Публикации - Белки

Зависимость подвижности белков модельных растворов сыворотки крови от рН среды и относительной концентрации компонентов
Ирина Михайловна Папок
Международный молодежный научный форум «ЛОМОНОСОВ-2012», 2012
https://lomonosov-msu.ru/archive/Lomonosov_2012/structure_26_1871_doc_name.htm


Post-translational Membrane Insertion of Tail-anchored Transmembrane EF-hand Ca2+ Sensor Calneurons Requires the TRC40/Asna1 Protein Chaperone
Johannes Hradsky, Vijeta Raghuram, Parameshwar Pasham Reddy, Gemma Navarro, Mike Hupe, Vicent Casado, Peter J. McCormick, Yogendra Sharma, Michael R. Kreutz, Marina Mikhaylova
Journal of Biological Chemistry, 2011, ISSN: 0021-9258, 1083-351X, Том: 286, Выпуск: 42, Стр.: 36762-36776, DOI: 10.1074/jbc.M111.280339
http://www.jbc.org/content/286/42/36762


A Protein Aggregation Based Test for Screening of the Agents Affecting Thermostability of Proteins
Tatyana Eronina, Vera Borzova, Olga Maloletkina, Sergey Kleymenov, Regina Asryants, Kira Markossian, Boris Kurganov
PLOS ONE, 2011, ISSN: 1932-6203, Том: 6, Выпуск: 7, Стр.: e22154, DOI: 10.1371/journal.pone.0022154
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0022154


Formation of dipole nanoclusters in blood serum protein solutions containing europium and potassium ions
T. N. Tikhonova, G. P. Petrova, Yu M. Petrusevich, K. V. Fedorova, V. V. Kashin
Moscow University Physics Bulletin, 2011, ISSN: 0027-1349, 1934-8460, Том: 66, Выпуск: 2, Стр.: 190-195, DOI: 10.3103/S0027134911020172
http://link.springer.com/article/10.3103/S0027134911020172


Effect of secreted Rpf protein on intracellular contacts in Micrococcus luteus and Mycobacterium smegmatis cultures
V. D. Nikitushkin, G. R. Demina, A. S. Kaprelyants
Microbiology, 2011, ISSN: 0026-2617, 1608-3237, Том: 80, Выпуск: 2, Стр.: 143-149, DOI: 10.1134/S0026261711020123
http://link.springer.com/article/10.1134/S0026261711020123


Refolding of urea-induced denaturation of model proteins by trimethylamine N-oxide
Pankaj Attri, Pannuru Venkatesu
Thermochimica Acta, 2011, ISSN: 0040-6031, Том: 526, Выпуск: 1–2, Стр.: 143-150, DOI: 10.1016/j.tca.2011.09.006
http://www.sciencedirect.com/science/article/pii/S0040603111004667


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, 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