Zobrazeno 1 - 10
of 152
pro vyhledávání: '"Alexey S, Ladokhin"'
Autor:
Alexey S. Ladokhin
Publikováno v:
BBA Advances, Vol 3, Iss , Pp 100093- (2023)
The current Special Issue entitled “Highlights of Ukrainian Molecular Biosciences” is dedicated to presenting recent contributions in the areas of biochemistry and biophysics, molecular biology and genetics, molecular and cellular physiology, and
Externí odkaz:
https://doaj.org/article/02c611c777754f6484501d6edd06abcb
Publikováno v:
BBA Advances, Vol 3, Iss , Pp 100076- (2023)
Permeabilization of the mitochondrial outer membrane–a point of no return in apoptotic regulation–is tightly controlled by proteins of the Bcl-2 family. Apoptotic inhibitor Bcl-xL is an important member of this family, responsible for blocking th
Externí odkaz:
https://doaj.org/article/b3fdaba1bb8b45beb1982cc152eca7b2
Autor:
Mykola V. Rodnin, Victor Vasques-Montes, Alexander Kyrychenko, Nuno F. B. Oliveira, Maithri M. Kashipathy, Kevin P. Battaile, Justin Douglas, Scott Lovell, Miguel Machuqueiro, Alexey S. Ladokhin
Publikováno v:
Toxins, Vol 15, Iss 7, p 410 (2023)
Protonation of key histidine residues has been long implicated in the acid-mediated cellular action of the diphtheria toxin translocation (T-) domain, responsible for the delivery of the catalytic domain into the cell. Here, we use a combination of c
Externí odkaz:
https://doaj.org/article/e62e1a5ad3bb4daab95b0257006a04fb
Autor:
Vivek Tyagi, Victor Vasquez-Montes, J. Alfredo Freites, Alexander Kyrychenko, Douglas J. Tobias, Alexey S. Ladokhin
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 17, p 9388 (2021)
The anti-apoptotic protein Bcl-xL regulates apoptosis by preventing the permeation of the mitochondrial outer membrane by pro-apoptotic pore-forming proteins, which release apoptotic factors into the cytosol that ultimately lead to cell death. Two di
Externí odkaz:
https://doaj.org/article/7e4a674630de4e418b35ae6cebd4c4f7
Publikováno v:
Data in Brief, Vol 12, Iss C, Pp 213-221 (2017)
This article supplies raw data related to a research article entitled “Joint refinement of FRET measurements using spectroscopic and computational tools” (Kyrychenko et al., 2017) [1], in which we demonstrate the use of molecular dynamics simulat
Externí odkaz:
https://doaj.org/article/c07bac29b36741f3966de9d5ede8b709
Publikováno v:
The Journal of Membrane Biology. 255:461-468
Dynamic disorder of the lipid bilayer presents a challenge for establishing structure-function relationships in membrane proteins, especially to those that insert by refolding from soluble states, e.g., bacterial toxins and Bcl-2 apoptotic regulators
Autor:
Mykola V. Rodnin, Maithri M. Kashipathy, Alexander Kyrychenko, Kevin P. Battaile, Scott Lovell, Alexey S. Ladokhin
Publikováno v:
Toxins, Vol 12, Iss 11, p 704 (2020)
Diphtheria toxin, an exotoxin secreted by Corynebacterium that causes disease in humans by inhibiting protein synthesis, enters the cell via receptor-mediated endocytosis. The subsequent endosomal acidification triggers a series of conformational cha
Externí odkaz:
https://doaj.org/article/048109f7b54b413aa2201ff716c83348
Autor:
Alexey S. Ladokhin
Publikováno v:
Cells, Vol 9, Iss 9, p 2121 (2020)
Apoptosis, a form of programmed cell death, is a highly regulated process critical for tissue development, homeostasis, and pathogenesis of various diseases [...]
Externí odkaz:
https://doaj.org/article/11c6cdf56600498eb1e66a36f9b567fb
Autor:
Victor Vasquez-Montes, Alexander Kyrychenko, Mauricio Vargas-Uribe, Mykola V. Rodnin, Alexey S. Ladokhin
Publikováno v:
Cells, Vol 9, Iss 3, p 539 (2020)
The inhibition of mitochondrial permeabilization by the anti-apoptotic protein Bcl-xL is crucial for cell survival and homeostasis. Its inhibitory role requires the partitioning of Bcl-xL to the mitochondrial outer membrane from an inactive state in
Externí odkaz:
https://doaj.org/article/74a5d35717bd477fbeb9256181c796ab
Role of Acidic Residues in Helices TH8–TH9 in Membrane Interactions of the Diphtheria Toxin T Domain
Autor:
Chiranjib Ghatak, Mykola V. Rodnin, Mauricio Vargas-Uribe, Andrew J. McCluskey, Jose C. Flores-Canales, Maria Kurnikova, Alexey S. Ladokhin
Publikováno v:
Toxins, Vol 7, Iss 4, Pp 1303-1323 (2015)
The pH-triggered membrane insertion of the diphtheria toxin translocation domain (T domain) results in transferring the catalytic domain into the cytosol, which is relevant to potential biomedical applications as a cargo-delivery system. Protonation
Externí odkaz:
https://doaj.org/article/df02cc8fece446b9b301fa8d675fc1f1