The Menin Inhibitor Ziftomenib (KO-539) Synergizes with Agents Targeting Chromatin Regulation or Apoptosis and Sensitizes AML with MLL Rearrangement or NPM1 Mutation to Venetoclax

Autor: Johanna Rausch, Margarita M. Dzama, Nadezda Dolgikh, Hanna Stiller, Stephan Bohl, Catharina Lahrmann, Kerstin Kunz, Linda Kessler, Hakim Echchannaoui, Chun-Wei David Chen, Thomas Kindler, Francis Burrows, Matthias Theobald, Daniel Sasca, Scott A. Armstrong, Michael Kuehn

Publikováno v: Blood. 140:6226-6227

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8a8a7406f54435e5d684652b2b9502f0
https://doi.org/10.1182/blood-2022-167566

Distinct populations of embryonic epithelial progenitors generate Lgr5+ intestinal stem cells

Autor: Margarita M. Dzama, Lira Nigmatullina, Sergi Sayols, Nastasja Kreim, Natalia Soshnikova

Publikováno v: Developmental Biology. 432:258-264

The adult intestinal stem cells (ISCs) are transcriptionally heterogeneous. As the mechanisms governing their developmental specification are still poorly understood, whether this heterogeneity reflects an early determination of distinct cellular sub

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::53a0ed9a60a4d2f04efd14e75d765c64
https://doi.org/10.1016/j.ydbio.2017.10.012

A bacterial homolog YciH of eukaryotic translation initiation factor eIF1 regulates stress-related gene expression and is unlikely to be involved in translation initiation fidelity

Autor: Olga Pobeguts, P. I. Pletnev, Olga A. Dontsova, S. A. Evfratov, Petr V. Sergiev, Ilya A. Osterman, Sergey I. Kovalchuk, Ivan Butenko, Vadim M. Govorun, Margarita M. Dzama, Anna Y. Golovina, Alexey A. Bogdanov

Publikováno v: RNA Biology. 12:966-971

YciH is a bacterial protein, homologous to eukaryotic translation initiation factor eIF1. Preceding evidence obtained with the aid of in vitro translation initiation system suggested that it may play a role of a translation initiation factor, ensurin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c9391ac93f2ae5d0d5462bb17094c95
https://doi.org/10.1080/15476286.2015.1069464

The last rRNA methyltransferase of E. coli revealed: The yhiR gene encodes adenine-N6 methyltransferase specific for modification of A2030 of 23S ribosomal RNA

Autor: Ilya A. Osterman, Olga A. Dontsova, Marina V. Serebryakova, Anna Y. Golovina, Margarita M. Dzama, Alexey A. Bogdanov, Petr V. Sergiev

Publikováno v: RNA. 18:1725-1734

The ribosomal RNA (rRNA) of Escherichia coli contains 24 methylated residues. A set of 22 methyltransferases responsible for modification of 23 residues has been described previously. Herein we report the identification of the yhiR gene as encoding t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34c79c461003a120e18c7701fa145c0d
https://doi.org/10.1261/rna.034207.112

Comprehensive Functional Analysis of Escherichia coli Ribosomal RNA Methyltransferases.

Autor: Pletnev P; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.; Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia., Guseva E; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Zanina A; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia., Evfratov S; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia., Dzama M; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Treshin V; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia., Pogorel'skaya A; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Osterman I; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.; Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia., Golovina A; Belozersky Institute of Physico-Chemical Biololgy, Lomonosov Moscow State University, Moscow, Russia., Rubtsova M; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.; Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia., Serebryakova M; Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.; Belozersky Institute of Physico-Chemical Biololgy, Lomonosov Moscow State University, Moscow, Russia., Pobeguts OV; Federal Research and Clinical Centre of Physical-Chemical Medicine, Moscow, Russia., Govorun VM; Federal Research and Clinical Centre of Physical-Chemical Medicine, Moscow, Russia., Bogdanov AA; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.; Belozersky Institute of Physico-Chemical Biololgy, Lomonosov Moscow State University, Moscow, Russia., Dontsova OA; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.; Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia.; Belozersky Institute of Physico-Chemical Biololgy, Lomonosov Moscow State University, Moscow, Russia., Sergiev PV; Department of Chemistry, Lomonosov Moscow State University, Moscow, Russia.; Center of Life Sciences, Skolkovo Institute of Science and Technology, Moscow, Russia.; Belozersky Institute of Physico-Chemical Biololgy, Lomonosov Moscow State University, Moscow, Russia.; Institute of Functional Genomics, Lomonosov Moscow State University, Moscow, Russia.

Publikováno v: Frontiers in genetics [Front Genet] 2020 Feb 27; Vol. 11, pp. 97. Date of Electronic Publication: 2020 Feb 27 (Print Publication: 2020).