Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Meh Sameen Nawaz"'
Autor:
Natalia Berges, Meh Sameen Nawaz, Tuva Børresdatter Dahl, Lars Hagen, Magnar Bjørås, Jon K Laerdahl, Ingrun Alseth
Publikováno v:
PLoS ONE, Vol 14, Iss 11, p e0225081 (2019)
Endonuclease V (ENDOV) is a ribonuclease with affinity for inosine which is the deamination product of adenosine. The genomes of most organisms, including human, encode ENDOV homologs, yet knowledge about in vivo functions and gene regulation is spar
Externí odkaz:
https://doaj.org/article/8d64d470004b4056b649ebbd5430c0d2
Autor:
Vigdis Bjerkli, Natalia Berges, Stig Ove Bøe, Jonas Øgaard, Meh Sameen Nawaz, Sverre Holm, Pål Aukrust, Erik Sebastian Vik, Xiang Yi Kong, Camilla Huse, Cathrine Fladeby, Magnar Bjørås, Ana Quiles-Jiménez, Tuva B. Dahl, Ingrun Alseth, Anna Lång, Rajikala Suganthan, Mona Skjelland, Azita Rashidi, Kuan Yang, Ellen Lund Sagen, Ida Gregersen, Azhar Abbas, Bente Halvorsen
Publikováno v:
Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease
Journal of the American Heart Association (JAHA)
Journal of the American Heart Association (JAHA)
Background In cardiovascular diseases, atherosclerotic disorder are the most frequent and important with respect to morbidity and mortality. Inflammation mediated by immune cells is central in all parts of the atherosclerotic progress, and further un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::deafa0f32957c9be5adcd18fbff87342
https://doi.org/10.1161/jaha.120.020656
https://doi.org/10.1161/jaha.120.020656
Autor:
Meh Sameen Nawaz, Jon K. Laerdahl, Tuva B. Dahl, Lars Hagen, Natalia Berges, Ingrun Alseth, Magnar Bjørås
Publikováno v:
PLoS ONE, Vol 14, Iss 11, p e0225081 (2019)
PLOS ONE
PLoS ONE
PLOS ONE
PLoS ONE
Endonuclease V (ENDOV) is a ribonuclease with affinity for inosine which is the deamination product of adenosine. The genomes of most organisms, including human, encode ENDOV homologs, yet knowledge about in vivo functions and gene regulation is spar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58860d4a54382528038fcfc11382143c
https://doaj.org/article/8d64d470004b4056b649ebbd5430c0d2
https://doaj.org/article/8d64d470004b4056b649ebbd5430c0d2
Autor:
Ingrun Alseth, Bjørn Dalhus, Pernille Blicher, Magnar Bjørås, Erik Sebastian Vik, Mia Elise Ronander, Anne Marthe Solvoll, Meh Sameen Nawaz
Publikováno v:
Scientific Reports
'Scientific Reports ', vol: 6, pages: 24979-1-24979-11 (2016)
'Scientific Reports ', vol: 6, pages: 24979-1-24979-11 (2016)
Endonuclease V (EndoV) is an enzyme with specificity for deaminated adenosine (inosine) in nucleic acids. EndoV from Escherichia coli (EcEndoV) acts both on inosines in DNA and RNA, whereas the human homolog cleaves only at inosines in RNA. Inosines
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d68b36b024d17d08bdc339d6584547a
Autor:
Magnar Bjørås, Bjørn Dalhus, Ingrun Alseth, Erik Sebastian Vik, Meh Sameen Nawaz, Cathrine Fladeby, Natalia Berges
Publikováno v:
The Journal of biological chemistry. 291(41)
Endonuclease V (EndoV) is an enzyme with specificity for inosines in nucleic acids. Whereas the bacterial homologs are active on both DNA and RNA, the mammalian variants only cleave RNA, at least when assayed with recombinant proteins. Here we show t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b137f978efcd57956d44923da9256da3
https://pubmed.ncbi.nlm.nih.gov/27573237
https://pubmed.ncbi.nlm.nih.gov/27573237
Autor:
Ingrun Alseth, Pernille Strøm Andersen, Magnar Bjørås, Bjørn Dalhus, Cathrine Fladeby, Meh Sameen Nawaz, Erik Sebastian Vik
Publikováno v:
Nature Communications
Endonuclease V orthologues are highly conserved proteins found in all kingdoms of life. While the prokaryotic enzymes are DNA repair proteins for removal of deaminated adenosine (inosine) from the genome, no clear role for the eukaryotic counterparts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e432f4a0451673c34dae8bf1eb7a36a7
https://pubmed.ncbi.nlm.nih.gov/23912683
https://pubmed.ncbi.nlm.nih.gov/23912683