Form of presentation | Articles in international journals and collections |
Year of publication | 2016 |
Язык | английский |
|
Devyatiyarov Ruslan Mansurovich, author
Kikavada Takhakiro , author
Nesmelov Aleksandr Aleksandrovich, author
Cherkasov Aleksandr Vadimovich, author
Shagimardanova Elena Ilyasovna, author
|
|
Cornette Richard Marcelle, author
|
Bibliographic description in the original language |
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 |
Annotation |
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 |
Keywords |
Anhydrobiosis, P. vanderplanki, Thioredoxins, Amino acid substitution, CxxC motif |
The name of the journal |
BioNanoScience
|
URL |
http://link.springer.com/10.1007/s12668-016-0278-x |
Please use this ID to quote from or refer to the card |
https://repository.kpfu.ru/eng/?p_id=139047&p_lang=2 |
Full metadata record |
Field DC |
Value |
Language |
dc.contributor.author |
Devyatiyarov Ruslan Mansurovich |
ru_RU |
dc.contributor.author |
Kikavada Takhakiro |
ru_RU |
dc.contributor.author |
Nesmelov Aleksandr Aleksandrovich |
ru_RU |
dc.contributor.author |
Cherkasov Aleksandr Vadimovich |
ru_RU |
dc.contributor.author |
Shagimardanova Elena Ilyasovna |
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/eng/?p_id=139047&p_lang=2 |
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 |
Articles in international journals and collections |
ru_RU |
|