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Публикации - Белки

Acceleration of protein aggregation by amphiphilic peptides: Transformation of supramolecular structure of the aggregates
N. V. Artemova, V. A. Stein-Margolina, Z. M. Bumagina, B. Ya. Gurvits
Biotechnology Progress, 2011, ISSN: 1520-6033, Том: 27, Выпуск: 3, Стр.: 846-854, DOI: 10.1002/btpr.574

http://onlinelibrary.wiley.com/doi/10.1002/btpr.574/abstract


Влияние секретируемого белка Rpf на межклеточные контакты в культурах Micrococcus luteus и Mycobacterium smegmatis
В. Д. Никитушкин, Г. Р. Демина, А. С. Капрельянц
Микробиология, 2011, Том: 80, Выпуск: 2, Стр.: 155–161

https://elibrary.ru/item.asp?id=15638977


Single-stranded DNA binding protein from human malarial parasite Plasmodium falciparum is encoded in the nucleus and targeted to the apicoplast
Dhaneswar Prusty, Ashraf Dar, Rashmi Priya, Atul Sharma, Srikanta Dana, Nirupam Roy Choudhury, N. Subba Rao, Suman Kumar Dhar
Nucleic Acids Research, 2010, ISSN: 0305-1048, 1362-4962, Стр.: gkq565, DOI: 10.1093/nar/gkq565

http://nar.oxfordjournals.org/content/early/2010/06/22/nar.gkq565


Physicochemical properties of a new group of regulatory proteins isolated from various mammal tissues
I. A. Yamskov, I. V. Blagodatskikh, M. S. Krasnov, A. V. Borisenko, D. V. Margasyuk, V. V. Vecherkin, V. S. Skripnikova, P. A. Nazarova, S. A. Bitko, B. B. Berezin
Russian Chemical Bulletin, 2010, ISSN: 1066-5285, 1573-9171, Том: 58, Выпуск: 3, Стр.: 640-645, DOI: 10.1007/s11172-009-0069-4

http://link.springer.com/article/10.1007/s11172-009-0069-4


Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins
N. V. Artemova, Z. M. Bumagina, A. S. Kasakov, V. V. Shubin, B. Ya. Gurvits
Peptides, 2010, ISSN: 0196-9781, Том: 31, Выпуск: 2, Стр.: 332-338, DOI: 10.1016/j.peptides.2009.11.025

http://www.sciencedirect.com/science/article/pii/S0196978109005166


Исследование нанокомпозитов кремнеземов с белком как модельных лекарственных транспортных наносистем
Г. А. Куликова, Е. В. Парфенюк
Перспективные материалы, 2010, Выпуск: 9, Стр.: 132–136

https://elibrary.ru/item.asp?id=15290013


Modulators of activity of regulatory proteins acting at ultra low doses
V. P. Yamskova, M. S. Krasnov, V. S. Skripnikova, A. A. Molyavka, A. P. Il’ina, D. V. Margasyuk, A. V. Borisenko, B. B. Berezin, I. A. Yamskov
Cytology and Genetics, 2009, ISSN: 0095-4527, 1934-9440, Том: 43, Выпуск: 6, Стр.: 387-395, DOI: 10.3103/S0095452709060048

http://link.springer.com/article/10.3103/S0095452709060048


Mechanism of Suppression of Protein Aggregation by α-Crystallin
Kira A. Markossian, Igor K. Yudin, Boris I. Kurganov
International Journal of Molecular Sciences, 2009, Том: 10, Выпуск: 3, Стр.: 1314-1345, DOI: 10.3390/ijms10031314

http://www.mdpi.com/1422-0067/10/3/1314


Some properties of complexes formed by small heat shock proteins with denaturated actin
A. V. Pivovarova, N. A. Chebotareva, N. B. Gusev, D. I. Levitsky
Biophysics, 2009, ISSN: 0006-3509, 1555-6654, Том: 53, Выпуск: 5, Стр.: 361-365, DOI: 10.1134/S0006350908050072

http://link.springer.com/article/10.1134/S0006350908050072


Effect of dispersion structure variation on chemometrical calibration of near-infrared spectrometer: Protein fractions in milk and reversed micelles solutions
A. V. Kalinin, V. N. Krasheninnikov, A. V. Potapov
Chemometrics and Intelligent Laboratory Systems, 2009, ISSN: 0169-7439, Том: 97, Выпуск: 1, Стр.: 33-38, DOI: 10.1016/j.chemolab.2008.08.007

http://www.sciencedirect.com/science/article/pii/S0169743908001718