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Публикации - Белки

Comprehensive proteomic analysis and pathogenic role of membrane vesicles of Listeria monocytogenes serotype 4b reveals proteins associated with virulence and their possible interaction with host
Raman Karthikeyan, Pratapa Gayathri, Paramasamy Gunasekaran, Medicharla V. Jagannadham, Jeyaprakash Rajendhran
International Journal of Medical Microbiology, 2019, ISSN: 1438-4221, DOI: 10.1016/j.ijmm.2019.03.008

http://www.sciencedirect.com/science/article/pii/S1438422118305812
Модель прибора: Photocor Complex


Use of Water Proton NMR to Characterize Protein Aggregates: Gauging the Response and Sensitivity
Marc B. Taraban, Roberto A. DePaz, Brian Lobo, Yihua Bruce Yu
Analytical Chemistry, 2019, ISSN: 0003-2700, DOI: 10.1021/acs.analchem.8b05733

https://doi.org/10.1021/acs.analchem.8b05733
Модель прибора: Photocor Complex


Effect of organic and inorganic salt environment on the complex coacervation of in situ formed protein nanoparticles and DNA
Pankaj Kumar Pandey, Priyanka Kaushik, Kamla Rawat, H. B. Bohidar
International Journal of Biological Macromolecules, 2018, ISSN: 0141-8130, DOI: 10.1016/j.ijbiomac.2018.09.088

http://www.sciencedirect.com/science/article/pii/S0141813018336936
Модель прибора: Photocor Complex


Effect of iron oxide nanoparticles on the concentration-versus-sizes relation of proteins in the blood plasma and serum, and in model solutions
M. N. Kirichenko, N. A. Bulychev, L. L. Chaikov, M. A. Kazaryan, A. V. Masalov
XIII International Conference on Atomic and Molecular Pulsed Lasers, 2018, Том: 10614, Стр.: 106140M, DOI: 10.1117/12.2303471

https://www.spiedigitallibrary.org/conference-proceedings-of-spie/10614/106140M/Effect-of-iron-oxide-nanoparticles-on-the-concentration-versus-sizes/10.1117/12.2303471.short
Модель прибора: Photocor FC


Interaction of DDP with bovine serum albumin facilitates formation of the protein dimers
I. Belaya, E. Chikhirzhina, A. Polyanichko
Journal of Molecular Structure, 2017, ISSN: 0022-2860, Том: 1140, Стр.: 148-153, DOI: 10.1016/j.molstruc.2016.12.107

http://www.sciencedirect.com/science/article/pii/S0022286016314260
Модель прибора: Photocor Complex


Alumina nanoparticle-assisted enzyme refolding: A versatile methodology for proteins renaturation
Katerina V. Volodina, David Avnir, Vladimir V. Vinogradov
Scientific Reports, 2017, ISSN: 2045-2322, Том: 7, DOI: 10.1038/s41598-017-01436-6

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431136/
Модель прибора: Photocor Compact-Z


Clusterin: full-length protein and one of its chains show opposing effects on cellular lipid accumulation
Suvarsha Rao Matukumalli, Ramakrishna Tangirala, C. M. Rao
Scientific Reports, 2017, ISSN: 2045-2322, Том: 7, Стр.: 41235, DOI: 10.1038/srep41235

http://www.nature.com/srep/2017/170125/srep41235/full/srep41235.html
Модель прибора: Photocor Complex


Water Proton NMR: A Tool for Protein Aggregation Characterization
Marc B. Taraban, Roberto A. DePaz, Brian Lobo, Y. Bruce Yu
Analytical Chemistry, 2017, ISSN: 0003-2700, Том: 89, Выпуск: 10, Стр.: 5494-5502, DOI: 10.1021/acs.analchem.7b00464

http://dx.doi.org/10.1021/acs.analchem.7b00464
Модель прибора: Photocor Complex


Interaction of Plasma Proteins with ZnSe and ZnSe@ZnS Core-Shell Quantum Dots
Irshad Ahmed Mir, Kamla Rawat, H. B. Bohidar
Colloids and Surfaces A: Physicochemical and Engineering Aspects, 2017, ISSN: 0927-7757, DOI: 10.1016/j.colsurfa.2017.01.032

http://www.sciencedirect.com/science/article/pii/S0927775717300614
Модель прибора: Photocor Complex


Caesalpinia bonduc serine proteinase inhibitor CbTI–2: Exploring the conformational features and antimalarial activity
Arindam Bhattacharyya, C. R. Babu
International Journal of Biological Macromolecules, 2017, ISSN: 0141-8130, DOI: 10.1016/j.ijbiomac.2017.05.044

http://www.sciencedirect.com/science/article/pii/S0141813016324436
Модель прибора: Photocor Complex