Výsledky vyhledávání - "George B, Benedek"

Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and Neurotoxicity

Autor: Panchanan Maiti, Aleksey Lomakin, Margaret M. Condron, Xueyun Zheng, Michael T. Bowers, David B. Teplow, Robin Roychaudhuri, George B. Benedek, Gal Bitan

Publikováno v: ACS chemical neuroscience, vol 6, iss 12
Roychaudhuri, R; Zheng, X; Lomakin, A; Maiti, P; Condron, MM; Benedek, GB; et al.(2015). Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and Neurotoxicity. ACS Chemical Neuroscience, 6(12), 1941-1955. doi: 10.1021/acschemneuro.5b00180. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4tn327rk

© 2015 American Chemical Society. A variety of species express the amyloid β-protein (Aβ (the term A refers both to Aβ40 and Aβ42, whereas Aβ40 and Aβ42 refer to each isoform specifically). Those species expressing Aβ with primary structure i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25b2a300d3470aa0f68b2ba8396fdbe2
https://doi.org/10.1021/acschemneuro.5b00180

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Transformation of Oligomers of Lipidated Peptide Induced by Change in pH

Autor: Sonoko Kanai, Rainer Alex, George B. Benedek, Aleksey Lomakin, Ying Wang

Publikováno v: Molecular Pharmaceutics. 12:411-419

Oligomerization of lipidated peptides is of general scientific interest and is important in biomedical and pharmaceutical applications. We investigated the solution properties of a lipidated peptide, Liraglutide, which is one of the glucagon-like pep

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::748782ef2246446c6ca4eca26b9c381f
https://doi.org/10.1021/mp500519s

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Liquid-Liquid Phase Separation in Oligomeric Peptide Solutions

Autor: George B. Benedek, Rainer Alex, Ying Wang, Aleksey Lomakin, Sonoko Kanai

Publikováno v: Langmuir : the ACS journal of surfaces and colloids. 33(31)

Oligomeric peptides exist widely in living organisms and play a role in a broad range of biological functions. We report the first observation of liquid–liquid phase separation (LLPS) in peptide solutions, in particular, solutions of peptides consi

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https://pubmed.ncbi.nlm.nih.gov/28689408

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A beta dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies

Autor: Nur Alia Oktaviani, Aleksey Lomakin, Frans A. A. Mulder, Dainan Zhang, Tiernan T. O'Malley, Brian O'Nuallain, George B. Benedek, Michael J. Rowan, Dominic M. Walsh, Sara Linse

Publikováno v: Biochemical Journal, 461(3), 413-426. PORTLAND PRESS LTD
O'Malley, T T, Oktaviani, N A, Zhang, D, Lomakin, A, O'Nuallain, B, Linse, S, Benedek, G B, Rowan, M J, Mulder, F A A & Walsh, D M 2014, ' Aβ dimers differ from monomers in structural propensity, aggregation paths and population of synaptotoxic assemblies ', Biochemical Journal, vol. 461, no. 3, pp. 413-426 . https://doi.org/10.1042/BJ20140219

Dimers of A beta (amyloid beta-protein) are believed to play an important role in Alzheimer's disease. In the absence of sufficient brain-derived dimers, we studied one of the only possible dimers that could be produced in vivo, [A beta](DiY) (dityro

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https://research.rug.nl/en/publications/bbbcefdf-1029-41b3-991e-665d37bc666c

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The ELISA-Measured Increase in Cerebrospinal Fluid Tau that Discriminates Alzheimer's Disease from other Neurodegenerative Disorders is not Attributable to Differential Recognition of Tau Assembly Forms

Autor: Henrik Zetterberg, Dominic M. Walsh, Aleksey Lomakin, Johan Svensson, Timothy Lynch, Omar M. El Agnaf, Mustafa T. Ardah, Per Johansson, Seán O'Dowd, Kinley Roberts, Gemma Cummins, George B. Benedek

Publikováno v: Journal of Alzheimer's Disease. 33:923-928

Elevated cerebrospinal fluid concentrations of tau discriminate Alzheimer's disease from other neurodegenerative conditions. The reasons for this are unclear. While commercial assay kits are widely used to determine total-tau concentrations, little i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61865f7a2e429b183cf5b66429c9d074
https://doi.org/10.3233/jad-2012-121393

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C-Terminal Turn Stability Determines Assembly Differences between Aβ40 and Aβ42

Autor: Robin Roychaudhuri, Sally A. Frautschy, Atul Deshpande, George B. Benedek, David B. Teplow, Aleksey Lomakin, Mingfeng Yang, Gregory M. Cole

Publikováno v: Journal of Molecular Biology. 425:292-308

Oligomerization of the amyloid β-protein (Aβ) is a seminal event in Alzheimer’s disease (AD). Aβ42, which is only two amino acids longer than Aβ40, is particularly pathogenic. Why this is so has not been elucidated fully. We report here results

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https://doi.org/10.1016/j.jmb.2012.11.006

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Evaluation of effects of pH and ionic strength on colloidal stability of IgG solutions by PEG-induced liquid-liquid phase separation

Autor: Suresh Vunnum, Aleksey Lomakin, Julie A. Meyer, Ying Wang, George B. Benedek, Ramil F. Latypov, Ronald W. Thompson

Publikováno v: The Journal of chemical physics. 145(18)

Colloidal stability of IgG antibody solutions is important for pharmaceutical and medicinal applications. Solution pH and ionic strength are two key factors that affect the colloidal stability of protein solutions. In this work, we use a method based

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https://pubmed.ncbi.nlm.nih.gov/27846698

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Phase separation in solutions of monoclonal antibodies and the effect of human serum albumin

Autor: Aleksey Lomakin, Ying Wang, George B. Benedek, Ramil F. Latypov

Publikováno v: Proceedings of the National Academy of Sciences. 108:16606-16611

We report the observation of liquid-liquid phase separation in a solution of human monoclonal antibody, IgG2, and the effects of human serum albumin, a major blood protein, on this phase separation. We find a significant reduction of phase separation

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https://doi.org/10.1073/pnas.1112241108

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Mechanistic Investigation of the Inhibition of Aβ42 Assembly and Neurotoxicity by Aβ42 C-Terminal Fragments

Autor: George B. Benedek, Miao Tan, Aleksey Lomakin, Brigita Urbanc, Bernhard H. Monien, Sean M. Spring, Erica A. Fradinger, Huiyuan Li, Reeve Zemel, Gal Bitan, Cui-Wei Xie

Publikováno v: Biochemistry. 49:6358-6364

Oligomeric forms of amyloid beta-protein (Abeta) are key neurotoxins in Alzheimer's disease (AD). Previously, we found that C-terminal fragments (CTFs) of Abeta42 interfered with assembly of full-length Abeta42 and inhibited Abeta42-induced toxicity.

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https://doi.org/10.1021/bi100773g

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Phase behavior of mixtures of human lens proteins Gamma D and Beta B1

Autor: Ying Wang, Aleksey Lomakin, Jennifer J. McManus, Olutayo Ogun, George B. Benedek

Publikováno v: Proceedings of the National Academy of Sciences. 107:13282-13287

We have experimentally determined the coexistence surface characterizing the phase behavior of gammaD-betaB1-water ternary solutions. The coexistence surface fully describes the solution conditions, i.e., temperature, protein concentration, and prote

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https://doi.org/10.1073/pnas.1008353107

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