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Balnase, a New Dimer-Forming Ribonuclease from Bacillus altitudinis

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dc.contributor.author Dudkina E.
dc.contributor.author Ulyanova V.
dc.contributor.author Ilinskaya O.
dc.date.accessioned 2018-09-19T22:58:57Z
dc.date.available 2018-09-19T22:58:57Z
dc.date.issued 2017
dc.identifier.issn 2191-1630
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/145862
dc.description.abstract © 2016, Springer Science+Business Media New York.Current cancer treatments still remain ineffective and cause side effects which ruinously affect healthy cells. Among new promising anticancer drugs, special attention is paid to the ribonucleases (RNases) which possess selective cytotoxicity against malignant cells. It is found that besides enzymatic activity conformational state of RNase molecules plays a role in the anticancer activity. Balnase, a new RNase from Bacillus altitudinis, is a close homolog of Bacillus pumilus RNase (binase) which selectively kills malignant cells expressing oncogenes KIT, ras, AML1/ETO, and FLT3. Earlier, homogeneous sample of balnase was obtained. Here, we have characterized structural organization of balnase. It was shown that it is a natural dimer. The enzyme has the same conformational state as binase but balnase dimers are less stable.
dc.relation.ispartofseries BioNanoScience
dc.subject Anticancer activity
dc.subject Balnase
dc.subject Binase
dc.subject Conformational state
dc.subject Dimerization
dc.subject Structural organization
dc.title Balnase, a New Dimer-Forming Ribonuclease from Bacillus altitudinis
dc.type Article
dc.relation.ispartofseries-issue 1
dc.relation.ispartofseries-volume 7
dc.collection Публикации сотрудников КФУ
dc.relation.startpage 127
dc.source.id SCOPUS21911630-2017-7-1-SID85017663758


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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