Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Valentyna Semenchenko"'
Autor:
Pallabi Sil Paul, Tark Patel, Jae-Young Cho, Allan Yarahmady, Aria Khalili, Valentyna Semenchenko, Holger Wille, Marianna Kulka, Sue-Ann Mok, Satyabrata Kar
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-16 (2024)
Abstract Evidence suggests that beta-amyloid (Aβ)-induced phosphorylation/aggregation of tau protein plays a critical role in the degeneration of neurons and development of Alzheimer’s disease (AD), the most common cause of dementia affecting the
Externí odkaz:
https://doaj.org/article/873e2f7dd82d41a68b93515e4db067ac
Autor:
Sibel Cetinel, Valentyna Semenchenko, Jae-Young Cho, Mehdi Ghaffari Sharaf, Karim F Damji, Larry D Unsworth, Carlo Montemagno
Publikováno v:
PLoS ONE, Vol 12, Iss 5, p e0177991 (2017)
Environmental factors, mainly oxidative stress and exposure to sunlight, induce the oxidation, cross-linking, cleavage, and deamination of crystallin proteins, resulting in their aggregation and, ultimately, cataract formation. Various denaturants ha
Externí odkaz:
https://doaj.org/article/e8321d5e8ad54813924221dc9d60a46d
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e54982 (2013)
Prion diseases are fatal neurodegenerative diseases associated with the conversion of cellular prion protein (PrP(C)) in the central nervous system into the infectious isoform (PrP(Sc)). The mechanics of conversion are almost entirely unknown, with u
Externí odkaz:
https://doaj.org/article/c8c7cc3e49c34e92a33a032908756d2e
Autor:
Steven D. Willows, Valentyna Semenchenko, Grant Norman, Michael T. Woodside, Valerie L. Sim, Marianna Kulka
Publikováno v:
The Journal of Immunology. 210:1447-1458
IgE Abs, best known for their role in allergic reactions, have only rarely been used in immunotherapies. Nevertheless, they offer a potential alternative to the more commonly used IgGs. The affinity of IgE Ag binding influences the type of response f
Publikováno v:
Journal of Allergy and Clinical Immunology. 149:AB55
Autor:
Carlo Montemagno, Karim F. Damji, Sibel Cetinel, Valentyna Semenchenko, Larry D. Unsworth, Mehdi Ghaffari Sharaf
Publikováno v:
Experimental Eye Research. 165:109-117
Crystallins are a major family of proteins located within the lens of the eye. Cataracts are thought to be due to the formation of insoluble fibrillar aggregates, which are largely composed of proteins from the crystallin family. Today the only catar
Autor:
Jae-Young Cho, Valentyna Semenchenko, Carlo D. Montemagno, Larry D. Unsworth, Sibel Cetinel, Karim F. Damji, Mehdi Ghaffari Sharaf
Publikováno v:
PLoS ONE, Vol 12, Iss 5, p e0177991 (2017)
PLoS ONE
PLoS ONE
Environmental factors, mainly oxidative stress and exposure to sunlight, induce the oxidation, cross-linking, cleavage, and deamination of crystallin proteins, resulting in their aggregation and, ultimately, cataract formation. Various denaturants ha
Autor:
Jack A. Tuszynski, Jonathan Y. Mane, Rolando Perez-Pineiro, Philip Winter, David S. Wishart, Valentyna Semenchenko
Publikováno v:
Chemical Biology & Drug Design. 82:60-70
The binding free energies on human tubulin of selected colchicine and thiocolchicine compounds were determined. Two methods were used for the determination of binding free energies: one is based on theoretical prediction simulating the dissociation o
Autor:
Valentyna Semenchenko, Rolando Perez-Pineiro, Bruce W. Fenske, Jack A. Tuszynski, Jonathan Y. Mane, David S. Wishart, Khaled Barakat, Douglas E. Friesen
Publikováno v:
Chemical Biology & Drug Design. 79:639-652
Recent studies have shown an overexpression of γ-tubulin in human glioblastomas and glioblastoma cell lines. As the 2-year survival rate for glioblastoma is very poor, potential benefit exists for discovering novel chemotherapeutic agents that can i
Autor:
Steven S. Plotkin, Neil R. Cashman, Edward Pokrishevsky, David S. Wishart, Ebrima Gibbs, Anat Yanai, Masoud Yousefi, Megan A. O'Neill, Leslie I. Grad, Valentyna Semenchenko, Will Guest
Publikováno v:
Proceedings of the National Academy of Sciences. 108:16398-16403
Human wild-type superoxide dismutase-1 (wtSOD1) is known to coaggregate with mutant SOD1 in familial amyotrophic lateral sclerosis (FALS), in double transgenic models of FALS, and in cell culture systems, but the structural determinants of this proce