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of 4
pro vyhledávání: '"Matthias Erlacher"'
Autor:
Motahareh Solina Safari, Priska Woerl, Carolin Garmsiri, Dido Weber, Marcel Kwiatkowski, Madlen Hotze, Louisa Kuenkel, Luisa Lang, Matthias Erlacher, Ellen Gelpi, Johannes A. Hainfellner, Gottfried Baier, Gabriele Baier-Bitterlich, Stephanie zur Nedden
Publikováno v:
Molecular Metabolism, Vol 88, Iss , Pp 102018- (2024)
Objective: Glucose-1,6-bisphosphate (G-1,6-BP), a byproduct of glycolysis that is synthesized by phosphoglucomutase 2 like 1 (PGM2L1), is particularly abundant in neurons. G-1,6-BP is sensitive to the glycolytic flux, due to its dependence on 1,3-bis
Externí odkaz:
https://doaj.org/article/56bca8caec1144bc82e557e68d31c3f2
Publikováno v:
RNA Biology
Ribosomal decoding is an essential process in every living cell. During protein synthesis the 30S ribosomal subunit needs to accomplish binding and accurate decoding of mRNAs. From mutational studies and high-resolution crystal structures nucleotides
Autor:
Kamilla Bakowska-Zywicka, Matthias Erlacher, Norbert Polacek, Melanie Amort, Ronald Micura, Brigitte Wotzel
Publikováno v:
Nucleic Acids Research
Peptide bond formation and peptidyl-tRNA hydrolysis are the two elementary chemical reactions of protein synthesis catalyzed by the ribosomal peptidyl transferase ribozyme. Due to the combined effort of structural and biochemical studies, details of
Publikováno v:
Koch, Miriam; Clementi, Nina; Rusca, Nicola; Vögele, Paul; Erlacher, Matthias; Polacek, Norbert (2015). The integrity of the G2421-C2395 base pair in the ribosomal E-site is crucial for protein synthesis. RNA biology, 12(1), pp. 70-81. Taylor and Francis 10.1080/15476286.2015.1017218
RNA biology
RNA Biology
RNA biology
RNA Biology
During the elongation cycle of protein biosynthesis, tRNAs traverse through the ribosome by consecutive binding to the 3 ribosomal binding sites (A-, P-, and E- sites). While the ribosomal A- and P-sites have been functionally well characterized in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d50660c4eebe039f2f9b6f730d775286