Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Tõnu Reintamm"'
Autor:
Margit Mutso, Andrei Nikonov, Arno Pihlak, Eva Žusinaite, Liane Viru, Anastasia Selyutina, Tõnu Reintamm, Merike Kelve, Mart Saarma, Mati Karelson, Andres Merits
Publikováno v:
PLoS ONE, Vol 10, Iss 6, p e0128686 (2015)
The inhibitory potency of an antisense oligonucleotide depends critically on its design and the accessibility of its target site. Here, we used an RNA interference-guided approach to select antisense oligonucleotide target sites in the coding region
Externí odkaz:
https://doaj.org/article/7277237ed6764f10b0ca77bf0770ac43
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e66601 (2013)
Multicopy genes, like ribosomal RNA genes (rDNA), are widely used to describe and distinguish individuals. Despite concerted evolution that homogenizes a large number of rDNA gene copies, the presence of different gene variants within a genome has be
Externí odkaz:
https://doaj.org/article/749ee2b92f2643439fe924182bc47134
Publikováno v:
Biochimie. 146:113-118
Deoxynucleoside 5-monophosphate N-glycosidase or DNPH1 (former name Rcl) is a nucleotide hydrolase whose expression in mammalian cancer tissues has been associated with its tumorigenic potential. Therefore, the enzyme has been studied principally in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28dcc8516d9e2c1bf400c3d10e948aa6
https://doi.org/10.1016/j.biochi.2017.12.005
https://doi.org/10.1016/j.biochi.2017.12.005
Autor:
Kerli Vallmann, Nele Aas-Valleriani, Tõnu Reintamm, Annika Lopp, Mailis Päri, Kaidi Kolk, Merike Kelve
Publikováno v:
Biochimie. 158
Previously we had discovered unusual enzymatic activity in the marine sponge Axinella polypoides, ATP N-glycosidase (Reintamm et al., 2003). We show here that the Ephydatia muelleri mRNA encoding protein with PNP_UDP_1 (phosphorylase superfamily) sig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f314dfc8facf1b1c885d30faa8e4e88
https://pubmed.ncbi.nlm.nih.gov/30597179
https://pubmed.ncbi.nlm.nih.gov/30597179
Publikováno v:
Biochimie. 156
Several genes of IFN-mediated pathways in vertebrates, among them the genes that participate in the 2ʹ,5ʹ-oligoadenylate synthetase (OAS)/RNase L pathway, have been identified in C. gigas. In the present study, we identified genes, which encode pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::362cc71bc985497f74a4afdeb75fb809
https://pubmed.ncbi.nlm.nih.gov/30195052
https://pubmed.ncbi.nlm.nih.gov/30195052
Publikováno v:
Gene. 683
Deoxynucleoside 5-monophosphate N-glycosidase, DNPH1 is a member of the nucleoside 2-deoxyribosyltransferase (NDT) family. This enzyme catalyzes the hydrolysis of deoxynucleoside monophosphates into free nucleobase moieties and 2-deoxyribose 5-phosph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5edad7e7999b3737def124b181ede35f
https://pubmed.ncbi.nlm.nih.gov/30296565
https://pubmed.ncbi.nlm.nih.gov/30296565
Publikováno v:
Biochimie. 94:1635-1646
In the marine sponge Tethya aurantium a novel endoribonuclease was found which specifically catalyzed the degradation of 2′,5′-phosphodiester linkages and was therefore named endo-2′,5′-ribonuclease. This enzymatic reaction yielded 2′,3′-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a36b04a2f2088a40c2df6bd70fba4139
https://doi.org/10.1016/j.biochi.2012.04.002
https://doi.org/10.1016/j.biochi.2012.04.002
Publikováno v:
Gene. 478:42-49
The 2′,5′-oligoadenylate synthetases (2–5A synthetases, OAS) form a family of proteins presented in many branches of Metazoa. The phylum Porifera (sponges) contains OAS proteins which are different from those in vertebrates and form a distinct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2b7b863306fccf2fdeed3da2f285257
https://doi.org/10.1016/j.gene.2011.01.014
https://doi.org/10.1016/j.gene.2011.01.014
Publikováno v:
Marine Drugs
Volume 8
Issue 2
Pages 235-254
Marine Drugs, Vol 8, Iss 2, Pp 235-254 (2010)
Volume 8
Issue 2
Pages 235-254
Marine Drugs, Vol 8, Iss 2, Pp 235-254 (2010)
2',5'-oligoadenylate synthetases (OAS) as a component of mammalian interferon-induced antiviral enzymatic system catalyze the oligomerization of cellular ATP into 2',5'-linked oligoadenylates (2-5A). Though vertebrate OASs have been characterized as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3ec35bae60b32dfdae9004b461ca8a6
https://doi.org/10.3390/md8020235
https://doi.org/10.3390/md8020235
Publikováno v:
FEBS Journal. 274:3462-3474
2',5'-oligoadenylate (2-5A) synthetases are known as components of the interferon-induced cellular defence mechanism in mammals. The existence of 2-5A synthetases in the evolutionarily lowest multicellular animals, the marine sponges, has been demons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85f5931410e3e82bdd50207aec45dd92
https://doi.org/10.1111/j.1742-4658.2007.05878.x
https://doi.org/10.1111/j.1742-4658.2007.05878.x