Zobrazeno 1 - 10 of 4 905 pro vyhledávání: '"Teplow, DB"'
1
Akademický článek
Extracellular high molecular weight α-synuclein oligomers induce cell death by disrupting the plasma membrane.
Autor: Ito N; Department of Pharmacology, School of Medicine, Showa University, Tokyo, 142-8555, Japan.; Department of Internal Medicine, Division of Neurology, School of Medicine, Showa University, Tokyo, 142-8666, Japan., Tsuji M; Pharmacological Research Center, Showa University, Tokyo, 142-8555, Japan. tsujim@med.showa-u.ac.jp., Adachi N; Department of Physiology, School of Medicine, Showa University, Tokyo, 142-8555, Japan., Nakamura S; Department of Oral Physiology, School of Dentistry, Showa University, Tokyo, 142-8555, Japan., Sarkar AK; Department of Developmental Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, 45229-3026, USA., Ikenaka K; Department of Neurology, Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan., Aguirre C; Department of Neurology, Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan., Kimura AM; Brain Research Institute Center for Integrated Human Brain Science, Department of Functional Neurology and Neurosurgery, Niigata University, Niigata, 951-8122, Japan., Kiuchi Y; Department of Pharmacology, School of Medicine, Showa University, Tokyo, 142-8555, Japan.; Pharmacological Research Center, Showa University, Tokyo, 142-8555, Japan., Mochizuki H; Department of Neurology, Graduate School of Medicine, Osaka University, Osaka, 565-0871, Japan., Teplow DB; Department of Neurology, David Geffen School of Medicine, University of California-Los Angeles (UCLA), Los Angeles, LA, 10833, USA., Ono K; Department of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa University, Kanazawa, 920-8640, Japan. onoken@med.kanazawa-u.ac.jp.
Publikováno v: NPJ Parkinson's disease [NPJ Parkinsons Dis] 2023 Sep 28; Vol. 9 (1), pp. 139. Date of Electronic Publication: 2023 Sep 28.
Zobrazit plný text záznamu
2
Akademický článek
Structural Dynamics of Amyloid-β Protofibrils and Actions of Anti-Amyloid-β Antibodies as Observed by High-Speed Atomic Force Microscopy.
Autor: Watanabe-Nakayama T; WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan., Tsuji M; Pharmacological Research Center, Showa University, Tokyo 142-8555, Japan., Umeda K; WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan., Oguchi T; Pharmacological Research Center, Showa University, Tokyo 142-8555, Japan.; Department of Pharmacology, Division of Medical Pharmacology, School of Medicine, Showa University, Shinagawa-ku, Tokyo 142-8555, Japan., Konno H; WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan., Noguchi-Shinohara M; Department of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa University, 13-1, Takara-machi, Kanazawa 920-8640, Japan., Kiuchi Y; Pharmacological Research Center, Showa University, Tokyo 142-8555, Japan.; Department of Pharmacology, Division of Medical Pharmacology, School of Medicine, Showa University, Shinagawa-ku, Tokyo 142-8555, Japan., Kodera N; WPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan., Teplow DB; Department of Neurology, David Geffen School of Medicine at UCLA, University of California, 635 Charles E. Young Drive South, Los Angeles, California 90095-7334, United States., Ono K; Department of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa University, 13-1, Takara-machi, Kanazawa 920-8640, Japan.
Publikováno v: Nano letters [Nano Lett] 2023 Jul 12; Vol. 23 (13), pp. 6259-6268. Date of Electronic Publication: 2023 May 04.
Zobrazit plný text záznamu
3
Akademický článek
The effects of enhancing angiotensin converting enzyme in myelomonocytes on ameliorating Alzheimer's-related disease and preserving cognition.
Autor: Danziger R; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States.; Department of Neurology, Cedars-Sinai Medical Center, Los Angeles, CA, United States., Fuchs DT; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States., Koronyo Y; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States., Rentsendorj A; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States., Sheyn J; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States., Hayden EY; Department of Neurology, David Geffen School of Medicine at UCLA, Mary S. Easton Center for Alzheimer's Disease Research at UCLA, Brain Research Institute, Molecular Biology Institute, University of California, Los Angeles, CA, United States., Teplow DB; Department of Neurology, David Geffen School of Medicine at UCLA, Mary S. Easton Center for Alzheimer's Disease Research at UCLA, Brain Research Institute, Molecular Biology Institute, University of California, Los Angeles, CA, United States., Black KL; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States., Fuchs S; College of Osteopathic Medicine of the Pacific, Western University of Health Sciences, Pomona, CA, United States., Bernstein KE; Department of Biomedical Sciences, Cedars-Sinai Medical Center, Los Angeles, CA, United States.; Department of Pathology and Laboratory Medicine, Cedars-Sinai Medical Center, Los Angeles, CA, United States., Koronyo-Hamaoui M; Department of Neurosurgery, Maxine Dunitz Neurosurgical Institute, Cedars-Sinai Medical center, Los Angeles, CA, United States.; Department of Neurology, Cedars-Sinai Medical Center, Los Angeles, CA, United States.; Department of Biomedical Sciences, Cedars-Sinai Medical Center, Los Angeles, CA, United States.
Publikováno v: Frontiers in physiology [Front Physiol] 2023 Jun 23; Vol. 14, pp. 1179315. Date of Electronic Publication: 2023 Jun 23 (Print Publication: 2023).
Zobrazit plný text záznamu
4
Akademický článek
The Feasibility of Early Alzheimer's Disease Diagnosis Using a Neural Network Hybrid Platform.
Autor: Yu X; Department of Materials Science and Engineering, University of California, Los Angeles, CA 90095, USA., Srivastava S; Department of Materials Science and Engineering, University of California, Los Angeles, CA 90095, USA., Huang S; Department of Materials Science and Engineering, University of California, Los Angeles, CA 90095, USA., Hayden EY; Department of Neurology, David Geffen School of Medicine at UCLA, University of California, Los Angeles, CA 90095, USA., Teplow DB; Department of Neurology, David Geffen School of Medicine at UCLA, University of California, Los Angeles, CA 90095, USA., Xie YH; Department of Materials Science and Engineering, University of California, Los Angeles, CA 90095, USA.; Jonsson Comprehensive Cancer Center, University of California, Los Angeles, CA 90095, USA.
Publikováno v: Biosensors [Biosensors (Basel)] 2022 Sep 13; Vol. 12 (9). Date of Electronic Publication: 2022 Sep 13.
Zobrazit plný text záznamu
5
Surface enhanced Raman spectroscopy distinguishes amyloid Β-protein isoforms and conformational states
Autor: Yu, X, Hayden, EY, Xia, M, Liang, O, Cheah, L, Teplow, DB, Xie, Y-H
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
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,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::ae48530dc6ec4b5a947ba82fc5703fa2
https://escholarship.org/uc/item/6mx5521q
Zobrazit plný text záznamu
6
A Critical Role of Ser26 Hydrogen Bonding in A beta 42 Assembly and Toxicity
Autor: Roychaudhuri, R, Huynh, T-PV, Whitaker, TR, Hodara, E, Condron, MM, Teplow, DB
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
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::990c1299091c6f49a380e0acfbaece71
http://www.escholarship.org/uc/item/4rk8407b
Zobrazit plný text záznamu
7
Identification of key regions and residues controlling A beta folding and assembly
Autor: Hayden, EY, Hoi, KK, Lopez, J, Inayathullah, M, Condron, MM, Teplow, DB
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
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::08398b4425855ec0fd4d5b7a7fc39144
http://www.escholarship.org/uc/item/3j74j9dh
Zobrazit plný text záznamu
8
Preparation of pure populations of covalently stabilized amyloid beta-protein oligomers of specific sizes
Autor: Hayden, EY, Conovaloff, JL, Mason, A, Bitan, G, Teplow, DB
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
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::ebc14aa6128775591be10ceb1ed36169
http://www.escholarship.org/uc/item/9038v8nv
Zobrazit plný text záznamu
9
Pittsburgh Compound-B (PiB) binds amyloid beta-protein protofibrils
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
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::fb88d593014204916d68a7f7b5856535
http://www.escholarship.org/uc/item/70w4c2vn
Zobrazit plný text záznamu
10
A novel role for osteopontin in macrophage-mediated amyloid-beta clearance in Alzheimer's models
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
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______325::7a60a25b9b6bdf43d6fd2eae7e8e7c86
http://www.escholarship.org/uc/item/7x21944x
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje