Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Vladimir Zamotin"'
Autor:
Kiran Yanamandra, Oleg Alexeyev, Vladimir Zamotin, Vaibhav Srivastava, Andrei Shchukarev, Ann-Christin Brorsson, Gian Gaetano Tartaglia, Thomas Vogl, Rakez Kayed, Gunnar Wingsle, Jan Olsson, Christopher M Dobson, Anders Bergh, Fredrik Elgh, Ludmilla A Morozova-Roche
Publikováno v:
PLoS ONE, Vol 4, Iss 5, p e5562 (2009)
BACKGROUND:The conversion of soluble peptides and proteins into polymeric amyloid structures is a hallmark of many age-related degenerative disorders, including Alzheimer's disease, type II diabetes and a variety of systemic amyloidoses. We report he
Externí odkaz:
https://doaj.org/article/9d7ef73e60f04cd6b63b0882068677f5
Publikováno v:
Nanomedicine: Nanotechnology, Biology and Medicine. 10:1243-1252
Drug release from 1,2-dipalmitoyl- sn -glycero-3-phosphocholine (DPPC) liposomes occurs close to the main transition temperature T m =41°C. The exact release temperature can be adjusted by additional lipids, which shift T m . A major issue is drug l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa7e6f3ea2192c5701144e3a1f2c08d7
https://doi.org/10.1016/j.nano.2014.03.013
https://doi.org/10.1016/j.nano.2014.03.013
Publikováno v:
Langmuir
Several techniques are available for making large unilamellar vesicles (LUV) with an average diameter of approximately 100 nm, widely employed as model biomembranes as well as vehicles for drug delivery. Here we describe the use of adaptive focused u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9a86ab16ceb5f26d6c89c09ee1623a1
http://juuli.fi/Record/0338093211
http://juuli.fi/Record/0338093211
Autor:
Irina A. Kostanyan, Olesya S. Moskaleva, Boris A. Margulis, Vladimir Zamotin, Ludmilla A. Morozova-Roche, Kiran Yanamandra, Anna L. Gharibyan
Publikováno v:
Journal of Molecular Biology. 365:1337-1349
Among the newly discovered amyloid properties, its cytotoxicity plays a key role. Lysozyme is a ubiquitous protein involved in systemic amyloidoses in vivo and forming amyloid under destabilising conditions in vitro. We characterized both oligomers a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::527e8910f57f579164ef856fa504e6e4
https://doi.org/10.1016/j.jmb.2006.10.101
https://doi.org/10.1016/j.jmb.2006.10.101
Autor:
Irina A. Kostanyan, Kirpichnikov Mp, Anna L. Gharibyan, Ludmilla A. Morozova-Roche, Marika A. Lavrikova, Natalia V. Gibanova, Vladimir Zamotin, Dmitry A. Dolgikh
Publikováno v:
FEBS Letters. 580:2451-2457
Prefibrillar cytotoxicity was suggested as a common amyloid characteristic. We showed two types of albebetin prefibrillar oligomers are formed during incubation at pH 7.3. Initial round-shaped oligomers consist of 10–15 molecules determined by atom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::078a4ada9d335d5a0a3f142eeb0e883c
https://doi.org/10.1016/j.febslet.2006.03.074
https://doi.org/10.1016/j.febslet.2006.03.074
Autor:
Mantas Malisauskas, Vladimir Zamotin, Ludmilla A. Morozova-Roche, Evaldas Liutkevicius, Adas Darinskas, Erik Lundgren, Johan Ostman
Publikováno v:
Journal of Biological Chemistry. 280:6269-6275
In amyloid diseases, it is not evident which protein aggregates induce cell death via specific molecular mechanisms and which cause damage because of their mass accumulation and mechanical properties. We showed that equine lysozyme assembles into sol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0547b1123db57988176fd36db621102
https://doi.org/10.1074/jbc.m407273200
https://doi.org/10.1074/jbc.m407273200
Autor:
Dmiltry A Dolgikh, Rita V. Chertkova, Irina A. Kostanyan, Ludmilla Morozova-Roche, Mantas Malisauskas, Marika A. Lavrikova, Kirpichnikov Mp, Anders Öhman, Vladimir Zamotin
Publikováno v:
Biochemistry. 43:9610-9619
We showed that the genetically engineered carrier-protein albebetin and its biologically active constructs with interferon-alpha(2) octapeptide LKEKKYSP or differentiation factor hexapeptide TGENHR are inherently highly amyloidogenic at physiological
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed1e901427266e9b3ac3d0e025e1a3da
https://doi.org/10.1021/bi0494121
https://doi.org/10.1021/bi0494121
Autor:
Mantas Malisauskas, Jana Jass, Vladimir Zamotin, Christopher M. Dobson, Wim Noppe, Ludmilla A. Morozova-Roche
Publikováno v:
Journal of Molecular Biology. 330:879-890
The calcium-binding equine lysozyme has been found to undergo conversion into amyloid fibrils during incubation in solution at acidic pH. At pH 4.5 and 57 degrees C, where equine lysozyme forms a partially unfolded molten globule state, the protein f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0395840455b5f84fcc58c0eda4835a9a
https://doi.org/10.1016/s0022-2836(03)00551-5
https://doi.org/10.1016/s0022-2836(03)00551-5
Autor:
Ann-Christin Brorsson, Thomas Vogl, Rakez Kayed, Kiran Yanamandra, Ludmilla A. Morozova-Roche, Christopher M. Dobson, Fredrik Elgh, Jan Olsson, Gunnar Wingsle, Anders Bergh, Oleg A. Alexeyev, Gian Gaetano Tartaglia, Andrei Shchukarev, Vladimir Zamotin, Vaibhav Srivastava
Publikováno v:
PLoS ONE, Vol 4, Iss 5, p e5562 (2009)
PLoS ONE
PLoS ONE
BACKGROUND: The conversion of soluble peptides and proteins into polymeric amyloid structures is a hallmark of many age-related degenerative disorders, including Alzheimer's disease, type II diabetes and a variety of systemic amyloidoses. We report h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb4c03e56594f083f558f1aac3193769
http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-45431
http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-45431
Autor:
Ludmilla Morozova-Roche, Adas Darinskas, Vladimir Zamotin, Anna L. Gharibyan, Irina A. Kostanyan, Mantas Malisauskas
Publikováno v:
Biochemistry. Biokhimiia. 71(5)
In the current study we investigated the molecular mechanisms of cytotoxicity of amyloid oligomers of horse milk lysozyme. We have shown that lysozyme forms soluble amyloid oligomers and protofibrils during incubation at pH 2.0 and 4.5 and 57 degrees
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17ad17d69231f277a4cd3e9aff36ede6
https://pubmed.ncbi.nlm.nih.gov/16732728
https://pubmed.ncbi.nlm.nih.gov/16732728