Zobrazeno 1 - 10
of 141
pro vyhledávání: '"A. V. Rodnin"'
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
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
Autor:
Ladokhin, 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.
Publikováno v:
Toxins; Volume 15; Issue 7; Pages: 410
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
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:
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
Publikováno v:
J Membr Biol
Protegrin-1 (PG-1), an 18-residue β-hairpin stabilized by two disulfide bonds, is a member of a family of powerful antimicrobial peptides which are believed to act through membrane permeabilization. Here we used a combination of experimental and com
Publikováno v:
Proc Natl Acad Sci U S A
Regulation of apoptosis is tightly linked with the targeting of numerous Bcl-2 proteins to the mitochondrial outer membrane (MOM), where their activation or inhibition dictates cell death or survival. According to the traditional view of apoptotic re
Publikováno v:
Economy of Region
Èkonomika Regiona, Vol 15, Iss 4, Pp 1088-1102 (2019)
Èkonomika Regiona, Vol 15, Iss 4, Pp 1088-1102 (2019)
The high level of uncertainty in the Russian pharmaceutical competitive environment creates a necessity of using open data that indicate the degree of the organizations' technological competencies. The Analysis of the information on the organizations
Publikováno v:
Toxins, Vol 9, Iss 10, p 299 (2017)
Cellular entry of diphtheria toxin is a multistage process involving receptor targeting, endocytosis, and translocation of the catalytic domain across the endosomal membrane into the cytosol. The latter is ensured by the translocation (T) domain of t
Externí odkaz:
https://doaj.org/article/02ad09142ac943a98c8740987f568a53