Zobrazeno 1 - 10
of 64
pro vyhledávání: '"H. Robert Guy"'
Autor:
H. Robert Guy
Publikováno v:
Open Access Government. 38:124-125
Understanding amyloid beta and Alzheimer's disease: the key to helping AD patients Efforts to prevent or treat Alzheimer's Disease (AD) by targeting Amyloid beta (Aβ) assemblies should be continued, but the strategies should be altered dramatically.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a4290d612145f5bc2d4dc0ecc0a9f55
https://doi.org/10.56367/oag-038-10431
https://doi.org/10.56367/oag-038-10431
Autor:
Stewart R. Durell, H. Robert Guy
Publikováno v:
Proteins
Amyloid beta (Aβ of Alzheimer's disease) and α-synuclein (α-Syn of Parkinson's disease) form large fibrils. Evidence is increasing however that much smaller oligomers are more toxic and that these oligomers can form transmembrane ion channels. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3bf638e45c1adf5b2d22d6b540c3a80
https://doi.org/10.1002/prot.26249
https://doi.org/10.1002/prot.26249
Publikováno v:
Proteins
Amyloid beta (Aβ) peptides are a major contributor to Alzheimers disease. They occur in differing lengths, each of which forms a multitude of assembly types. The most toxic soluble oligomers are formed by Aβ42; some of which have antiparallel β-sh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67cd68d0d9a7f97f34796781bf6eb357
https://pubmed.ncbi.nlm.nih.gov/35038191
https://pubmed.ncbi.nlm.nih.gov/35038191
Publikováno v:
Journal of Molecular Graphics and Modelling. 29:657-662
Amyloid-β (Aβ) oligomers appear to play a pivotal role in Alzheimer's disease. A 42 residue long alloform, Aβ42, is closely related to etiology of the disease. In vitro results show evidences of hexamers; however structures of these hexamers have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0efc4177341afa7c04cf165b8f8fbf57
https://doi.org/10.1016/j.jmgm.2010.11.008
https://doi.org/10.1016/j.jmgm.2010.11.008
Autor:
Sarosh N. Fatakia, Sergei Sukharev, Carson C. Chow, H. Robert Guy, Adina L. Milac, Andriy Anishkin
Publikováno v:
Channels. 5:23-33
Mechanosensitive TREK channels belong to the family of K2P channels, a family of widely distributed, well-modulated channels that uniquely have two similar or identical subunits, each with two TM1-P-TM2 motifs. Our goal is to build viable structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0d733b27243068f5bd7a47fa2e9b17f
https://doi.org/10.4161/chan.5.1.13905
https://doi.org/10.4161/chan.5.1.13905
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 78:3458-3472
Both soluble and membrane-bound pre-fibrillar assemblies of Abeta (Aβ) peptides have been associated with Alzheimer's disease (AD). The size and nature of theses assemblies vary greatly and are affected by many factors. Here we present models of sol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fad42320f29566371e4af686135f7758
https://doi.org/10.1002/prot.22832
https://doi.org/10.1002/prot.22832
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 78:3473-3487
Although it is clear that amyloid beta (Aβ) peptides play a pivotal role in the development of Alzheimer's disease, the precise molecular model of action remains unclear. Aβ peptide forms assemble both in aqueous solution and in lipid membranes. It
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dd1149b685288f18a43957835a54cd7
https://doi.org/10.1002/prot.22853
https://doi.org/10.1002/prot.22853
Publikováno v:
Biochemistry. 49:7847-7853
On the basis of the consistent demonstrations that the Abeta peptide of Alzheimer's disease forms calcium permeant channels in artificial membranes, we have proposed that the intracellular calcium increase observed in cells exposed to Abeta is initia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3be1902df34f4207a853ab97532fa0eb
https://doi.org/10.1021/bi1006833
https://doi.org/10.1021/bi1006833
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 78:932-949
Most crystallized homo-oligomeric ion channels are highly symmetric, which dramatically decreases conformational space and facilitates building homology models (HMs). However, in molecular dynamics (MD) simulations channels deviate from ideal symmetr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::190399cf70cfa7adf20ca32fd42aaa62
https://doi.org/10.1002/prot.22618
https://doi.org/10.1002/prot.22618