Zobrazeno 1 - 10
of 53
pro vyhledávání: '"Victor V. Marchenkov"'
Autor:
Olga M. Selivanova, Elizaveta I. Grigorashvili, Mariya Yu. Suvorina, Ulyana F. Dzhus, Alexey D. Nikulin, Victor V. Marchenkov, Alexey K. Surin, Oxana V. Galzitskaya
Publikováno v:
Data in Brief, Vol 8, Iss , Pp 108-113 (2016)
The data presented in this article are related to the research article entitled “One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42” (Dovidchenko et al., 2016)
Externí odkaz:
https://doaj.org/article/0c5a23618d29459893cf9b413d1131af
Autor:
Bogdan S. Melnik, Natalya S. Katina, Natalya A. Ryabova, Victor V. Marchenkov, Tatiana N. Melnik, Natalya E. Karuzina, Elena V. Nemtseva
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 23; Pages: 14645
Many proteins form amyloid fibrils only under conditions when the probability of transition from a native (structured, densely packed) to an intermediate (labile, destabilized) state is increased. It implies the assumption that some structural interm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d6b938887b56c67d87c8b08ca9bf1cc
https://pubmed.ncbi.nlm.nih.gov/36498970
https://pubmed.ncbi.nlm.nih.gov/36498970
Publikováno v:
Microbiology. 89:520-531
The structures of exo-oligosaccharides produced by a symbiotic nitrogen-fixing bacterium Rhizobium leguminosarum bv. viciae VF39 were determined using the methods of mass spectrometry and HCD fragmentation of ions. Exo-oligosaccharides were shown to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::efbbd0c214dc11a0b6515490ef537d1f
https://doi.org/10.1134/s0026261720050112
https://doi.org/10.1134/s0026261720050112
Autor:
Vitaly A. Balobanov, N. S. Katina, Nelly B. Ilyina, Anatoly S. Glukhov, Victor V. Marchenkov, Natalya Ryabova
Publikováno v:
Biomolecules, Vol 11, Iss 1608, p 1608 (2021)
Biomolecules
Volume 11
Issue 11
Biomolecules
Volume 11
Issue 11
The development of many severe human diseases is associated with the formation of amyloid fibrils. Most of the available information on the process of amyloid formation has been obtained from studies of small proteins and peptides, wherein the featur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e2edf922531bbb81447ed86fc3ead3c
https://www.mdpi.com/2218-273X/11/11/1608
https://www.mdpi.com/2218-273X/11/11/1608
Publikováno v:
Biochemical and Biophysical Research Communications. 516:1211-1215
It has been shown that spontaneous release of non-covalent flavins (from flavoenzymes) begins after isolation of mitochondria from rat liver, which is hydrolyzed to riboflavin. This process is stopped by 1 mM EDTA in the incubation medium. In the pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d7c2ccce1b7ff82f5302d99d10fa900
https://doi.org/10.1016/j.bbrc.2019.07.021
https://doi.org/10.1016/j.bbrc.2019.07.021
Autor:
Andrey S Sokolov, Oxana V. Galzitskaya, Ekaterina L. Nemashkalova, Eugene A. Permyakov, Alexei S. Kazakov, Ekaterina A. Litus, E.I. Galushko, S.E. Permyakov, Victor V. Marchenkov, Ulyana F. Dzhus
Publikováno v:
Biochemical and Biophysical Research Communications. 510:248-253
Human serum albumin (HSA) serves as a natural depot of amyloid β peptide (Aβ). Improvement of Aβ binding to HSA should impede Alzheimer's disease (AD). We developed a method for quantitation of the interaction between monomeric Aβ40/42 and HSA us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac81fe9d4b958c091bf2af425a0fcf9b
https://doi.org/10.1016/j.bbrc.2019.01.081
https://doi.org/10.1016/j.bbrc.2019.01.081
Autor:
Liliia Fakhranurova, Natalya Ryabova, Vitaly A. Balobanov, Anatoly S. Glukhov, Natalia Markelova, N. S. Katina, Victor V. Marchenkov, Nelly B. Ilyina
Publikováno v:
Biochemical and biophysical research communications. 524(2)
In most cases high cytotoxicity is characteristic of aggregates formed during lag phase of amyloid formation, whereas mature fibrils represent the depot of protein molecules incapable of damaging cell membranes. However, new experimental data show th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::447a645b01a3f703b85ebfba1493049f
https://pubmed.ncbi.nlm.nih.gov/32007272
https://pubmed.ncbi.nlm.nih.gov/32007272
Publikováno v:
Vestnik of Saint Petersburg University. Physics. Chemistry. 5:365-371
Работа поддержана программой президиума РАН «Клеточная и молекулярная биология» (проект № 01201358029) и Российским научным фондом (грант РН
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::976b7f93c1eb8a736a81b258403901c8
https://doi.org/10.21638/11701/spbu04.2016.403
https://doi.org/10.21638/11701/spbu04.2016.403
Publikováno v:
Молекулярная биология. :82-87
GroES is a heptameric partner of tetradecameric molecular chaperone GroEL, which ensures the correct folding and assembly of numerous cellular proteins both in vitro and in vivo. This work demonstrates the results of a study of structural aspects of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0913950fda9967ebc92a689911c92b70
https://doi.org/10.7868/s002689841801-0012
https://doi.org/10.7868/s002689841801-0012
Autor:
N. A. Ryabova, Alexey D. Nikulin, N. S. Katina, Elizaveta I. Grigorashvili, Victor V. Marchenkov, Alexey K. Surin, M. Yu. Suvorina
Publikováno v:
Journal of Analytical Chemistry. 72:1271-1279
The formation of amyloid aggregates in human organs and tissues causes the development of incurable diseases. However, experimental studies of the mechanism of amyloid formation by proteins and the structural characteristics of amyloids are complicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4746146e21717d1d18a18b6151ca750c
https://doi.org/10.1134/s1061934817130056
https://doi.org/10.1134/s1061934817130056