Protein Translational Diffusion and Intermolecular Interactions of Globular and Intrinsically Unstructured Proteins
Aleksandra M. Kusova, Aleksandr E. Sitnitsky, Dzhigangir A Faizullin, Yuriy F. Zuev
The Journal of Physical Chemistry A, 2019, ISSN: 1089-5639, DOI: 10.1021/acs.jpca.9b08601
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
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
Quantification of Protein Aggregation Rate and Quenching effect in amylin-inhibitors complex
Suparna Khatun, Anurag Singh, Debabrata Mandal, Amreesh Chandra, Amar Nath Gupta
Physical Chemistry Chemical Physics, 2019, DOI: 10.1039/C9CP03238J
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
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
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
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
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
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
Aleksandra M. Kusova, Aleksandr E. Sitnitsky, Dzhigangir A Faizullin, Yuriy F. Zuev
The Journal of Physical Chemistry A, 2019, ISSN: 1089-5639, DOI: 10.1021/acs.jpca.9b08601
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
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
Quantification of Protein Aggregation Rate and Quenching effect in amylin-inhibitors complex
Suparna Khatun, Anurag Singh, Debabrata Mandal, Amreesh Chandra, Amar Nath Gupta
Physical Chemistry Chemical Physics, 2019, DOI: 10.1039/C9CP03238J
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
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
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
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
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
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