Форма представления | Статьи в зарубежных журналах и сборниках |
Год публикации | 2016 |
Язык | английский |
|
Девятияров Руслан Мансурович, автор
Кикавада Тахакиро , автор
Несмелов Александр Александрович, автор
Черкасов Александр Вадимович, автор
Шагимарданова Елена Ильясовна, автор
|
|
Cornette Richard Marcelle, автор
|
Библиографическое описание на языке оригинала |
New Antioxidant Genes from an Anhydrobiotic Insect: Unique Structural Features in Functional Motifs of Thioredoxins. A.A. Nesmelov, R.M. Devatiyarov, T.A. Voronina, S.A. Kondratyeva, A. V. Cherkasov, R. Cornette, et al., Bionanoscience. (2016) 6: 568. doi:10.1007/s12668-016-0278-x |
Аннотация |
P. vanderplanki is the most complex known organism able to survive body desiccation via entering a state of suspended metabolism called anhydrobiosis. This unique ability is based on the specific molecular machinery involving a synthesis of non-reducing sugar trehalose and a variety of protective proteins. Genes encoding these protective proteins are extensively duplicated in P. vanderplanki genome and become hugely upregulated in response to desiccation. Some of these highly expressed genes encode substitutions of amino acids crucial for the function of corresponding proteins. An intriguing group of protective proteins in P. vanderplanki are thioredoxins. These antioxidant proteins are important for P. vanderplanki anhydrobiosis since desiccation is tightly related to the elevated production of free radicals and oxidative damage. TRX set is unprecedentedly expanded in P. vanderplanki genome up to 25 TRX genes. Genomes of congeneric midge P. nubifer, Apis mellifera, Drosophila melano |
Ключевые слова |
Anhydrobiosis, P. vanderplanki, Thioredoxins, Amino acid substitution, CxxC motif |
Название журнала |
BioNanoScience
|
URL |
http://link.springer.com/10.1007/s12668-016-0278-x |
Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=139047 |
Полная запись метаданных |
Поле DC |
Значение |
Язык |
dc.contributor.author |
Девятияров Руслан Мансурович |
ru_RU |
dc.contributor.author |
Кикавада Тахакиро |
ru_RU |
dc.contributor.author |
Несмелов Александр Александрович |
ru_RU |
dc.contributor.author |
Черкасов Александр Вадимович |
ru_RU |
dc.contributor.author |
Шагимарданова Елена Ильясовна |
ru_RU |
dc.contributor.author |
Cornette Richard Marcelle |
ru_RU |
dc.date.accessioned |
2016-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2016-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2016 |
ru_RU |
dc.identifier.citation |
New Antioxidant Genes from an Anhydrobiotic Insect: Unique Structural Features in Functional Motifs of Thioredoxins. A.A. Nesmelov, R.M. Devatiyarov, T.A. Voronina, S.A. Kondratyeva, A. V. Cherkasov, R. Cornette, et al., Bionanoscience. (2016) 6: 568. doi:10.1007/s12668-016-0278-x |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/?p_id=139047 |
ru_RU |
dc.description.abstract |
BioNanoScience |
ru_RU |
dc.description.abstract |
P. vanderplanki is the most complex known organism able to survive body desiccation via entering a state of suspended metabolism called anhydrobiosis. This unique ability is based on the specific molecular machinery involving a synthesis of non-reducing sugar trehalose and a variety of protective proteins. Genes encoding these protective proteins are extensively duplicated in P. vanderplanki genome and become hugely upregulated in response to desiccation. Some of these highly expressed genes encode substitutions of amino acids crucial for the function of corresponding proteins. An intriguing group of protective proteins in P. vanderplanki are thioredoxins. These antioxidant proteins are important for P. vanderplanki anhydrobiosis since desiccation is tightly related to the elevated production of free radicals and oxidative damage. TRX set is unprecedentedly expanded in P. vanderplanki genome up to 25 TRX genes. Genomes of congeneric midge P. nubifer, Apis mellifera, Drosophila melano |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
Anhydrobiosis |
ru_RU |
dc.subject |
P. vanderplanki |
ru_RU |
dc.subject |
Thioredoxins |
ru_RU |
dc.subject |
Amino acid substitution |
ru_RU |
dc.subject |
CxxC motif |
ru_RU |
dc.title |
A.A. Nesmelov, R.M. Devatiyarov, T.A. Voronina, S.A. Kondratyeva, A. V. Cherkasov, R. Cornette, et al., Bionanoscience. (2016) 6: 568. doi:10.1007/s12668-016-0278-x. |
ru_RU |
dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|