Zobrazeno 1 - 10
of 38
pro vyhledávání: '"Alexei Korennykh"'
Autor:
Michael A. Estrella, Jin Du, Li Chen, Sneha Rath, Eliza Prangley, Alisha Chitrakar, Tsutomu Aoki, Paul Schedl, Joshua Rabinowitz, Alexei Korennykh
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Nocturnin is a rhythmically expressed protein that regulates metabolism under the control of circadian clock proposed to function through the deadenylation of metabolic enzyme mRNAs. Here the authors show that Nocturnin and its fly homolog Curled cat
Externí odkaz:
https://doaj.org/article/91822378ee9c4553912dbca3ceb0472b
Autor:
Samantha R Oakes, David Gallego-Ortega, Prudence M Stanford, Simon Junankar, Wendy Wing Yee Au, Zoya Kikhtyak, Anita von Korff, Claudio M Sergio, Andrew M K Law, Lesley E Castillo, Stephanie L Allerdice, Adelaide I J Young, Catherine Piggin, Belinda Whittle, Edward Bertram, Matthew J Naylor, Daniel L Roden, Jesse Donovan, Alexei Korennykh, Christopher C Goodnow, Moira K O'Bryan, Christopher J Ormandy
Publikováno v:
PLoS Genetics, Vol 13, Iss 11, p e1007072 (2017)
We identified a non-synonymous mutation in Oas2 (I405N), a sensor of viral double-stranded RNA, from an ENU-mutagenesis screen designed to discover new genes involved in mammary development. The mutation caused post-partum failure of lactation in hea
Externí odkaz:
https://doaj.org/article/76d21e2f20924475a4c47cb697a95a92
Autor:
Yize Li, Shuvojit Banerjee, Stephen A Goldstein, Beihua Dong, Christina Gaughan, Sneha Rath, Jesse Donovan, Alexei Korennykh, Robert H Silverman, Susan R Weiss
Publikováno v:
eLife, Vol 6 (2017)
ADAR1 isoforms are adenosine deaminases that edit and destabilize double-stranded RNA reducing its immunostimulatory activities. Mutation of ADAR1 leads to a severe neurodevelopmental and inflammatory disease of children, Aicardi-Goutiéres syndrome.
Externí odkaz:
https://doaj.org/article/10892b8d0012417b8d9719dca9a847cd
Publikováno v:
Cell Reports, Vol 2, Iss 4, Pp 902-913 (2012)
2′,5′-linked oligoadenylates (2-5As) serve as conserved messengers of pathogen presence in the mammalian innate immune system. 2-5As induce self-association and activation of RNase L, which cleaves cytosolic RNA and promotes the production of int
Externí odkaz:
https://doaj.org/article/61d4314c8aa645cda2f77d21e8636b02
Autor:
Liping Zhao, Alexei Korennykh, Guojun Wu, Abhishek Biswas, Mohamed S. Donia, Michael A. Estrella, Philip D. Jeffrey, Jared N. Balaich
Publikováno v:
Nature
The human microbiome encodes a large repertoire of biochemical enzymes and pathways, most of which remain uncharacterized. Here, using a metagenomics-based search strategy, we discovered that bacterial members of the human gut and oral microbiome enc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20cfa8468d8ea049932f3b488cd3e871
https://doi.org/10.1038/s41586-021-04091-0
https://doi.org/10.1038/s41586-021-04091-0
Publikováno v:
Proceedings of the National Academy of Sciences. 119
All kingdoms of life produce essential nicotinamide dinucleotide NADP(H) using NAD kinases (NADKs). A panel of published NADK structures from bacteria, eukaryotic cytosol, and yeast mitochondria revealed similar tetrameric enzymes. Here, we present t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f236b718d3ee6de34827c91d42e90efd
https://doi.org/10.1073/pnas.2200923119
https://doi.org/10.1073/pnas.2200923119
Autor:
Susan R. Weiss, Sneha Rath, Sergei V. Kotenko, Kaitlin Demarest, Ned S. Wingreen, Alisha Chitrakar, Alexei Korennykh, Jesse Donovan, Raghavendra Rao Sridhar, Yize Li
Publikováno v:
Proceedings of the National Academy of Sciences
Cells of all mammals recognize double-stranded RNA (dsRNA) as a foreign material. In response, they release interferons (IFNs) and activate a ubiquitously expressed pseudokinase/endoribonuclease RNase L. RNase L executes regulated RNA decay and halts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f342e8cf6dcb39b252b32364fcb36d9e
https://doi.org/10.1073/pnas.1818363116
https://doi.org/10.1073/pnas.1818363116