Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Nelly B. Ilyina"'
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
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
Autor:
Elizaveta I. Grigorashvili, N. A. Ryabova, Alexey K. Surin, N. S. Katina, Nelly B. Ilyina, Olga M. Selivanova, M. Yu. Suvorina
Publikováno v:
Молекулярная биология. :51-61
As has been recently shown, the toxicity of protein aggregates is determined by their structure. Therefore, special attention has been focused on the search for factors that specify the structural features of formed amyloid fibrils. The effect of ami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22ccbe7a8fe539e29cdc4eca35a76b1f
https://doi.org/10.7868/s0026898418010081
https://doi.org/10.7868/s0026898418010081
Autor:
N. S. Katina, Victor V. Marchenkov, V. E. Bychkova, Anatoly S. Glukhov, Vitalii A. Balobanov, Nelly B. Ilyina, V.D. Vasiliev, Alexey D. Nikulin
Publikováno v:
Biophysical journal. 113(5)
Investigation of the molecular mechanisms underlying amyloid-related human diseases attracts close attention. These diseases, the number of which currently is above 40, are characterized by formation of peptide or protein aggregates containing a cros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b29c90693e0b5d9757c3e49b18c6eebe
https://pubmed.ncbi.nlm.nih.gov/28877500
https://pubmed.ncbi.nlm.nih.gov/28877500
Autor:
Vitaly A. Balobanov, I. A. Kashparov, V.D. Vasiliev, Nelly B. Ilyina, V. E. Bychkova, N. S. Katina
Publikováno v:
Biochemistry (Moscow). 76:555-563
Formation of amyloid-like protein aggregates in human organs and tissues underlies many serious diseases, therefore being in the focus of numerous biochemical, medical, and molecular biological studies. So far, formation of amyloids by globular prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d85029d7c277d160645f01399279507b
https://doi.org/10.1134/s0006297911050051
https://doi.org/10.1134/s0006297911050051
Publikováno v:
Molecular Biology. 39:292-297
Equilibrium unfolding of apomyoglobin (ApoMb) in the presence of urea was studied as dependent on the temperature (5–2°C) at two pH values (5.7 and 6.2). Thermodynamic parameters of ApoMb transition from the native to the unfolded state were estim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6b7efd43699d48325c53af055e635ed6
https://doi.org/10.1007/s11008-005-0041-9
https://doi.org/10.1007/s11008-005-0041-9
Autor:
Vitaly A. Balobanov, Anna Egorova, Nelly B. Ilyina, Rita V. Chertkova, Victor D. Vasilyev, V. E. Bychkova
Publikováno v:
Biophysical Journal. 102:254a
As shown previously, practically every protein can form amyloid structures in appropriate conditions. It is of great interest to investigate fusion proteins because they are used to produce target proteins. This study is focused on amyloid formation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e5f83b3f73227f69f1df98675fd5c90
https://doi.org/10.1016/j.bpj.2011.11.1401
https://doi.org/10.1016/j.bpj.2011.11.1401
Publikováno v:
Biophysical Journal. 100:397a
The protein structure can be strongly influenced by phospholipid membranes. As it follows from our papers, apomyoglobin structure undergoes a transition from the native to some intermediate state upon interaction with small negatively charged phospho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d72b506c233eb9af7be234398bcfcd85
https://doi.org/10.1016/j.bpj.2010.12.2357
https://doi.org/10.1016/j.bpj.2010.12.2357
Autor:
Vitaly A. Balobanov, Yakov S. Anisimov, Rita V. Chertkova, Victor D. Vasilyev, V. E. Bychkova, Nelly B. Ilyina
Publikováno v:
Biophysical Journal. 98:254a
It is suggested that partially folded states play a key role in amyloid formation. So, it was of special interest to investigate a protein the “wild” type of which is initially in this state. Albebetin, a de novo protein, is an example of such pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b81202e7a125b89f7f4906b65af6596
https://doi.org/10.1016/j.bpj.2009.12.1381
https://doi.org/10.1016/j.bpj.2009.12.1381