Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Alejandro M. Sevillano"'
Autor:
Julia A. Callender, Alejandro M. Sevillano, Katrin Soldau, Timothy D. Kurt, Taylor Schumann, Donald P. Pizzo, Hermann Altmeppen, Markus Glatzel, Jeffrey D. Esko, Christina J. Sigurdson
Publikováno v:
Neurobiology of Disease, Vol 142, Iss , Pp 104955- (2020)
Many aggregation-prone proteins linked to neurodegenerative disease are post-translationally modified during their biogenesis. In vivo pathogenesis studies have suggested that the presence of post-translational modifications can shift the aggregate a
Externí odkaz:
https://doaj.org/article/e65409fc3f7f4f5db6a77675774e64c7
Autor:
Makoto Kobayashi, Jody Vykoukal, Hiroyuki Katayama, James Long, Jinsong Liu, Ehsan Irajizad, Nikul Patel, Xiangying Mao, Leona Rusling, Yining Cai, Fuchung Hsiao, Chuan-Yih Yu, Franscisco Esteva, Johannes Fahrmann, Sam Hanash, Alejandro M Sevillano
Publikováno v:
Journal for ImmunoTherapy of Cancer, Vol 9, Iss 6 (2021)
Background Citrulline post-translational modification of proteins is mediated by protein arginine deiminase (PADI) family members and has been associated with autoimmune diseases. The role of PADI-citrullinome in immune response in cancer has not bee
Externí odkaz:
https://doaj.org/article/65be92c8f6ac418b8232f5690477e537
Autor:
Alejandro M Sevillano, Natalia Fernández-Borges, Neelam Younas, Fei Wang, Saioa R Elezgarai, Susana Bravo, Ester Vázquez-Fernández, Isaac Rosa, Hasier Eraña, David Gil, Sonia Veiga, Enric Vidal, Melissa L Erickson-Beltran, Esteban Guitián, Christopher J Silva, Romolo Nonno, Jiyan Ma, Joaquín Castilla, Jesús R Requena
Publikováno v:
PLoS Pathogens, Vol 14, Iss 1, p e1006797 (2018)
Very solid evidence suggests that the core of full length PrPSc is a 4-rung β-solenoid, and that individual PrPSc subunits stack to form amyloid fibers. We recently used limited proteolysis to map the β-strands and connecting loops that make up the
Externí odkaz:
https://doaj.org/article/a5a65062a45e40f184b776930d9e28d0
Autor:
Hermann C. Altmeppen, Christina J. Sigurdson, Timothy D. Kurt, Donald P. Pizzo, Sofie Nyström, Thu H Nam, Katrin Soldau, Jeffrey D. Esko, K. Peter R. Nilsson, Taylor Schumann, Jessica Lawrence, Markus Glatzel, Patricia Aguilar-Calvo, Biswa Choudhury, Alejandro M. Sevillano
Publikováno v:
J Clin Invest
The Journal of clinical investigation, vol 130, iss 3
The Journal of clinical investigation, vol 130, iss 3
Posttranslational modifications (PTMs) are common among proteins that aggregate in neurodegenerative disease, yet how PTMs impact the aggregate conformation and disease progression remains unclear. By engineering knockin mice expressing prion protein
Publikováno v:
Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname
Prion
instname
Prion
Understanding the structure of PrPSc is without doubt a sine qua non to understand not only PrPSc propagation, but also critical features of that process such as the strain phenomenon and transmission barriers. While elucidation of the PrPSc structur
Autor:
Alejandro M. Sevillano, Donald P. Pizzo, Hermann C. Altmeppen, Katrin Soldau, Christina J. Sigurdson, Timothy D. Kurt, Taylor Schumann, Jeffrey D. Esko, Markus Glatzel, Julia A. Callender
Publikováno v:
Neurobiol Dis
Neurobiology of Disease, Vol 142, Iss, Pp 104955-(2020)
Neurobiology of Disease, Vol 142, Iss, Pp 104955-(2020)
Many aggregation-prone proteins linked to neurodegenerative disease are post-translationally modified during their biogenesis. In vivo pathogenesis studies have suggested that the presence of post-translational modifications can shift the aggregate a
Autor:
Alejandro M. Sevillano, K. Peter R. Nilsson, Katrin Soldau, Jiri G. Safar, Jeffrey D. Esko, Daniel R. Sandoval, Jaidev Bapat, Hermann C. Altmeppen, Steven D. Edland, Christina J. Sigurdson, Luise Linsenmeier, Markus Glatzel, Patricia Aguilar-Calvo, Michael D. Geschwind, Mark L. Cohen, Henry Sanchez, Brian S. Appleby, Donald P. Pizzo
Publikováno v:
Acta neuropathologica, vol 139, iss 3
Acta Neuropathol
Acta Neuropathol
Cofactors are essential for driving recombinant prion protein into pathogenic conformers. Polyanions promote prion aggregation in vitro, yet the cofactors that modulate prion assembly in vivo remain largely unknown. Here we report that the endogenous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3ac0a657ecfc3434047c1b621e84614
https://escholarship.org/uc/item/4zv6s4nr
https://escholarship.org/uc/item/4zv6s4nr
Autor:
Jessica Lawrence, Cyrus Bett, Katrin Soldau, Christina J. Sigurdson, Patricia Aguilar-Calvo, Timothy D. Kurt, K. Peter R. Nilsson, Alejandro M. Sevillano, Per Hammarström
Publikováno v:
Brain Pathology. 28:999-1011
Prions typically spread into the central nervous system (CNS), likely via peripheral nerves. Yet prion conformers differ in their capacity to penetrate the CNS; certain fibrillar prions replicate persistently in lymphoid tissues with no CNS entry, le
Autor:
Jesús R. Requena, Simone Orioli, Alejandro M. Sevillano, Giovanni Spagnolli, Emiliano Biasini, Pietro Faccioli, Holger Wille, Marta Rigoli
Publikováno v:
Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname
PLoS Pathogens
PLoS Pathogens, Vol 15, Iss 7, p e1007864 (2019)
instname
PLoS Pathogens
PLoS Pathogens, Vol 15, Iss 7, p e1007864 (2019)
Prions are unusual protein assemblies that propagate their conformationally-encoded information in absence of nucleic acids. The first prion identified, the scrapie isoform (PrPSc) of the cellular prion protein (PrPC), caused epidemic and epizootic e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28d604f861fd14ec6c418c1076c51663
https://hdl.handle.net/10281/405604
https://hdl.handle.net/10281/405604
Autor:
Helen Khuu, Patricia Aguilar-Calvo, Julia A. Callender, Christina J. Sigurdson, Katrin Soldau, Alejandro M. Sevillano
Publikováno v:
The FASEB Journal. 34:1-1