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1    2  3  4   Oligomeric state of αB-crystallin under crowded conditions
Natalia A. Chebotareva, Tatiana B. Eronina, Svetlana G. Roman, Valeriya V. Mikhaylova, Nikolai N. Sluchanko, Nikolai B. Gusev, Boris I. Kurganov
Biochemical and Biophysical Research Communications, 2018, ISSN: 0006-291X, DOI: 10.1016/j.bbrc.2018.12.015

http://www.sciencedirect.com/science/article/pii/S0006291X18326585
Instrument model: Photocor Complex


Ultrasonic disintegration of tungsten trioxide pseudomorphs after ammonium paratungstate as a route for stable aqueous sols of nanocrystalline WO3
T. O. Shekunova, A. E. Baranchikov, A. D. Yapryntsev, P. G. Rudakovskaya, O. S. Ivanova, Yu A. Karavanova, M. A. Kalinina, M. N. Rumyantseva, S. G. Dorofeev, V. K. Ivanov
Journal of Materials Science, 2017, ISSN: 0022-2461, 1573-4803, Pages: 1-11, DOI: 10.1007/s10853-017-1668-3

https://link.springer.com/article/10.1007/s10853-017-1668-3
Instrument model: Photocor Complex


From nanoparticles to bulk crystalline solid: nucleation, growth kinetics and crystallisation of mixed oxide ZrxTi1−xO2 nanoparticles
K. Cheng, K. Chhor, O. Brinza, D. Vrel, A. Kanaev
CrystEngComm, 2017, ISSN: 1466-8033, Issue: 0, DOI: 10.1039/C7CE00505A

http://pubs.rsc.org/en/content/articlelanding/2017/ce/c7ce00505a
Instrument model: Photocor FC


Quantification of anti-aggregation activity of UV-irradiated α-crystallin
Vera A. Borzova, Kira A. Markossian, Konstantin O. Muranov, Nikolay B. Polyansky, Sergey Yu. Kleymenov, Boris I. Kurganov
International Journal of Biological Macromolecules, 2015, ISSN: 0141-8130, Volume: 73, Pages: 84-91, DOI: 10.1016/j.ijbiomac.2014.10.060

http://www.sciencedirect.com/science/article/pii/S0141813014007454


Effect of crowding on several stages of protein aggregation in test systems in the presence of α-crystallin
Natalia A. Chebotareva, Dmitrii O. Filippov, Boris I. Kurganov
International Journal of Biological Macromolecules, 2015, ISSN: 0141-8130, Volume: 80, Pages: 358-365, DOI: 10.1016/j.ijbiomac.2015.07.002

http://www.sciencedirect.com/science/article/pii/S0141813015004638


Preparation of Nanocrystalline Powders of ZrO2, Stabilized by Y2O3 Dobs for Ceramics
V. F. Petrunin, S. A. Korovin
Physics Procedia, 2015, ISSN: 1875-3892, Volume: 72, Pages: 544-547, DOI: 10.1016/j.phpro.2015.09.050

http://www.sciencedirect.com/science/article/pii/S1875389215012201


Usage of Molybdenum Nanocrystalline Powder for Radioisotope Production
A. P. Ilyin, S. A. Korovin, L. I. Menshikov, V. F. Petrunin, A. N. Semenov, D. Yu Chuvilin
Physics Procedia, 2015, Volume: 72, Pages: 548–551, DOI: 10.1016/j.phpro.2015.09.055

http://www.sciencedirect.com/science/article/pii/S1875389215012250


Peculiarities of the coagulation mechanism of a nanocrystalline cellulose hydrosol and a latex
V. N. Verezhnikov, I. V. Ostankova, V. A. Kuznetsov
Colloid Journal, 2014, ISSN: 1061-933X, 1608-3067, Volume: 76, Issue: 6, Pages: 668-674, DOI: 10.1134/S1061933X14060192

http://link.springer.com/article/10.1134/S1061933X14060192


Transient transformation of oligomeric structure of alpha-crystallin during its chaperone action
Ekaterina Smirnova, Natalia Chebotareva, Bella Gurvits
International Journal of Biological Macromolecules, 2013, ISSN: 0141-8130, Volume: 55, Pages: 62-68, DOI: 10.1016/j.ijbiomac.2012.12.013

http://www.sciencedirect.com/science/article/pii/S0141813012004862


Natural Dipeptides as Mini-Chaperones: Molecular Mechanism of Inhibition of Lens βL-Crystallin Aggregation
Antonina K. Dizhevskaya, Konstantin O. Muranov, Alexander A. Boldyrev, Mikhail A. Ostrovsky
Current Aging Science, 2012, Volume: 5, Issue: 3, Pages: 236-241, DOI: 10.2174/1874609811205030011

http://www.eurekaselect.com/107507/article


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