Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Gia G. Maisuradze"'
Autor:
Steve Tyler, Christophe Laforge, Adrien Guzzo, Adrien Nicolaï, Gia G. Maisuradze, Patrick Senet
Publikováno v:
Molecules, Vol 28, Iss 18, p 6659 (2023)
The folded structures of proteins can be accurately predicted by deep learning algorithms from their amino-acid sequences. By contrast, in spite of decades of research studies, the prediction of folding pathways and the unfolded and misfolded states
Externí odkaz:
https://doaj.org/article/1e0a764c1a2c48d6be7cb56a2de89458
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
α-Synuclein is a 140 amino-acid intrinsically disordered protein mainly found in the brain. Toxic α-synuclein aggregates are the molecular hallmarks of Parkinson’s disease. In vitro studies showed that α-synuclein aggregates in oligomeric struct
Externí odkaz:
https://doaj.org/article/c3eb8fd9f12c465f8453ba015b6785a7
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
α-Synuclein is an intrinsically disordered protein occurring in different conformations and prone to aggregate in β-sheet structures, which are the hallmark of the Parkinson disease. Missense mutations are associated with familial forms of this neu
Externí odkaz:
https://doaj.org/article/112f16c14a3c47bbb2e9336e93c00391
Exploring Structural Flexibility and Stability of α-Synuclein by the Landau-Ginzburg-Wilson Approach
Autor:
Anatolii Korneev, Alexander Begun, Sergei Liubimov, Khatuna Kachlishvili, Alexander Molochkov, Antti J. Niemi, Gia G. Maisuradze
Publikováno v:
The journal of physical chemistry. B. 126(36)
α-Synuclein (αS) is the principal protein component of the Lewy body and Lewy neurite deposits that are found in the brains of the victims of one of the most prevalent neurodegenerative disorders, Parkinson's disease. αS can be qualified as a cham
Publikováno v:
ACS Chem Neurosci
Abnormal aggregation of the Amyloid β (Aβ) peptides into fibrils play a critical role in the development of Alzheimer’s disease. A two-stage “dock-lock” model have been proposed for the Aβ fibril elongation process. However, the mechanisms o
Publikováno v:
The Journal of Physical Chemistry B. 127:2879-2880
Autor:
Luka Maisuradze, Gia G. Maisuradze
Publikováno v:
The Protein Journal. 40:140-147
The analytical expression for the Voigt profile, along with its simplified forms for the Gaussian and Lorentzian dominance, is presented. The applicability of the Voigt profile in the description of anomalous diffusion phenomena, ubiquitous in differ
Autor:
Adrien, Guzzo, Patrice, Delarue, Ana, Rojas, Adrien, Nicolaï, Gia G, Maisuradze, Patrick, Senet
Publikováno v:
Frontiers in molecular biosciences. 9
Autor:
Antti J. Niemi, Khatuna Kachlishvili, Luka Maisuradze, Patrick Senet, Anatolii Korneev, Harold A. Scheraga, Jiaojiao Liu, Alexander Molochkov, Gia G. Maisuradze
Publikováno v:
J Phys Chem B
Intermediate states in protein folding are associated with formation of amyloid fibrils, which are responsible for a number of neurodegenerative diseases. Therefore, prevention of the aggregation of folding intermediates is one of the most important
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2340
Protein aggregation is the cause of many, often lethal, diseases, including the Alzheimer's, Parkinson's, and Huntington's diseases, and familial amyloidosis. Theoretical investigation of the mechanism of this process, including the structures of the