Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Simon Bohleber"'
Autor:
Carolin Lisa Michaela Ludwig, Simon Bohleber, Rebecca Lapp, Alexander Rebl, Eva Katrin Wirth, Martina Langhammer, Ulrich Schweizer, Joachim M. Weitzel, Marten Michaelis
Publikováno v:
Journal of Ovarian Research, Vol 16, Iss 1, Pp 1-16 (2023)
Abstract The development and maturation of ovarian follicles is a complex and highly regulated process, which is essential for successful ovulation. During recent decades, several mouse models provided insights into the regulation of folliculogenesis
Externí odkaz:
https://doaj.org/article/0c473caab59c408e9f2bc99bc4e46ba8
Autor:
Noelia Fradejas-Villar, Wenchao Zhao, Uschi Reuter, Michael Doengi, Irina Ingold, Simon Bohleber, Marcus Conrad, Ulrich Schweizer
Publikováno v:
Redox Biology, Vol 48, Iss , Pp 102188- (2021)
Selenoproteins are a small family of proteins containing the trace element selenium in form of the rare amino acid selenocysteine (Sec), which is decoded by the UGA codon. In humans, a number of pathogenic variants in genes encoding distinct selenopr
Externí odkaz:
https://doaj.org/article/f6302178548c423e8a2aad1b6790908b
Publikováno v:
Biomolecules, Vol 12, Iss 10, p 1504 (2022)
Co-translational incorporation of selenocysteine (Sec) into selenoproteins occurs at UGA codons in a process in which translational elongation competes with translational termination. Selenocysteine insertion sequence-binding protein 2 (SECISBP2) gre
Externí odkaz:
https://doaj.org/article/4504362c517646c2b171a7b89b608e6c
Publikováno v:
Frontiers in Neuroscience, Vol 15 (2021)
Eighteen years ago, unexpected epileptic seizures in Selenop-knockout mice pointed to a potentially novel, possibly underestimated, and previously difficult to study role of selenium (Se) in the mammalian brain. This mouse model was the key to open t
Externí odkaz:
https://doaj.org/article/aa812168596d4f91b318c6c333a56aa7
Publikováno v:
Thyroid. 32:860-870
Autor:
Simon Bohleber, Ulrich Schweizer, Irina Ingold, Michael Doengi, Wenchao Zhao, Uschi Reuter, Noelia Fradejas-Villar, Marcus Conrad
Publikováno v:
Redox Biology
Redox Biol. 48:102188 (2021)
Redox Biology, Vol 48, Iss, Pp 102188-(2021)
Redox Biol. 48:102188 (2021)
Redox Biology, Vol 48, Iss, Pp 102188-(2021)
Selenoproteins are a small family of proteins containing the trace element selenium in form of the rare amino acid selenocysteine (Sec), which is decoded by the UGA codon. In humans, a number of pathogenic variants in genes encoding distinct selenopr
Autor:
Tsutomu Suzuki, Uschi Reuter, Noelia Fradejas-Villar, Wenchao Zhao, Kenjyo Miyauchi, Rainer Knoll, Robert McFarland, Mark Helm, Simon Bohleber, Robert W. Taylor, Yuriko Sakaguchi, Annika Kotter, Ulrich Schweizer, Yufeng Mo
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 21
International Journal of Molecular Sciences, Vol 22, Iss 11454, p 11454 (2021)
Volume 22
Issue 21
International Journal of Molecular Sciences, Vol 22, Iss 11454, p 11454 (2021)
Transfer RNA[Ser]Sec carries multiple post-transcriptional modifications. The A37G mutation in tRNA[Ser]Sec abrogates isopentenylation of base 37 and has a profound effect on selenoprotein expression in mice. Patients with a homozygous pathogenic p.R
Autor:
Uschi Reuter, Doreen Braun, Ulrich Schweizer, Michael T. Howard, Simon Bohleber, Sandra Seeher, Wenchao Zhao, S. Arndt, Hagen Wende, Carmen Birchmeier, Henrik Schmidt, Noelia Fradejas-Villar
Publikováno v:
Journal of Biological Chemistry. 294:14185-14200
Recoding of UGA codons as selenocysteine (Sec) codons in selenoproteins depends on a selenocysteine insertion sequence (SECIS) in the 3′-UTR of mRNAs of eukaryotic selenoproteins. SECIS-binding protein 2 (SECISBP2) increases the efficiency of this
Publikováno v:
The FASEB Journal. 35
Publikováno v:
RNA Biology
Base 37 in tRNA, 3′-adjacent to the anticodon, is occupied by a purine base that is thought to stabilize codon recognition by stacking interactions on the first Watson-Crick base pair. If the first codon position forms an A.U or U.A base pair, the