Výsledky vyhledávání - "O. V. Mitkevich"

Selection of DNA aptamers specifically interacting with the fibrillar form of the yeast Sup35 protein

Autor: O. V. Mitkevich, M. D. Ter-Avanesyan, V. V. Kushnirov, E. R. Surina, A. A. Antipin, S. V. Benevolensky, A. N. Marchenko, E. V. Morozkina

Publikováno v: Molecular Biology. 43:626-631

Single-stranded DNA aptamers interacting with fibrils of Saccharomyces cerevisiae Sup35p were obtained by the SELEX procedure. The specificity of interactions with Sup35p was investigated for 10 out of 40 selected aptamers. Nine aptamers were found t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d837e8b69f0a6c1ace5fe8e7579c21b5
https://doi.org/10.1134/s0026893309040153

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Monoclonal antibody directed to a fibrinogen A?? #529???539 epitope inhibits ??-chain crosslinking by transglutaminases

Autor: J H Sobel, G. P. Samokhin, G.F. Kalantarov, T. N. Vlasik, O. V. Mitkevich, J R Shainoff, I. N. Trakht, Z A Streltsova

Publikováno v: Blood Coagulation & Fibrinolysis. 7:85-92

A monoclonal antibody (5A2) recognizing a segment near the C-terminus of the fibrin(ogen) A alpha-chain (A alpha #529-539) was found to inhibit alpha-chain crosslinking catalyzed by coagulation factor XIIIa and by tissue-transglutaminase. The rapid g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26162c9783695e039d3620a07ffbf7db
https://doi.org/10.1097/00001721-199601000-00011

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Visualization of apo B, fibrinogen/fibrin, and fibronectin in the intima of normal human aorta and large arteries and during atherosclerosis

Autor: G.F. Kalantarov, O. V. Mitkevich, Mazurov Av, Eduard Tararak, G. P. Samokhin, T. N. Vlasik, Boris V. Shekhonin, Victor E. Koteliansky, D. V. Vinogradov

Publikováno v: Atherosclerosis. 82:213-226

Apolipoprotein B (apo B), fibrinogen/fibrin, blood platelets, factor VIII-related antigen of the blood coagulation system, and smooth muscle cells (SMC) were identified in the intima of normal and atherosclerotic human aorta and large arteries by the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::735bf57843b388d39ca1dd06e6a2d33e
https://doi.org/10.1016/0021-9150(90)90043-i

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Coagulation factor XIIIa undergoes a conformational change evoked by glutamine substrate. Studies on kinetics of inhibition and binding of XIIIA by a cross-reacting antifibrinogen antibody

Autor: O V, Mitkevich, J R, Shainoff, P M, DiBello, V C, Yee, D C, Teller, G B, Smejkal, P D, Bishop, I S, Kolotushkina, K, Fickenscher, G P, Samokhin

Publikováno v: The Journal of biological chemistry. 273(23)

Coagulation factor XIIIa, plasma transglutaminase (endo-gamma-glutamine:epsilon-lysine transferase EC 2.3.2.13) catalyzes isopeptide bond formation between glutamine and lysine residues and rapidly cross-links fibrin clots. A monoclonal antibody (5A2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a00117cae504dadc542da963f58d87d5
https://pubmed.ncbi.nlm.nih.gov/9603949

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