Messenger, Biomarkers, Gene Expression, Cystatins, Prion Diseases, Gene Expression Profiling, Mice
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