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CLAUDIO SOTO JARA UNIVERSITY OF TEXAS MEDICAL BRANCH AT GALVESTON TEXAS 77555‐0641 GALVESTON ESTADOS UNIDOS DE AM Nacionalidad CHILE Formación académica PhD. University of Chile, Santiago, Chile Postdoctoral Fellowship Catholic University of Chile, Santiago, Chile, and New York University School of Medicine, New York, New York Áreas de interés: Bases moleculares de las enfermedades neurodegenerativas asociadas con el mal plegamiento y la acumulación de proteínas en el cerebro, particularmente enfocado a Alzheimer, enfermedades priónicas y otros desordenes relacionados Línea(s) de Investigación ALZHEIMER PROBLEMAS PLEGAMIENTO PROTEINAS METODOS DIAG.ENF. ASOSCIADAS A PLEGAMIENTO PROTEINAS PRION El Dr. Soto ha publicado más de 100 publicaciones científicas de revisión por pares y ha contribuido a más de 20 libros, entre ellos uno escrito íntegramente por él mismo. Muchos de sus estudios han sido publicados en las revistas científicas más prestigiosas (incluyendo Cell, Nature, Science, Nature Medicine, PNAS, Neuron, EMBO J, etc). Publicaciones 2011‐2014 1. Duran‐Aniotz, C., et al., Aggregate‐depleted brain fails to induce abeta deposition in a mouse model of Alzheimer's disease. PLoS ONE, 2014. 9(2): p. e89014. 2. Concha‐Marambio, L., R. Diaz‐Espinoza, and C. Soto, The extent of protease resistance of misfolded prion protein is highly dependent on the salt concentration. J Biol Chem, 2014. 289(5): p. 3073‐9. 3. Chen, B., C. Soto, and R. Morales, Peripherally administrated prions reach the brain at sub‐
infectious quantities in experimental hamsters. FEBS Lett, 2014. 588(5): p. 795‐800. 4. Zhu, J., et al., De novo identification of VRC01 class HIV‐1‐neutralizing antibodies by next‐
generation sequencing of B‐cell transcripts. Proc Natl Acad Sci U S A, 2013. 110(43): p. E4088‐97. 5. Moreno‐Gonzalez, I., et al., Smoking exacerbates amyloid pathology in a mouse model of Alzheimer's disease. Nat Commun, 2013. 4: p. 1495. 6. Morales, R., et al., Lack of prion transmission by sexual or parental routes in experimentally infected hamsters. Prion, 2013. 7(5): p. 412‐9. 7. Morales, R., I. Moreno‐Gonzalez, and C. Soto, Cross‐seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog, 2013. 9(9): p. e1003537. 8. Cuanalo‐Contreras, K., A. Mukherjee, and C. Soto, Role of Protein Misfolding and Proteostasis Deficiency in Protein Misfolding Diseases and Aging. Int J Cell Biol, 2013. 2013: p. 638083. 9. Soto, C., Transmissible proteins: expanding the prion heresy. Cell, 2012. 149(5): p. 968‐77. 10. Soto, C., In vivo spreading of tau pathology. Neuron, 2012. 73(4): p. 621‐3. 11. Soto, C., Animal Models for Neurodegenerative Diseases Associated to Accumulation of Misfolded Protein Aggregates. Curr Pharm Des, 2012. 12. Shahnawaz, M. and C. Soto, Microcin amyloid fibrils A are reservoir of toxic oligomeric species. J Biol Chem, 2012. 287(15): p. 11665‐76. 13. Moreno‐Gonzalez, I. and C. Soto, Natural Animal Models of Neurodegenerative Protein Misfolding Diseases. Curr Pharm Des, 2012. 14. Morales, R., et al., Protein misfolding cyclic amplification of infectious prions. Nat Protoc, 2012. 7(7): p. 1397‐409. 15. Morales, R., et al., De novo induction of amyloid‐beta deposition in vivo. Mol Psychiatry, 2012. 17(12): p. 1347‐53. 16. Diaz‐Espinoza, R. and C. Soto, High‐resolution structure of infectious prion protein: the final frontier. Nat Struct Mol Biol, 2012. 19(4): p. 370‐7. 17. Diaz‐Espinoza, R., A. Mukherjee, and C. Soto, Kosmotropic anions promote conversion of recombinant prion protein into a PrPSc‐like misfolded form. PLoS One, 2012. 7(2): p. e31678. 18. Barria, M.A., D. Gonzalez‐Romero, and C. Soto, Cyclic amplification of prion protein misfolding. Methods Mol Biol, 2012. 849: p. 199‐212. 19. Urayama, A., et al., Initial fate of prions upon peripheral infection: half‐life, distribution, clearance, and tissue uptake. Faseb J, 2011. 20. Torres, M., et al., Abnormal calcium homeostasis and protein folding stress at the ER: A common factor in familial and infectious prion disorders. Commun Integr Biol, 2011. 4(3): p. 258‐
61. 21. Soto, C. and N. Satani, The intricate mechanisms of neurodegeneration in prion diseases. Trends in Molecular Medicine, 2011. In Press, Corrected Proof. 22. Soto, C., Prion hypothesis: the end of the controversy? Trends Biochem Sci, 2011. 36(3): p. 151‐8. 23. Mukherjee, A. and C. Soto, Role of calcineurin in neurodegeneration produced by misfolded proteins and endoplasmic reticulum stress. Curr Opin Cell Biol, 2011. 23(2): p. 223‐30. 24. Moreno‐Gonzalez, I. and C. Soto, Misfolded protein aggregates: Mechanisms, structures and potential for disease transmission. Semin Cell Dev Biol, 2011. 25. Morales, R., et al., De novo induction of amyloid‐beta deposition in vivo. Mol Psychiatry, 2011. 26. Lopez‐Lopez, E., et al., Responses of antioxidant enzymes, lipid peroxidation, and Na+/K+‐
ATPase in liver of the fish Goodea atripinnis exposed to Lake Yuriria water. Fish Physiol Biochem, 2011. 37(3): p. 511‐22. 27. Eiden, M., et al., Effects of polymorphisms in ovine and caprine prion protein alleles on cell‐free conversion. Vet Res, 2011. 42(1): p. 30. 28. Eiden, M., et al., Effects of polymorphisms in ovine and caprine prion protein alleles on cell‐free conversion. Veterinary Research, 2011. 42(1): p. 1‐7. 29. Barria, M.A., et al., Generation of a new form of human PrP(Sc) in vitro by interspecies transmission from cervid prions. J Biol Chem, 2011. 286(9): p. 7490‐5.