Zobrazeno 1 - 10
of 379
pro vyhledávání: '"Teplow, DB"'
Publikováno v:
Protein science : a publication of the Protein Society, vol 27, iss 8
Yu, X; Hayden, EY; Xia, M; Liang, O; Cheah, L; Teplow, DB; et al.(2018). Surface enhanced Raman spectroscopy distinguishes amyloid B-protein isoforms and conformational states. PROTEIN SCIENCE, 27(8), 1427-1438. doi: 10.1002/pro.3434. UCLA: Retrieved from: http://www.escholarship.org/uc/item/6mx5521q
Yu, X; Hayden, EY; Xia, M; Liang, O; Cheah, L; Teplow, DB; et al.(2018). Surface enhanced Raman spectroscopy distinguishes amyloid B-protein isoforms and conformational states. PROTEIN SCIENCE, 27(8), 1427-1438. doi: 10.1002/pro.3434. UCLA: Retrieved from: http://www.escholarship.org/uc/item/6mx5521q
Amyloid β-protein (Aβ) self-association is one process linked to the development of Alzheimer's disease (AD). Aβ peptides, including its most abundant forms, Aβ40 and Aβ42, are associated with the two predominant neuropathologic findings in AD,
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https://escholarship.org/uc/item/6mx5521q
https://escholarship.org/uc/item/6mx5521q
Autor:
Rentsendorj, A, Sheyn, J, Fuchs, D-T, Daley, D, Salumbides, BC, Schubloom, HE, Hart, NJ, Li, S, Hayden, EY, Teplow, DB, Black, KL, Koronyo, Y, Koronyo-Hamaoui, M
Publikováno v:
Rentsendorj, A; Sheyn, J; Fuchs, D-T; Daley, D; Salumbides, BC; Schubloom, HE; et al.(2018). A novel role for osteopontin in macrophage-mediated amyloid-beta clearance in Alzheimer's models. BRAIN BEHAVIOR AND IMMUNITY, 67, 163-180. doi: 10.1016/j.bbi.2017.08.019. UCLA: Retrieved from: http://www.escholarship.org/uc/item/7x21944x
Osteopontin (OPN), a matricellular immunomodulatory cytokine highly expressed by myelomonocytic cells, is known to regulate immune cell migration, communication, and response to brain injury. Enhanced cerebral recruitment of monocytes achieved throug
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http://www.escholarship.org/uc/item/7x21944x
http://www.escholarship.org/uc/item/7x21944x
Publikováno v:
Roychaudhuri, R; Huynh, T-PV; Whitaker, TR; Hodara, E; Condron, MM; & Teplow, DB. (2017). A Critical Role of Ser26 Hydrogen Bonding in A beta 42 Assembly and Toxicity. BIOCHEMISTRY, 56(48), 6321-6324. doi: 10.1021/acs.biochem.7b00772. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4rk8407b
Amyloid β-protein (Aβ) assembly is a seminal process in Alzheimer's disease. Elucidating the mechanistic features of this process is thought to be vital for the design and targeting of therapeutic agents. Computational studies of the most pathologi
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https://explore.openaire.eu/search/publication?articleId=od_______325::990c1299091c6f49a380e0acfbaece71
http://www.escholarship.org/uc/item/4rk8407b
http://www.escholarship.org/uc/item/4rk8407b
Publikováno v:
Hayden, EY; Hoi, KK; Lopez, J; Inayathullah, M; Condron, MM; & Teplow, DB. (2017). Identification of key regions and residues controlling A beta folding and assembly. SCIENTIFIC REPORTS, 7. doi: 10.1038/s41598-017-10845-6. UCLA: Retrieved from: http://www.escholarship.org/uc/item/3j74j9dh
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http://www.escholarship.org/uc/item/3j74j9dh
http://www.escholarship.org/uc/item/3j74j9dh
Publikováno v:
Hayden, EY; Conovaloff, JL; Mason, A; Bitan, G; & Teplow, DB. (2017). Preparation of pure populations of covalently stabilized amyloid beta-protein oligomers of specific sizes. ANALYTICAL BIOCHEMISTRY, 518, 78-85. doi: 10.1016/j.ab.2016.10.026. UCLA: Retrieved from: http://www.escholarship.org/uc/item/9038v8nv
Evidence suggests that amyloid β-protein (Aβ) oligomers may be seminal pathogenic agents in Alzheimer's disease (AD). If so, developing oligomer-targeted therapeutics requires an understanding of oligomer structure. This has been difficult due to t
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https://explore.openaire.eu/search/publication?articleId=od_______325::ebc14aa6128775591be10ceb1ed36169
http://www.escholarship.org/uc/item/9038v8nv
http://www.escholarship.org/uc/item/9038v8nv
Autor:
Yamin, G, Teplow, DB
Publikováno v:
Yamin, G; & Teplow, DB. (2017). Pittsburgh Compound-B (PiB) binds amyloid beta-protein protofibrils. JOURNAL OF NEUROCHEMISTRY, 140(2), 210-215. doi: 10.1111/jnc.13887. UCLA: Retrieved from: http://www.escholarship.org/uc/item/70w4c2vn
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http://www.escholarship.org/uc/item/70w4c2vn
http://www.escholarship.org/uc/item/70w4c2vn
Publikováno v:
Yamin, G; Coppola, G; & Teplow, DB. (2016). Design, Characterization, and Use of a Novel Amyloid beta-Protein Control for Assembly, Neurotoxicity, and Gene Expression Studies. BIOCHEMISTRY, 55(36), 5049-5060. doi: 10.1021/acs.biochem.6b00579. UCLA: Retrieved from: http://www.escholarship.org/uc/item/7dh3p3tf
A key pathogenic agent in Alzheimer's disease (AD) is the amyloid β-protein (Aβ), which self-assembles into a variety of neurotoxic structures. Establishing structure-activity relationships for these assemblies, which is critical for proper therape
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http://www.escholarship.org/uc/item/7dh3p3tf
http://www.escholarship.org/uc/item/7dh3p3tf
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
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http://www.escholarship.org/uc/item/46z0d0ht
Publikováno v:
Watanabe-Nakayama, T; Ono, K; Itami, M; Takahashi, R; Teplow, DB; & Yamada, M. (2016). High-speed atomic force microscopy reveals structural dynamics of amyloid beta(1-42) aggregates. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(21), 5835-5840. doi: 10.1073/pnas.1524807113. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4hj587tm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::e39777dbe11e5c3151e87abc40fab374
http://www.escholarship.org/uc/item/4hj587tm
http://www.escholarship.org/uc/item/4hj587tm
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
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https://explore.openaire.eu/search/publication?articleId=od_______325::8a0292d57308b9cca3645f975ab9dcc4
http://www.escholarship.org/uc/item/15r3g68v
http://www.escholarship.org/uc/item/15r3g68v