Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Megan Murray Gessel"'
Publikováno v:
International Journal of Mass Spectrometry. 413:52-60
In living organisms all peptides and proteins used endogenously are homochiral. However, heterochiral peptides, formed by post-translational modifications in some species, are used exclusively exogenously. These puzzling facts, accomplished at signif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7517b6d97e5d4c585b96b72c921dd12b
https://doi.org/10.1016/j.ijms.2016.08.002
https://doi.org/10.1016/j.ijms.2016.08.002
Autor:
Dennis L. Wright, Meagan L. Wisniewski, Xueyun Zheng, Kishore Viswanathan, Ben A. Bahr, Michael T. Bowers, Megan Murray Gessel
Publikováno v:
Journal of Biological Chemistry. 287:6084-6088
The oligomerization of the amyloid-β protein (Aβ) is an important event in Alzheimer disease (AD) pathology. Developing small molecules that disrupt formation of early oligomeric states of Aβ and thereby reduce the effective amount of toxic oligom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a204e956c84d13694b087dbe043d120d
https://doi.org/10.1074/jbc.c111.328575
https://doi.org/10.1074/jbc.c111.328575
Publikováno v:
Biochemistry. 51:108-117
Recently, certain C-terminal fragments (CTFs) of Aβ42 have been shown to be effective inhibitors of Aβ42 toxicity. Here, we examine the interactions between the shortest CTF in the original series, Aβ(39-42), and full-length Aβ. Mass spectrometry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16d3980d1ab75fd14a9845830fd2687a
https://doi.org/10.1021/bi201520b
https://doi.org/10.1021/bi201520b
Publikováno v:
Gessel, MM; Bernstein, S; Kemper, M; Teplow, DB; & Bowers, MT. (2012). Familial Alzheimers disease mutations differentially alter amyloid β-protein oligomerization. ACS Chemical Neuroscience, 3(11), 909-918. doi: 10.1021/cn300050d. UC Santa Barbara: Retrieved from: http://www.escholarship.org/uc/item/4v17s2b9
Although most cases of Alzheimers disease (AD) are sporadic, ∼5% of cases are genetic in origin. These cases, known as familial Alzheimers disease (FAD), are caused by mutations that alter the rate of production or the primary structure of the amyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbc88bc5a587bb8135e7beabd5fe9d47
https://europepmc.org/articles/PMC3503339/
https://europepmc.org/articles/PMC3503339/
Initiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study
Autor:
Stuart C. Feinstein, Michael T. Bowers, Thanh D. Do, Luca Larini, Nichole E. LaPointe, Megan Murray Gessel, Joan-Emma Shea
Publikováno v:
Physical Chemistry Chemical Physics. 15:8916
The microtubule associated protein tau is essential for the development and maintenance of the nervous system. Tau dysfunction is associated with a class of diseases called tauopathies, in which tau is found in an aggregated form. This paper focuses
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4377eefbd7e7cc89a5d0900de7f0443
https://doi.org/10.1039/c3cp00063j
https://doi.org/10.1039/c3cp00063j