Pritzkow S, Morales R, Moda F, Telling GC, Hoover E, and Soto, C. (2015) Grass plants bind, retain, uptake, and transport infectious prions. Cell Rep. 2015 May26:11(8):1168-75. http://www.ncbi.nlm.nih.gov/pubmed/25981035
Morales, R., Bravo-Alegria, J., Duran-Aniotz, C. and Soto, C. (2015) Titration of biologically active amyloid–β seeds in a transgenic mouse model of Alzheimer’s disease. Scientific Reports 5:9349. http://www.ncbi.nlm.nih.gov/pubmed/25879692
Moda, F., Gambetti, P., Notari, S., Concha-Marambio, L., Catania, M., Park, K.W., Maderna, E., Suardi, S., Haïk, S., Brandel, J.P., Ironside, J., Knight, R., Tagliavini, F., Soto, C. (2014) Prions in the urine of patients with variant Creutzfeldt-Jakob disease. N Engl J Med. 371(6):530-9. http://www.ncbi.nlm.nih.gov/pubmed/25099577
Salvadores, N., Shahnawaz, M., Scarpini, E., Tagliavini, F., Soto, C. (2014) Detection of misfolded Aβ oligomers for sensitive biochemical diagnosis of Alzheimer’s disease. Cell Rep. 7(1):261-8. http://www.ncbi.nlm.nih.gov/pubmed/24656814
Moreno-Gonzalez, I., Estrada, L.D., Sanchez-Mejias, E. and Soto, C. (2013) Smoking exacerbates amyloid pathology in a mouse model of Alzheimer’s disease. Nature Communications 4: 1495. http://www.ncbi.nlm.nih.gov/pubmed/23422663
Morales, R., Duran-Aniotz C, Castilla, J., Estrada, L.D., and Soto, C. (2012) De novo induction of amyloid-B deposition in vivo. Mol. Psych. 17(12):1347-53. http://www.ncbi.nlm.nih.gov/pubmed/21968933
Chen, B., Morales, R., Barria, M.A. and Soto, C. (2010) Estimating prion concentration in fluids and tissues by quantitative PMCA. Nature methods 7: 519-521. http://www.ncbi.nlm.nih.gov/pubmed/20512142
Castilla, J., Gonzalez, D., Saa, P., Morales, R., De Castro, J. and Soto, C. (2008) Crossing the species barrier by PrP(Sc) replication in vitro generates unique infectious prions. Cell. 134:757-768, 2008. http://www.ncbi.nlm.nih.gov/pubmed/18775309
Saborio, G.P., Permanne, B. and Soto, C. (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature. 411:810-813. http://www.ncbi.nlm.nih.gov/pubmed/11459061
Soto, C., Kascsak, R.J., Saborio, G., Aucouturier, P., Wisniewski, T., Prelli, F., R. Kascsak, Mendez, E., Harris, D.A., Ironside, J., Tagliavini, F., Carp, R.I. & Frangione, B. (2000) Reversion of prion protein conformational changes by synthetic ß-sheet breaker peptides. The Lancet. 355:192-197. http://www.ncbi.nlm.nih.gov/pubmed/10675119
Soto, C., Sigursson, E., Morelli, L., Kumar, R.A., Castaño, E.M. and Frangione, B. (1998) ß-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer’s therapy. Nature Med. 4(7):822-826. http://www.ncbi.nlm.nih.gov/pubmed/9662374
All Publications
Mukherjee A, Morales, R., Moda, F., Telling, G.C., Hoover, E. and Soto, C. (2015) Prion contaminated plants transmit prion disease. Cell Reports 11(8):1168-75.
Torres M, Medinas DB, Matamala JM, Woehlbier U, Cornejo VH, Solda T, Andreu C, Rozas P, Matus S, Muñoz N, Vergara C, Cartier L, Soto C, Molinari M, Hetz C. (2015) The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein. J Biol Chem. 290(39):23631-45.
Pritzkow, S, Morales, R, Moda, F, Telling, GC, Hoover, E and Soto, C (2015) Prion contaminated plants transmit prion disease. Cell Reports 11(8):1168-75.
Mukherjee, A., Morales-Scheihing, D., Butler, P.C., and Soto, C. (2015) Type 2 Diabetes as a Protein Misfolding Disease. Trends Mol. Med. 21(7):439-49.
Maheshwari A, Fischer M, Gambetti P, Parker A, Ram A, Soto C, Concha-Marambio L, Cohen Y, Belay ED, Maddox RA, Mead S, Goodman C, Kass JS, Schonberger LB, Hussein HM. (2015) Recent US Case of Variant Creutzfeldt-Jakob Disease-Global Implications. Emerg Infect Dis. 21(5):750-9.
Morales R, Bravo-Alegria J, Duran-Aniotz C, Soto C. (2015) Titration of biologically active amyloid-β seeds in a transgenic mouse model of Alzheimer’s disease. Sci Rep. 5:9349.
Morales R, Callegari K, Soto C. Prion-like features of misfolded Aβ and tau aggregates. (2015) Virus Res. S0168-1702(14)00545-0.
Moda, F., Gambetti, P., Notari, S., Concha-Marambio, L., Catania, M., Park, K.W., Maderna, E., Suardi, S., Haïk, S., Brandel, J.P., Ironside, J., Knight, R., Tagliavini, F., Soto, C. (2014) Prions in the urine of patients with variant Creutzfeldt-Jakob disease. N Engl J Med. 371(6):530-9.
Salvadores N, Shahnawaz M, Scarpini E, Tagliavini F, Soto C. (2014) Detection of misfolded Aβ oligomers for sensitive biochemical diagnosis of Alzheimer’s disease. Cell Rep. 10;7(1):261-8.
Armijo, E., Soto, C., Davis, B.R. (2014) HIV/AIDS: modified stem cells in the spotlight. Cell Mol Life Sci. 71(14):2641-9.
Soto, C. (2014) The Story of the Rogue Prions. Nature Medicine 20: 1089.
Chen, B., Soto, C., Morales, R. (2014) Peripherally administrated prions reach the brain at sub-infectious quantities in experimental hamsters. FEBS Lett. 588(5):795-800.
Concha-Marambio, L., Diaz-Espinoza, R., Soto, C. (2014) The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. J Biol Chem. 289(5):3073-9.
Duran-Aniotz, C., Morales, R., Moreno-Gonzalez, I., Hu, P.P., Fedynyshyn, J., Soto, C. (2014) Aggregate-depleted brain fails to induce Aβ deposition in a mouse model of Alzheimer’s disease. PLoS One. 9(2):e89014.
Duran-Aniotz, C., Morales, R., Moreno-Gonzalez, I., Hu, P.P., Soto, C. (2013) Brains from non-Alzheimer’s individuals containing amyloid deposits accelerate Aβ deposition in vivo. Acta Neuropathol Commun. 1(1):76.
Morales, R., Moreno-Gonzalez, I., Soto, C. (2013) Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog. 9(9):e1003537.
Soto, C. (2013) Protein Misfolding in Neurodegenerative Diseases: The Key Pending Questions. J. Neurol. Transl. Neurosci. 1: 1010-1013.
Morales, R., Pritzkow, S., Hu, P.P., Duran-Aniotz, C., Soto, C. (2013) Lack of prion transmission by sexual or parental routes in experimentally infected hamsters. Prion. 7(5):412-9.
Cuanalo-Contreras, K., Mukherjee, A., Soto, C. (2013) Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging. Int J Cell Biol. 2013:638083.
Moreno-Gonzalez, I., Estrada, L.D., Sanchez-Mejias, E., Soto, C. (2013) Smoking exacerbates amyloid pathology in a mouse model of Alzheimer’s disease. Nat Commun. 4:1495.
Morales, R., Duran-Aniotz C, Castilla, J., Estrada, L.D., Soto, C. (2012) De novo induction of amyloid-B deposition in vivo. Mol Psych. 17(12):1347-53.
Morales, R., Duran-Aniotz, C., Diaz-Espinoza, R., Camacho, M., Soto, C. (2012) Protein misfolding cyclic amplification of infectious prions. Nat Protoc. 7(7):1397-409.
Soto, C. (2012) Transmissible proteins: expanding the prion heresy. Cell. 149(5):968-77.
Shahnawaz, M., Soto, C. (2012) Microcin amyloid fibrils A are reservoir of toxic oligomeric species. J Biol Chem. 287(15):11665-76.
Diaz-Espinoza, R. and Soto, C. (2012) High-resolution Structure of Infectious Prion Protein: the final frontier. Nature Struct Mol Biol. 19(4):370-7.
Soto, C. (2012) In vivo spreading of tau pathology. Neuron. 73(4):621-3.
Moreno-Gonzalez, I and Soto, C. (2012) Natural Animal Models of Neurodegenerative Protein Misfolding Diseases. Curr Pharm Des. 18(8):1148-58.
Barria, M.A., Gonzalez-Romero, D., Soto, C. (2012) Cyclic amplification of prion protein misfolding. Methods Mol Biol. 849:199-212.
Diaz-Espinoza, R., Mukherjee, A. and Soto, C. (2012) Kosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded form. PLoS ONE. 7(2):e31678.
Morales, R., Duran-Aniotz, C., Castilla, J., Estrada, L.D., and Soto, C. (2011) De novo induction of amyloid-b deposition in vivo. Mol. Psych. Advanced Online Publication October 4, 2011 (DOI 10.1038/mp.2011.120)
Moreno-Gonzalez, I. and Soto, C. (2011) Misfolded Protein Aggregates: Mechanisms, Structures and Potential for Disease Transmission. Seminars Cell Biol. 22: 482-487
Torres, M., Encina, G., Soto, C. and Hetz, C. (2011). Abnormal calcium homeostasis and protein folding stress at the ER: a common factor in familial and infectious prion disorders. Commun. Integr. Biol. 4: 258-261.
Urayama, A., Morales, R., Niehoff, M.I., Banks, W.A. and Soto, C. (2011) Initial Fate of Prions upon Peripheral Infection: Half-life, Distribution, Clearance, and Tissue Uptake. FASEB J. 25: 2792-2803.
Soto, C. (2011) Prion Hypothesis: The End of the Controversy? Trends Biochem. Sci. 36: 151-158. Article selected for cover page.
Barria, M.A., Telling, G.C., Gambetti, P., Mastrianni, J.A. and Soto, C. (2011) Generation of a new form of human PrPSc in vitro by inter-species transmission from cervids prions. J. Biol. Chem. 286: 7490-7495.
Mukherjee, A. and Soto, C. (2011) Role of Calcineurin in Neurodegeneration Induced by Brain Accumulation of Misfolded Proteins. Curr. Op. Cell Biol. 23: 223-230.
Soto, C. and Satani, N. (2011) The Intricate Mechanisms of Neurodegeneration in Prion Diseases. Trends Mol. Med. 17: 14-24.
Torres, M., Castillo, K., Armisen, R., Stutzin, A., Soto, C. and Hetz, C. (2010) Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS One 5: e15658.
Mukherjee, A., Morales-Scheihing, D., Gonzalez-Romero, D., Green, K., Taglialatela, G. and Soto, C. (2010) Calcineurin Inhibition at the Clinical Phase of Prion Disease Decreases Neurodegeneration leading to clinical Improvement and Increase of Animal Survival. PLoS Pathogen 6: e1001138.
Diaz-Espinoza, R. and Soto, C. (2010) Generation of prions in vitro and the protein-only hypothesis. Prions 4: 53-59.
Chen, B., Morales, R., Barria, M.A. and Soto, C. (2010) Estimating prion concentration in fluids and tissues by quantitative PMCA. Nature meth. 7: 519-521.
Angers, R.C., Kang, H., Napier, D., Browning, S., Seward, T., Mathiason, C., Balachandran, A., McKenzie, D., Castilla, J., Soto, C., Jewell, J., Graham, C., Hoover, E.A. and Telling, G.C. (2010) Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science 328: 1154-1158. (Highlighted in Science)
Abid, K., Morales, R. and Soto, C. (2010) Cellular factors implicated in prion replication. FEBS Lett 584: 2409-2414.
Morales, R., Estrada, L.D., Diaz-Espinoza, R., Morales-Scheihing, D., Jara, M.C., Castilla, J. and Soto, C. (2010) Molecular cross-talk between misfolded proteins in animal models of Alzheimer’s and Prion diseases. J. Neurosci. 30: 4528-4525.
Lasagna-Reeves, C., Gonzalez-Romero, D., Barria, M., Olmedo, I., Clos, A., Sadagopa Ramanujam, V.M., Urayama, A., Vergara, L., Kogan, M.J. and Soto, C. (2010) Bioaccumulation and Toxicity of Gold Nanoparticles after Repeated Administration in Mice. Biochem. Biophys. Res. Commun. 393: 649-655.
Morales, R., Green, K. and Soto, C. (2009) Cross-currents in Protein Misfolding Disorders: Interaction and Therapy. CNS & Neurol. Dis. Drug Targets 8: 363-371.
Fernandez-Funez, P., Casas-Tinto, P., Zhang, Y., Gómez-Velázquez, M., Morales-Garza, M.A., Cepeda-Nieto, A.C., Castilla, J., Soto, C. and Rincon-Limas, D.E. (2009) In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded Isoforms. PLoS Genetics 5(6): e1000507.
Banks, W.A., Robinson, S.M., Diaz-Espinoza, R., Urayama, A. and Soto, C. (2009) Transport of prion protein across the blood brain barrier. Exp Neurol. 218: 162-167.
Chen, D., Martin, Z., Soto, C. and Schein, C.H. (2009) Computational Selection of Inhibitors of A-beta Aggregation and Neuronal Toxicity. Biorg. Med Chem. 17: 5189-5197.
Barria, M.A., Mukherjee, A., Gonzalez-Romero, D., Morales, R. and Soto, C. (2009) De novo generation of infectious prions in vitro produces a new disease. PLoS Pathogen 5:e1000421. Highlighted in Nature Methods.
Piro, J.R., Harris, B.T., Nishina, K., Soto, C., Morales, R., Rees, J.R. and Supattapone, S. (2009) Prion Protein Glycosylation is not Required for Strain-Specific Neurotropism. J. Virol. 83: 5321-5328.
Soto, C. (2009) Constraining the loop, releasing prion infectivity. Proc Natl. Acad. Sci. USA 106: 10-11.
Soto, C., Martin, Z. (2009). Therapeutic strategies against protein misfolding in neurodegenerative diseases. Exp. Op. Drug Disc. 4: 71-84.
Castilla, J., Gonzalez, D., Saa, P., Morales, R., De Castro, J. and Soto, C. (2008) Crossing the species barrier by PrPSc replication in vitro generates new infectious prions. Cell 134: 757-768. Highlighted in Nature, Science, Nature Neuroscience, nature Medicine.
Soto, C. (2008) Endoplasmic reticulum stress, PrP trafficking and Neurodegeneration. Dev. Cell 15: 339-341.
Castilla, J., Morales, R., Saa, P., Barria, M., Gambetti, P. and Soto, C. (2008) Propagation of prion strains in vitro. EMBO J. 27: 2557-2566.
Morales R., Buytaert-Hoefen K.A., Gonzalez-Romero D., Castilla J., Hansen E.T., Hlavinka D., Goodrich R.P. and Soto C. (2008) Reduction of prion infectivity in packed red blood cells. Biochem. Biophys. Res. Commun. 377: 373-378.
Gonzalez-Romero, D., Barria, M., Leon, P., Morales, R., and Soto, C. (2008) Detection of infectious prions in urine. FEBS Lett. 582: 3161-3166.
Green, K.M., Castilla, J., Seward, T.S., Ross, D.L., Jewell, J., Soto, C. and Telling, G.C. (2008) Expedited Intra- and Inter-species prion transmission. PLoS Pathogen. 4:e1000139.
Gambetti, P., Dong, Z., Yuan, J., Xiao, X., Zheng, M., Alshekhlee, A., Castellani, R., Cohen, M., Barria, M., Gonzalez-Romero, D., Belay, E., Schoenberger, L., Marder, K., Harris, C., Burke, J.R., Montine, T., Wisniewski, T., Dickson, D.W., Soto, C., Hulette C.M., Mastrianni, J.A., Kong, Q., and Zou, W. (2008) A novel human prion disease with protease-sensitive prion. Ann. Neurol. 63: 697-708. Selected article of the year by the American Neurological Association
Hetz, C., Lee, A.H., Gonzalez-Romero, D., Thielen, P., Castilla, J., Soto, C. and Laurie H. Glimcher. (2008) Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc. Natl. Acad. Sci. USA 105: 757-762.
Soto, C. and Estrada, L.D. (2008) Protein Misfolding and Neurodegeneration. Arch. Neurol. 65: 184-189.
Hetz, C., Castilla, J. and Soto, C. (2007) Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J. Biol. Chem. 282: 12725-12723.
Morales, R., Abid, K. and Soto, C. (2007) The prion strain phenomenon: Molecular basis and unprecedented features. Biochim. Biophys. Acta 1772: 681-691.
Estrada, L.D. and Soto, C. (2007) Disrupting beta-amyloid for Alzheimer’s disease treatment. Curr. Top Med. Chem. 7: 115-126.
Soto, C. (2007) Reversibility of prion-induced neurodegeneration. Lancet Neurol. 6: 294-295.
Richt, J.A., Kasinathan, P., Hamir, A.N., Castilla, J., Sathiyaseelan, T., Vargas, F., Sarhiyaseelan, J., Wu, H., Matsushita, H., Koster, J., Kato, S., Ishida, I., Soto, C., Robl, J. and Kuroiwa, Y. (2007) Prion protein deficient cattle develop normally and are resistant to in vitro PrPBSE propagation. Nature Biotech. 25: 132-138.
Bieler, S., Silva, F., Soto, C. and Belin, D. (2006) Bactericidal activity of both secreted and nonsecreted microcin E492 requires the mannose permease. J. Bacteriol. 188: 7049-7061.
Saa, P., Castilla, J. and Soto, C.. (2006) Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 281: 35245-35252.
Pastrana, M.A., Sajmani, G., Onisko, B., Castilla, J., Soto, C. and Requena, J.R. (2006) isolation and characterization of a PK sensitive PrPSc fraction. Biochemistry 45: 15710-16717.
Abid, K. and Soto, C. (2006) The intriguing prion disorders. Cell Mol. Life Science 63: 2342-2351. Picture selected for cover page.
Saa, P., Castilla, J. and Soto, C. (2006) Pre-symptomatic detection of prions in blood. Science 313: 92-94.
Estrada L.D. and Soto C. (2006) Peptide inhibitors of protein misfolding and aggregation. Curr. Pharm. Des. 12: 2557-2568.
Soto C. (2006) Therapeutic for Protein Misfolding Disorders. Curr. Pharm. Des. 12: 2541-2542. (Picture selected for cover page)
Castilla, J., Saa, P., Morales, R., Abid, K., Maundrell, K. and Soto, C. (2006) PMCA for diagnosis and prion propagation studies. Meth Enzymol. 412, 3-20
Soto, C., Estrada, L.D. and Castilla, J. (2006) Amyloid, Prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem. Sci. 31: 150-155.
Hetz, C. and Soto, C. (2006) Stressing out the ER: A role for the unfolded protein response in prion-related disorders. Curr. Mol. Med. 6: 37-43.
Hetz, C. and Soto, C. (2006) Emerging roles of the unfolded protein response signaling in physiology and disease. Curr. Mol. Med. 6: 1. (picture selected for cover page)
Estrada LD., Yowtak J., and Soto C. (2006)Protein misfolding disorders and rational design of antimisfolding agents. Meth. Mol. Biol. 340:277-93.
Castilla, J., Saa, P. and Soto, C. (2005) Biochemical detection of prions in blood. Nature medicine 11: 982-985. Highlighted in Nature, Science, Anal. Biochem.
Bieler, S., Estrada, L., Lagos, R., Castilla, J. and Soto, C. (2005) Amyloid formation modulates the biological activity of a bacterial protein. J. Biol. Chem. 280: 26880-26885.
Castilla, J., Saa, P., Hetz, C. and Soto, C. (2005) In vitro generation of infectious scrapie prions. Cell 121: 195-206. Highlighted in Cell, Science, Nature, Nature Medicine, Nature Methods, Trends in Molecular Medicine.
Saa, P., Castilla, J. and Soto C. (2005) Cyclic amplification of protein misfolding and aggregation. Meth. Mol. Biol. 299:53-65.
Hetz, C., Russelakis-Carneiro, M., Walchli, S., Carboni, S., Vial- Knecht, E., Maundrell, K. and Soto, C. (2005) The disulfide isomerase Grp58 is a neuroprotective factor against prion replication. J. Neurosci. 25: 2793-2802.
Soto, C., Anderes, L., Suardi, S., Cardone, F., Castilla, J., Frossard, M.J., Peano, S., Saa, P., Limido, L., Carbonatto, M., Ironside J.W., Torres, J.M., Pocchiari, M. and Tagliavini, F. (2005) Pre-symptomatic detection of prions by Cyclic Amplification of Protein Misfolding. FEBS Lett. 579: 638-642.
Soto, C. (2004) Diagnosing prion diseases: needs, challenges and hopes. Nature Rev. Microbiol. 2: 809-819. Selected article of the month by the editors.
Russelakis-Carneiro, M., Hetz, C., Maundrell, K and Soto, C. (2004) Accumulation of PrP in neuronal lipid rafts leads to a change in the subcellular localization of caveolin and synaptophysin: a putative mechanism of neurodegeneration in prion disease. Am. J. Pathol. 165: 1839-1848.
Chacon, M., Barria, M.I., Soto, C. and Inestrosa, N.C. (2004) Beta-sheet breaker peptide rescue spatial memory impairments with partial disaggregation of amyloid deposits in a rat model of Alzheimer’s disease. Mol. Psych. 9: 953-961. Picture selected for cover page.
Soto, C. and Castilla, J. (2004) The controversial protein-only hypothesis of prion propagation. Nature medicine 10: S63-S67.
Golabek, A.A., Wujek, P., Walus, M., Bieler, S., Soto, C., Wisniewski, K.E. and Kida, E. (2004) Maturation of human tripeptidyl-peptidase I in vitro. J. Biol. Chem. 279: 31058-31067.
Bieler, S and Soto, C. (2004) ß-sheet breakers for Alzheimer’s disease therapy. Curr. Drug Targets. 5: 553-558.
Castilla, J., Hetz, C. and Soto, C. (2004) Molecular Mechanism of Neurotoxicity of Pathological Prion Protein. Curr. Mol. Med. 4: 397-403.
Banks, W.A., Niehoff, M.L., Adessi, C. and Soto, C. (2004) Passage of murine scrapie across the mouse vascular blood-brain barrier. Biochem. Biophys. Res. Commun. 318: 125-130.
Adessi, C and Soto, C. (2004) Strategies to improve stability and bioavailability of peptide drugs. Frontier Med. Chem. 1: 513-528.
Hetz, C., Russelakis, M., Maundrell, K., Castilla, J. and Soto, C. (2003) Neuronal apoptosis induced by pathological prion protein is mediated by caspase-12 and endoplasmic reticulum stress. EMBO J. 22: 5436-5445. Highlighted in Science.
Hetz, C., Benavent, S., Bieler, S. and Soto, C. (2003) Prion protein misfolding and brain damage. Curr. Med. Chem. Immunol. Endoc. & Metab. Agents 3: 137-147.
Wilson, J., Rossi, CP., Carboni, S., Fremaux, C., Perrin, D., Soto C., Kosco-Vilbois M., and Scheer, A. (2003) A homogeneous 384-well high-throughput binding assay for a TNF receptor using alphascreen technology. J. Biomol. Screening 8: 522-532.
Hetz, C, Maundrell, K. and Soto, C. (2003) Is the loss of function of prion protein the cause of prion disorders? Trends Mol. Med. 9: 237-243.
Adessi, C., Frossard, M.J, Boisard, C., Fraga, S., Bieler, S., Ruckle, T., Robinson, S.M., Mutter, M., Banks, W.A. and Soto, C. (2003) Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer’s disease. J. Biol. Chem. 278: 13905-13911.
Soto, C. (2003) Unfolding the role of Protein Misfolding in Neurodegenerative Diseases. Nature Rev. Neurosci. 4: 49-60.
Hetz, C and Soto, C. (2003) Protein Misfolding and Disease: The case of prion protein. Cell. Mol. Life Sci. 60: 133-143. (picture selected for cover page)
Russelakis-Carneiro, M., Saborio, G.P., Anderes, L. and Soto, C. (2002) Changes in the glycosylation pattern of prion protein in murine scrapie: implications for the mechanism of neurodegeneration in prion diseases. J. Biol. Chem. 277: 36872-36877.
Soto, C., Saborio, G.P. and Anderes, L (2002) Cyclic amplification of Protein Misfolding: Applications in prion research and beyond. Trends Neurosci. 25: 390-394
Adessi, C and Soto, C. (2002) Beta-sheet breaker approach for the treatment of Alzheimer’s disease. Drug. Dev. Res. 56: 184-193.
Soto, C. (2002) Altering prion replication for therapy and diagnosis of Transmissible Spongiform Encephalopathies. Biochem. Soc. Transactions 30: 569-574.
Adessi, C. and Soto, C. (2002) Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr. Med. Chem. 9: 963-978.
Permanne, B., Adessi, C., Saborio, G.P., Fraga, S., Frossard, M.J., Van Dorpe, J., Dewachter, I., Banks, W.A., Van Leuven, F. And Soto, C. (2002) Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer’s disease by treatment with a ß-sheet breaker peptide. FASEB J. 16: 860-862 (full-version published online on April 10, 2002 as 10.1096/fj.01-0841fje).
Permanne, B., Adessi, C., Fraga, S., Frosard, M.J., Saborio, G.P. and Soto, C. (2002) Are ß-sheet breaker peptides dissolving the therapeutic problem of Alzheimer’s disease?. J. Neural Transmission 62: 293-301.
Petchanikow, C., Saborio, G.P., Anderes, L., Frossard, M.J., Olmedo, M.I. and Soto, C. (2001) Structural and biochemical studies of prion protein polymorphism. FEBS Lett. 509: 451-456.
Soto, C. (2001) Protein misfolding and disease; Protein refolding and therapy. FEBS Lett 498: 204-207.
Saborio, G.P., Permanne, B. and Soto, C. (2001) Cyclic amplification of protein misfolding: A novel approach for sensitive detection of pathological prion protein. Nature 411: 810-813. (Selected article of the week by Nature editors).
Calero, M., Pawlik, M., Soto, C., Castano, E.M., Sigurdsson, E.M., Kumar, A., Gallo, G., Frangione, B. and Levy, E. (2001) Distinct properties of wild-type and the amyloidogenic human cystatin C variant of hereditary cerebral hemorrhage with amyloidosis, Icelandic type. J. Neurochem. 77: 628-637.
Soto, C. and Saborio, G.P. (2001) Prions: Disease-propagation and disease-therapy by conformational transmission. Trends Mol. Med. 7: 109-114. (Among the 5 most read articles of the Journal in year 2001)
Soto, C., Saborio, G.P., and Permanne, B. (2000) Inhibiting the conversion of soluble amyloid-ß peptide into abnormally folded amyloidogenic intermediates: Relevance for Alzheimer’s disease therapy. Acta Neurol. Scand. 176: 90-95.
Golabek, A.A., Kida, E., Walus, M., Perez, C., Wisniewski, T. and Soto, C. (2000) SDS-resistant complexes of Alzheimer’s amyloid b-peptide with the N-terminal, receptor binding domain of apolipoprotein E. Byophis. J. 79:1008-1015.
Baumann, M., Kallijärvi, J., Lankinen, H., Soto, C. and Haltia, M. (2000) Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptides. Biochem. J. 349: 77-84
Yan, S.D., Fu, J., Golabek, A, Zhu, H., Zhu, A., Chen, X., Roher, A., Soto, C., Stern, D., Schmidt, A.M. & Kindy. M.S. (2000) RAGE and amyloid fibrils: A mechanism targeting fibrils to the cell surface and enhancing cytotoxicity in amyloidoses. Nature Med 6: 643-651.
Sigurdsson, E.M., Permanne, B. Soto, C., Wisniewski, T. & Frangione, B. (2000) In vivo disassembly of amyloid-ß deposits in rat brain. J. Neuropath. Exp. Neurol. 59: 11-17.
Soto, C., Kascsak, R.J., Saborio, G., Aucouturier, P., Wisniewski, T., Prelli, F., R. Kascsak, Mendez, E., Harris, D.A., Ironside, J., Tagliavini, F., Carp, R.I. & Frangione, B. (2000) Reversion of prion protein conformational changes by synthetic ß-sheet breaker peptides. The Lancet 355: 192-197.
Soto, C. (1999) ß-amyloid disrupting drugs: potential in the treatment of Alzheimer’s disease. CNS Drugs 12: 347-356.
Saborio, G.P., Soto, C., Kascsak, R.J., Levy, E., Kascsak, R., Harris, D. & Frangione, B. (1999) Cell-lysate conversion of prion protein into its protease-resistant isoform suggests the participation of a cellular chaperone. Biochem. Biophys. Res. Commun. 258: 470-475.
Soto, C. (1999) Plaque busters: strategies to inhibit amyloid plaque formation in Alzheimer’s disease. Mol. Med. Today 5: 343-350.
Poduslo, J.F., Curran, G., Kumar, A., Frangione, B., and Soto, C. (1999) ß-sheet breaker peptide inhibitor of Alzheimer’s amyloidogenesis with increased blood-brain barrier permeability and resistance to proteolytic degradation in plasma. J. Neurobiol. 39: 371-382.
Soto, C. (1999) Alzheimer’s and Prion diseases as disorders of protein conformation: Implications for the design of novel therapeutic approaches. J. Mol. Med. 77: 412-418.
Sigurdsson, E.M., Morelli, E.M., Kumar, R.A., Castaño, E.M., Frangione, B. & Soto, C. (1998) ß-sheet breaker peptides prevent Alzheimer’s amyloid formation in vivo. Alzheimer’s Reports 1: S35-S36.
Wisniewski, T., Aucouturier, P., Soto, C. & Frangione, B. (1998) The prionoses and other conformational disorders. Amyloid 5: 212-214.
Crawford, F., Soto, C., Suo, Z., Fang, C., Sawar, A., Parker, T., Frangione, B. & Mullan, M. (1998) Alzheimer’s ß-amyloid vasoactivity: identification of a novel ß-amyloid conformational Intermediate. FEBS Lett. 436: 445-448.
Soto, C., Sigursson, E., Morelli, L., Kumar, R.A., Castaño, E.M. and Frangione, B. (1998) ß-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer’s therapy. Nature med. 4: 822-826.
Alfonso, P., Soto, C. Albar, J.P., Escobar, H. and Mendez, E.(1998) ß-structure recognition of anti-gliadin antibodies in coeliac disease. FEBS Lett. 427: 36-40.
Pappolla, M., Bozner, P., Soto, C., Shao, H., Robakis, N.K., Zagorski, M., Frangione, B. and Ghiso, J. (1998) Inhibition of Alzheimer’s ß-fibrillogenesis by Melatonin. J. Biol. Chem. 273: 7185-7188.
Jimenez-Huete, A., Alfonso, P., Soto, C., Albar, J.P., Rabano, A., Ghiso, J., Frangione, B. and Mendez, E. (1998) Antibodies directed to the carboxyl terminus of amyloid beta peptide recognize sequence epitopes and distinct immunoreactive deposits in Alzheimer’s brain. Alzheimer’s Reports 1: 41-48.
Permanne, B., Perez, C., Soto, C., Frangione, B. and Wisniewski, T. (1997) Detection of soluble amyloid-ß/apolipoprotein E complexes in Alzheimer’s brain supernatants. Biochem. Biophys. Res. Commun. 240: 715-720.
Yan, S.D., Fu, J., Soto, C., Chen, X., Zhu, H., Al-Mohanna, F., Collison, K., Zhu, A., Stern, E., Saido, T., Tohyama, M., Ogawa, S., Roher, A. and Stern, D. (1997) A novel intracellular amyloid-beta peptide binding protein which mediates neurotoxicity in Alzheimer’s disease. Nature 389: 689-698.
Soto, C., Ghiso, J., & Frangione, B. (1997) Alzheimer’s Amyloid-ß aggregation is modulated by the interaction of multiple factors. Alzheimer’s Research. 3: 215-222.
Castaño, E.M., Prelli, F., Soto, C., Beavis, R., Matsubara, E., Shoji, M. & Frangione, B. (1996) The length of amyloid-ß in Hereditary Hemorrhage with amyloidosis, Dutch type: Implications for the role of amyloid- ß 1-42 in Alzheimer’s disease. J. Biol. Chem. 271: 32185-32191.
Soto, C., Kindy, M.S., Baumann, M & Frangione, B. (1996) Inhibition of Alzheimer’s amyloidosis by peptides that prevent ß-sheet conformation. Biochem. Biophys. Res. Commun. 226: 672-680.
Matsubara, E., Soto, C., Governale, S., Frangione, B. & Ghiso, J. (1996) Apolipoprotein J complexed to Alzheimer’s amyloid ß prevents peptide aggregation and degradation in vitro. Biochem. J. 316: 671-679.
Soto, C., Rodriguez, P. & Monasterio, O. (1996) Calcium and Gadolinium ions stimulate the GTPase activity of purified chicken brain tubulin through a conformational change. Biochemistry 35: 6337-6344.
Soto, C., Golabek, A., Wisniewski, T. & Castaño, E.M. (1996) Alzheimer’s ß-amyloid peptide is conformationally modulated by apolipoprotein E in vitro. NeuroReport 7: 721-725.
Inestrosa, N.C., Alvarez, A., Perez, C.A., Moreno, R.D., Vicente, M., Linker, C., Soto, C., & Garrido, J. (1996) Acetylcholinesterase accelerates assembly of amyloid- ß peptides into Alzheimer’s amyloid fibrils: Possible role of the peripheral binding site of the enzyme. Neuron 16: 881-891.
Golabek, Soto, C., Vogel, T. & Wisniewski, T. (1996) The interaction between apolipoprotein E and Alzheimer’s amyloid- ß is dependent on ß-peptide conformation. J. Biol. Chem. 271: 10602-10607.
Soto, C. & Castaño, E.M. (1996) The conformation of Alzheimer’s beta peptide determines the rate of amyloid formation and its resistance to proteolysis. Biochem. J. 314: 701-707
Bronfman, F., Soto, C., Tapia, L., Tapia, V., & Inestrosa, N.C. (1996) Extracellular matrix regulates the amount of the ß-amyloid precursor protein and its amyloidogenic derivatives. J. Cell. Physiol. 166: 360-369.
Soto, C., Castaño, E.M., Kumar, R.A., Beavis, R.C. and Frangione, B. (1995) Fibrillogenesis of synthetic amyloid-ß is dependent on the peptide initial secondary structure. Neurosci. Lett. 200: 105-108.
Soto, C., Castaño, E.M., Prelli, F., Kumar, R. & Baumann, M. (1995) Apolipoprotein E increase the fibrillogenic potential of synthetic peptides derived from Alzheimer’s, gelsolin and AA amyloid. FEBS Lett. 371: 110-114.
Soto, C. & Frangione, B. (1995) Two conformational states of amyloid ß-peptide: Implications for the pathogenesis of Alzheimer’s disease. Neurosci. Lett. 186: 115-118.
Castaño, E.M., Prelli, F., Wisniewski, T., Golabek, A., Kumar, R., Soto, C. & Frangione, B. (1995) Fibrillogenesis of Alzheimer’s amyloid ß-peptide and Apolipoprotein E. Biochem. J. 306: 599-604.
Soto, C., Castaño, E.M., Frangione, B. & Inestrosa, N.C. (1995) The a-helical to ß-stand transition in the N-terminal fragment of the amyloid ß-peptide modulates amyloid formation. J. Biol. Chem. 270: 3063-3067.
Soto, C., Brañes, M.C., Alvarez, J. & Inestrosa, N.C. (1994) Structural determinants of amyloid formation in Alzheimer’s disease. J. Neurochem. 63: 1191-1198.
Inestrosa N. & Soto, C. (1992) Cell and Molecular Biology of Alzheimer’s Disease. Biol. Res. 25: 63-72.