Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Saketh Chemuru"'
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
The elucidation of amyloid nucleation mechanisms remains challenging as early oligomeric intermediates are transient and difficult to distinguish. Here the authors use Aβ- polyglutamine hybrid peptides designed to slow and limit amyloid maturation t
Externí odkaz:
https://doaj.org/article/db9ce2df521e4e47a3b79fba5fc4d29d
Autor:
Martin Hubálek, Dhivya Ramakrishnan, Rudolf K. F. Beran, Saketh Chemuru, Henry W. Rohrs, Hyock Joo Kwon, Upasana Mehra, Weimei Xing, Iva Pichová, Michael L. Gross, Bruno Marchand, Michal Doležal, Anita Niedziela-Majka, Aleš Zábranský, Simon P. Fletcher
Publikováno v:
Journal of Virology
The structural maintenance of chromosomes 5/6 complex (Smc5/6) is a host restriction factor that suppresses HBV transcription. HBV counters this restriction by expressing HBV X protein (HBx), which redirects a host ubiquitin ligase to target Smc5/6 f
Autor:
Ronald, Wetzel, Saketh, Chemuru, Pinaki, Misra, Ravi, Kodali, Smita, Mukherjee, Karunakar, Kar
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1777
The red shift in the fluorescence excitation spectra of thioflavin dyes upon binding to fibrils has been a boon to the amyloid field, offering simple and effective methods for the qualitative detection of amyloid in tissue samples and for quantitatio
Publikováno v:
Methods in Molecular Biology ISBN: 9781493978090
The red shift in the fluorescence excitation spectra of thioflavin dyes upon binding to fibrils has been a boon to the amyloid field, offering simple and effective methods for the qualitative detection of amyloid in tissue samples and for quantitatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e4ca6e082815f5405a9ad760daee1776
https://doi.org/10.1007/978-1-4939-7811-3_6
https://doi.org/10.1007/978-1-4939-7811-3_6
Publikováno v:
Peptide Science. 102:206-221
Many amyloidogenic peptides are highly hydrophobic, introducing significant challenges to obtaining high quality peptides by chemical synthesis. For example, while good yield and purity can be obtained in the solid phase synthesis of the Alzheimer’
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-15 (2016)
Since early oligomeric intermediates in amyloid assembly are often transient and difficult to distinguish, characterize and quantify, the mechanistic basis of the initiation of spontaneous amyloid growth is often opaque. We describe here an approach
Publikováno v:
Journal of Molecular Biology. 401:503-517
The aggregated, β-sheet rich amyloid structure represents a stable, alternatively folded state of polypeptides. Amyloid fibrils are associated with several important neurodegenerative diseases, such as Alzheimer’s and Huntington’s diseases 1, as
Aβ43, a product of the proteolysis of the amyloid precursor protein APP, is related to Aβ42 by an additional Thr residue at the C-terminus. Aβ43 is typically generated at low levels compared with the predominant Aβ42 and Aβ40 forms, but it has b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7312e693576f11cbb78d1b1c8330d18f
https://europepmc.org/articles/PMC4691432/
https://europepmc.org/articles/PMC4691432/