M
Maria Selmer
Researcher at Uppsala University
Publications - 49
Citations - 3230
Maria Selmer is an academic researcher from Uppsala University. The author has contributed to research in topics: Translation (biology) & Transfer RNA. The author has an hindex of 18, co-authored 44 publications receiving 3017 citations. Previous affiliations of Maria Selmer include Laboratory of Molecular Biology & Lund University.
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Journal ArticleDOI
Structure of the 70S Ribosome Complexed with mRNA and tRNA
Maria Selmer,Christine M. Dunham,Frank V. Murphy,Albert Weixlbaumer,Sabine Petry,Ann C. Kelley,John R. Weir,Venki Ramakrishnan +7 more
TL;DR: The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (t RNA) and metal ions also stabilize the intersubunit interface.
Journal ArticleDOI
The structure of the ribosome with elongation factor G trapped in the posttranslocational state.
Yong-Gui Gao,Maria Selmer,Christine M. Dunham,Albert Weixlbaumer,Ann C. Kelley,Venki Ramakrishnan +5 more
TL;DR: A crystal structure refined to 3.6 angstrom resolution of the ribosome trapped with EF-G in the posttranslocational state using the antibiotic fusidic acid is reported, providing insights into translocation and decoding.
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Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon.
Sabine Petry,Ditlev E. Brodersen,Frank V. Murphy,Christine M. Dunham,Maria Selmer,Michael J. Tarry,Ann C. Kelley,Venki Ramakrishnan +7 more
TL;DR: In this article, the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at the same time, were presented.
Journal ArticleDOI
Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic.
TL;DR: The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex.
Journal ArticleDOI
Post-termination complex disassembly by ribosome recycling factor, a functional tRNA mimic.
Go Hirokawa,Go Hirokawa,Michael C. Kiel,Aiko Muto,Maria Selmer,V. Samuel Raj,V. Samuel Raj,Anders Liljas,Kazuei Igarashi,Hideko Kaji,Akira Kaji +10 more
TL;DR: The data are consistent with the notion that RRF binds to the A‐site and is translocated to the P‐site, releasing deacylated tRNA from the P- and E‐sites, and the release of mRNA, is accompanied by therelease of RRF and EF‐G from the ribosome.