Zobrazeno 1 - 10
of 253
pro vyhledávání: '"Robert Tycko"'
Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract Self-assembly of amyloid-β peptides leads to oligomers, protofibrils, and fibrils that are likely instigators of neurodegeneration in Alzheimer’s disease. We report results of time-resolved solid state nuclear magnetic resonance (ssNMR) a
Externí odkaz:
https://doaj.org/article/411364f4d8c9418088ffbbf28ca44e2f
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
The low-complexity (LC) domain mediates liquid-liquid phase separation and fibril formation of the RNA-binding protein FUS (FUsed in Sarcoma). Here, the authors combine cryo-EM, solid-state NMR measurements and MD simulations to structurally characte
Externí odkaz:
https://doaj.org/article/8142805573524157b65818c9f357da0e
Autor:
Katelyn Nagy-Smith, Peter J. Beltramo, Eric Moore, Robert Tycko, Eric M. Furst, Joel P. Schneider
Publikováno v:
ACS Central Science, Vol 3, Iss 6, Pp 586-597 (2017)
Externí odkaz:
https://doaj.org/article/f24ec97276de4d2bb99088eab039dc1a
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Fibrils formed by the 42-residue amyloid-β peptide (Aβ42), a main component of amyloid deposits in Alzheimer's disease (AD), are known to be polymorphic, i.e., to contain multiple possible molecular structures. Previous studies of Aβ42 fibrils, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::155ba757a91a0b9c1095f2b0cfb48358
https://doi.org/10.1073/pnas.2218831120
https://doi.org/10.1073/pnas.2218831120
Autor:
C. Blake Wilson, Robert Tycko
Publikováno v:
J Am Chem Soc
Elucidation of the detailed mechanisms by which biological macromolecules undergo major structural conversions, such as folding, complex formation, and self-assembly, is a central concern of biophysical chemistry that will benefit from new experiment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7f42d79d5b275240986aba35774ffdc
https://doi.org/10.1021/jacs.2c02704
https://doi.org/10.1021/jacs.2c02704
Publikováno v:
J Am Chem Soc
Previous studies have shown that racemic mixtures of 40- and 42-residue amyloid-β peptides (D,L-Aβ40 and D,L-Aβ42) form amyloid fibrils with accelerated kinetics and enhanced stability relative to their homochiral counterparts (L-Aβ40 and L-Aβ42
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cffb3089b07a127fd176f75ea218ec89
https://doi.org/10.1021/jacs.1c06339
https://doi.org/10.1021/jacs.1c06339
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 342
We review recent efforts to develop and apply an experimental approach to the structural characterization of transient intermediate states in biomolecular processes that involve large changes in molecular conformation or assembly state. This approach
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42f1468636abd1a115dc76c144e1fc37
https://pubmed.ncbi.nlm.nih.gov/35998398
https://pubmed.ncbi.nlm.nih.gov/35998398
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(22)
Spatial resolution in MRI is ultimately limited by the signal detection sensitivity of NMR, since resolution equal to ρiso in all three dimensions requires the detection of NMR signals from a volume ρiso3. With inductively detected NMR at room temp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdc8e849ceaf724718899d5026883f88
https://pubmed.ncbi.nlm.nih.gov/35605126
https://pubmed.ncbi.nlm.nih.gov/35605126
Publikováno v:
Proc Natl Acad Sci U S A
HIV-1 maturation involves conversion of the immature Gag polyprotein lattice, which lines the inner surface of the viral membrane, to the mature capsid protein (CA) lattice, which encloses the viral RNA. Maturation inhibitors such as bevirimat (BVM)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c038b2ac42c4cc5806c6a4300ca7617b
https://doi.org/10.1073/pnas.1917755117
https://doi.org/10.1073/pnas.1917755117
Autor:
Dylan T. Murray, Robert Tycko
Publikováno v:
Biochemistry, vol 59, iss 4
Biochemistry
Biochemistry
In aqueous solutions, the 214-residue low-complexity domain of the FUS protein (FUS-LC) is known to undergo liquid-liquid phase separation and also to self-assemble into amyloid-like fibrils. In previous work based on solid state nuclear magnetic res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c65121ba8246de6a802667bf7f05f13
https://doi.org/10.1021/acs.biochem.9b00892
https://doi.org/10.1021/acs.biochem.9b00892