Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Sofya Kuznetsova"'
Autor:
Olga A Zhuliabina, Sofya Kuznetsova, Dmitry S Tikhomirov, Anna E Filippova, Tatiana A Chebotareva, Olga S. Fedyanina, Olga I Demina, Alexander Filatov
Publikováno v:
The Journal of infectious diseases. 223(10)
Atypical mononuclear cells (AM) appear in significant numbers in peripheral blood of patients with Epstein-Barr virus (EBV)-associated infectious mononucleosis (IM). We investigated the number and lineage-specific clusters of differentiation (CD) exp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f18addd6e85921cc439e902f67f2780
https://pubmed.ncbi.nlm.nih.gov/32959062
https://pubmed.ncbi.nlm.nih.gov/32959062
Publikováno v:
Clinical Case Reports
Key Clinical Message The morphologic diagnosis of hairy cell leukemia coexisting with another lymphoproliferative disorder is hindered by the small size of hairy cell population. It can be simplified by presorting peripheral blood mononuclear cell us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::146234cc17e7caa063aee38b6a77f9a0
https://doi.org/10.1002/ccr3.1416
https://doi.org/10.1002/ccr3.1416
Autor:
Sofya Kuznetsova, Olga S. Fedyanina
Publikováno v:
Open Access Journal of Translational Medicine & Research. 2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa4d080ce5b510fc3b4c2666266cbf4e
https://doi.org/10.15406/oajtmr.2018.02.00045
https://doi.org/10.15406/oajtmr.2018.02.00045
Autor:
Amol V. Patil, Gerhild Zauner, Thijs J. Aartsma, Namik Akkilic, Hendrik A. Heering, Gerard W. Canters, Giulia Mizzon, Jante M. Salverda, Jason J. Davis, Sofya Kuznetsova
Publikováno v:
Angewandte Chemie (International ed. in English). 49(33)
(Figure Presented) Variations in the formal electrochemical potential (E 0) and electron-transfer rates (K 0) of the blue copper protein azurin have been directly observed. A new method, fluorescent cyclic voltammetry (FCV), was used to resolve the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bf453ad16ae2011944284d43d0ef863
https://pubmed.ncbi.nlm.nih.gov/20629001
https://pubmed.ncbi.nlm.nih.gov/20629001
Autor:
Hans Engelkamp, Nikos S. Hatzakis, Gerhild Zauner, Peter C. M. Christianen, Sofya Kuznetsova, Gerard W. Canters, Alan E. Rowan, Thijs J. Aartsma, Roeland J. M. Nolte
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 105(9), 3250-3255
Proceedings of the National Academy of Sciences USA, 105, 3250-3255
Proceedings of the National Academy of Sciences USA, 105, 9, pp. 3250-3255
Proceedings of the National Academy of Sciences USA, 105, 3250-3255
Proceedings of the National Academy of Sciences USA, 105, 9, pp. 3250-3255
A generic method is described for the fluorescence “readout” of the activity of single redox enzyme molecules based on Förster resonance energy transfer from a fluorescent label to the enzyme cofactor. The method is applied to the study of coppe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d1bd041d0989318f62914fd9fe88551
https://hdl.handle.net/1887/72397
https://hdl.handle.net/1887/72397
Autor:
Gerhild Zauner, Ralf Schmauder, Sofya Kuznetsova, Gerard W. Canters, Oleg A. Mayboroda, Thijs J. Aartsma, André M. Deelder
Publikováno v:
Analytical biochemistry. 350(1)
A method for fluorescence detection of a protein's redox state based on resonance energy transfer from an attached fluorescence label to the prosthetic group of the redox protein is described and tested for proteins containing three types of prosthet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f84fa9cee395c7e2d0ecfc0c4f2b033
https://pubmed.ncbi.nlm.nih.gov/16430854
https://pubmed.ncbi.nlm.nih.gov/16430854
Publikováno v:
Biochemistry. 43(33)
Plant nitrite reductase (NiR) catalyzes the reduction of nitrite (NO(2)(-)) to ammonia, using reduced ferredoxin as the electron donor. NiR contains a [4Fe-4S] cluster and an Fe-siroheme, which is the nitrite binding site. In the enzyme's as-isolated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ded3d38db6996c6fd713c273d973231
https://pubmed.ncbi.nlm.nih.gov/15311938
https://pubmed.ncbi.nlm.nih.gov/15311938