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Akademický článek

Development, Implementation, and Assessment of an Online Modular Telehealth Curriculum for Health Professions Students

Autor: Ostrovsky DA, Heflin MT, Bowers MT, Hudak NM, Leiman ER, Truong T, Waite K

Publikováno v: Advances in Medical Education and Practice, Vol Volume 15, Pp 743-753 (2024)

Daniel A Ostrovsky,1 Mitchell T Heflin,2 Margaret T Bowers,3 Nicholas M Hudak,4 Erin R Leiman,5 Tracy Truong,6 Kathleen Waite7 1Departments of Internal Medicine and Pediatrics, Duke University, Durham, NC, USA; 2Department of Medicine, Duke Universit

Externí odkaz: https://doaj.org/article/1e4aa571a1d849dcba19b43362c2d664

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Aggregation of Chameleon Peptides: Implications of alpha-Helicity in Fibril Formation

Autor: Kim, B, Do, TD, Hayden, EY, Teplow, DB, Bowers, MT, Shea, J-E

Publikováno v: Kim, B; Do, TD; Hayden, EY; Teplow, DB; Bowers, MT; & Shea, J-E. (2016). Aggregation of Chameleon Peptides: Implications of alpha-Helicity in Fibril Formation. JOURNAL OF PHYSICAL CHEMISTRY B, 120(26), 5874-5883. doi: 10.1021/acs.jpcb.6b00830. UCLA: Retrieved from: http://www.escholarship.org/uc/item/46z0d0ht

We investigate the relationship between the inherent secondary structure and aggregation propensity of peptides containing chameleon sequences (i.e., sequences that can adopt either α or β structure depending on context) using a combination of repl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::bf774f7f14680529b770b2aad6c7b33b
http://www.escholarship.org/uc/item/46z0d0ht

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Mechanism of C-Terminal Fragments of Amyloid beta-Protein as A beta Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?

Autor: Zheng, X, Wu, C, Liu, D, Li, H, Bitan, G, Shea, J-E, Bowers, MT

Publikováno v: Zheng, X; Wu, C; Liu, D; Li, H; Bitan, G; Shea, J-E; et al.(2016). Mechanism of C-Terminal Fragments of Amyloid beta-Protein as A beta Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?. JOURNAL OF PHYSICAL CHEMISTRY B, 120(8), 1615-1623. doi: 10.1021/acs.jpcb.5b08177. UCLA: Retrieved from: http://www.escholarship.org/uc/item/7595m688

Targeting the early oligomerization of amyloid β protein (Aβ) is a promising therapeutic strategy for Alzheimer's disease (AD). Recently, certain C-terminal fragments (CTFs) derived from Aβ42 were shown to be potent inhibitors of Aβ-induced toxic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::40fc7991e9560f597a3d8c163d485f91
http://www.escholarship.org/uc/item/7595m688

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Amyloid beta-Protein Assembly and Alzheimer's Disease: Dodecamers of A beta 42, but Not of A beta 40, Seed Fibril Formation

Autor: Economou, NJ, Giammona, MJ, Do, TD, Zheng, X, Teplow, DB, Buratto, SK, Bowers, MT

Publikováno v: Economou, NJ; Giammona, MJ; Do, TD; Zheng, X; Teplow, DB; Buratto, SK; et al.(2016). Amyloid beta-Protein Assembly and Alzheimer's Disease: Dodecamers of A beta 42, but Not of A beta 40, Seed Fibril Formation. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 138(6), 1772-1775. doi: 10.1021/jacs.5b11913. UCLA: Retrieved from: http://www.escholarship.org/uc/item/15r3g68v

Evidence suggests that oligomers of the 42-residue form of the amyloid β-protein (Aβ), Aβ42, play a critical role in the etiology of Alzheimer's disease (AD). Here we use high resolution atomic force microscopy to directly image populations of sma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::8a0292d57308b9cca3645f975ab9dcc4
http://www.escholarship.org/uc/item/15r3g68v

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Amyloid beta-Protein C-Terminal Fragments: Formation of Cylindrins and beta-Barrels

Autor: Do, TD, LaPointe, NE, Nelson, R, Krotee, P, Hayden, EY, Ulrich, B, Quan, S, Feinstein, SC, Teplow, DB, Eisenberg, D, Shea, J-E, Bowers, MT

Publikováno v: Do, TD; LaPointe, NE; Nelson, R; Krotee, P; Hayden, EY; Ulrich, B; et al.(2016). Amyloid beta-Protein C-Terminal Fragments: Formation of Cylindrins and beta-Barrels. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 138(2), 549-557. doi: 10.1021/jacs.5b09536. UCLA: Retrieved from: http://www.escholarship.org/uc/item/2dz88741

In order to evaluate potential therapeutic targets for treatment of amyloidoses such as Alzheimer's disease (AD), it is essential to determine the structures of toxic amyloid oligomers. However, for the amyloid β-protein peptide (Aβ), thought to be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::f175c770dd1fb59b4833533f8f455e5a
http://www.escholarship.org/uc/item/2dz88741

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Amyloid β-protein monomer structure: A computational and experimental study

Autor: Baumketner, A, Bernstein, SL, Wyttenbach, T, Bitan, G, Teplow, DB, Bowers, MT, Shea, JE

Publikováno v: Baumketner, A; Bernstein, SL; Wyttenbach, T; Bitan, G; Teplow, DB; Bowers, MT; et al.(2006). Amyloid β-protein monomer structure: A computational and experimental study. Protein Science, 15(3), 420-428. doi: 10.1110/ps.051762406. UCLA: Retrieved from: http://www.escholarship.org/uc/item/5kr1c4vg

The structural properties of the Aβ42 peptide, a main constituent of the amyloid plaques formed in Alzheimer's disease, were investigated through a combination of ion-mobility mass spectrometry and theoretical modeling. Replica exchange molecular dy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::56fb9b851a5142a4eb52d7d2a03ddbf8
http://www.escholarship.org/uc/item/5kr1c4vg

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