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of 4
pro vyhledávání: '"Billie J. Perry"'
Autor:
Fruma Yehiely, Paul Bamborough, Maria Da Costa, Billie J. Perry, Gopal Thinakaran, Fred E. Cohen, George A. Carlson, Stanley B. Prusiner
Publikováno v:
Neurobiology of Disease, Vol 3, Iss 4, Pp 339-355 (1997)
Prion diseases are disorders of protein conformation that produce neurodegeneration in humans and animals. Studies of transgenic (Tg) mice indicate that a factor designated protein X is involved in the conversion of the normal cellular prion protein
Externí odkaz:
https://doaj.org/article/88c5f85e9c5644c783be20cde95711f4
Autor:
Fruma Yehiely, Paul Bamborough, Maria Da Costa, Billie J. Perry, Gopal Thinakaran, Fred E. Cohen, George A. Carlson, Stanley B. Prusiner
Publikováno v:
Neurobiology of Disease, Vol 10, Iss 1, Pp 67-68 (2002)
Externí odkaz:
https://doaj.org/article/a53344cae47d4386b6978aed2bdc6b86
Autor:
Weiming Xia, Ivan Lieberburg, Peter St. George Hyslop, Dale Schenk, G. Levesque, Thekla S. Diehl, Peter Seubert, Dennis J. Selkoe, Paul E. Fraser, Billie J. Perry, Dora Kholodenko, Kelly Johnson-Wood, Robert Strome, Johanna M. Rommens, Soyeon Kim, Hong Yao, Angela Davis, Ruth Motter, Martin Citron, R. Sherrington, George A. Carlson, David Westaway, Michael K. Lee
Publikováno v:
Nature Medicine. 3:67-72
The mechanism by which mutations in the presenilin (PS) genes cause the most aggressive form of early-onset Alzheimer's disease (AD) is unknown, but fibroblasts from mutation carriers secrete increased levels of the amyloidogenic A beta 42 peptide, t
Autor:
Paul Bamborough, Frederick Cohen, Fruma Yehiely, Stanley B. Prusiner, Maria Da Costa, Gopal Thinakaran, Billie J. Perry, George A. Carlson
Publikováno v:
Neurobiology of Disease, Vol 3, Iss 4, Pp 339-355 (1997)
Neurobiology of Disease, Vol 10, Iss 1, Pp 67-68 (2002)
Neurobiology of Disease, Vol 10, Iss 1, Pp 67-68 (2002)
Prion diseases are disorders of protein conformation that produce neurodegeneration in humans and animals. Studies of transgenic (Tg) mice indicate that a factor designated protein X is involved in the conversion of the normal cellular prion protein