Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jenna Crowell"'
Autor:
Julianna L. Sun, Sehun Kim, Jenna Crowell, Bailey K. Webster, Emma K. Raisley, Diana C. Lowe, Jifeng Bian, Sirkka-Liisa Korpenfelt, Sylvie L. Benestad, Glenn C. Telling
Publikováno v:
Emerging Infectious Diseases, Vol 29, Iss 2, Pp 323-332 (2023)
Our previous studies using gene-targeted mouse models of chronic wasting disease (CWD) demonstrated that Norway and North America cervids are infected with distinct prion strains that respond differently to naturally occurring amino acid variation at
Externí odkaz:
https://doaj.org/article/831123ef9c134d55b29112bf630a78f7
Autor:
Jifeng Bian, Sehun Kim, Sarah J Kane, Jenna Crowell, Julianna L Sun, Jeffrey Christiansen, Eri Saijo, Julie A Moreno, James DiLisio, Emily Burnett, Sandra Pritzkow, Damian Gorski, Claudio Soto, Terry J Kreeger, Aru Balachandran, Gordon Mitchell, Michael W Miller, Romolo Nonno, Turid Vikøren, Jørn Våge, Knut Madslien, Linh Tran, Tram Thu Vuong, Sylvie L Benestad, Glenn C Telling
Publikováno v:
PLoS Pathogens, Vol 17, Iss 7, p e1009748 (2021)
Prions are infectious proteins causing fatal, transmissible neurodegenerative diseases of animals and humans. Replication involves template-directed refolding of host encoded prion protein, PrPC, by its infectious conformation, PrPSc. Following its d
Externí odkaz:
https://doaj.org/article/bea6273ddd5944c1a6d5966be71ea6e1
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0119863 (2015)
Natural prion diseases of ruminants are moderately contagious and while the gastrointestinal tract is the primary site of prion agent entry, other mucosae may be entry sites in a subset of infections. In the current study we examined prion neuroinvas
Externí odkaz:
https://doaj.org/article/27376673ec564186b90bab8ce679eabd
Autor:
Julianna L. Sun, Jifeng Bian, Sehun Kim, Jenna Crowell, Bailey K. Webster, Emma K. Raisley, Sirkka-Liisa Korpenfelt, Sylvie L. Benestad, Glenn C. Telling
Concern is mounting over the global emergence, expanding host range, and uncertain zoonotic potential of chronic wasting disease (CWD), a fatal, infectious disease of cervids caused by prions. Our previous studies using genetically modified CWD-susce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c691bda089a3ccbff930c0e240f59e09
https://doi.org/10.1101/2022.07.11.499602
https://doi.org/10.1101/2022.07.11.499602
Autor:
Jason C. Bartz, Sehun Kim, Jifeng Bian, Jenna Crowell, Hae Eun Kang, Sarah J. Kane, Glenn C. Telling, Vanessa Selwyn
Publikováno v:
J Biol Chem
The causative factors underlying conformational conversion of cellular prion protein (PrP(C)) into its infectious counterpart (PrP(Sc)) during prion infection remain undetermined, in part because of a lack of monoclonal antibodies (mAbs) that can dis
Autor:
Julie A. Moreno, Stephanie S Suinn, Glenn C. Telling, Jenna Crowell, Richard A. Bessen, Lindsay E. Parrie
Publikováno v:
Prion
Adult neurogenesis, analogous to early development, is comprised of several, often concomitant, processes including proliferation, differentiation, and formation of synaptic connections. However, due to continual, asynchronous turn-over, newly-born a
Autor:
Sylvie L. Benestad, Sandra Pritzkow, Tram Thu Vuong, Linh T. Tran, Romolo Nonno, Turid Vikøren, Knut Madslien, Sarah J. Kane, Jifeng Bian, Aru Balachandran, Terry J. Kreeger, Sehun Kim, Glenn C. Telling, Claudio Soto, Eri Saijo, Jenna Crowell, James E DiLisio, Damian Gorski, Jeffrey R. Christiansen, Jørn Våge, Julie A. Moreno, Michael W. Miller, Gordon Mitchell, Emily Burnett, Julianna L. Sun
Publikováno v:
PLoS Pathogens
PLoS Pathogens, Vol 17, Iss 7, p e1009748 (2021)
PLoS Pathogens, Vol 17, Iss 7, p e1009748 (2021)
Prions are infectious proteins causing fatal, transmissible neurodegenerative diseases of animals and humans. Replication involves template-directed refolding of host encoded prion protein, PrPC, by its infectious conformation, PrPSc. Following its d
Publikováno v:
Developmental biology. 438(1)
The cellular prion protein (PrP(C)) has been associated with diverse biological processes including cell signaling, neurogenesis, and neuroprotection, but its physiological function(s) remain ambiguous. Here we determine the role of PrP(C) in adult n
Phenotypic diversity in prion diseases can be specified by prion strains in which biological traits are propagated through an epigenetic mechanism mediated by distinct PrP Sc conformations. We investigated the role of host-dependent factors on phenot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40da23d35b9a0ad9720285cdf2ff0ebb
https://europepmc.org/articles/PMC4580196/
https://europepmc.org/articles/PMC4580196/