Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Laura Lancaster"'
Autor:
Tingting Liu, Ariel Kaplan, Lisa Alexander, Shannon Yan, Jin-Der Wen, Laura Lancaster, Charles E Wickersham, Kurt Fredrick, Harry Noller, Ignacio Tinoco Jr, Carlos J Bustamante
Publikováno v:
eLife, Vol 3 (2014)
Externí odkaz:
https://doaj.org/article/adf074da84554f9ab05adbcf7c89d94d
Autor:
Tingting Liu, Ariel Kaplan, Lisa Alexander, Shannon Yan, Jin-Der Wen, Laura Lancaster, Charles E Wickersham, Kurt Fredrick, Harry Noller, Ignacio Tinoco Jr, Carlos J Bustamante
Publikováno v:
eLife, Vol 3 (2014)
A detailed understanding of tRNA/mRNA translocation requires measurement of the forces generated by the ribosome during this movement. Such measurements have so far remained elusive and, thus, little is known about the relation between force and tran
Externí odkaz:
https://doaj.org/article/98075f63f1b8440fa55f66a2bef94493
Publikováno v:
Quality Engineering. 34:507-521
Publikováno v:
Proc Natl Acad Sci U S A
Viomycin, an antibiotic that has been used to fight tuberculosis infections, is believed to block the translocation step of protein synthesis by inhibiting ribosomal subunit dissociation and trapping the ribosome in an intermediate state of intersubu
Publikováno v:
in education. 25:3-22
The world, influenced by 21st century technologies and ecological challenges, has rapidly changed with more ability to “connect” locally and globally and more opportunities to learn from a range of sources. As a result, our learners and their nee
Autor:
Jie Zhou, Jake Cozy, Charlotte A. Nelson, Harry F. Noller, Gillian Rexroad, Calvin S. Leung, Laura Lancaster, Dustin Niblett
Publikováno v:
RNA
A recent crystal structure of a ribosome complex undergoing partial translocation in the absence of elongation factor EF-G showed disruption of codon–anticodon pairing and slippage of the reading frame by −1, directly implicating EF-G in preserva
Publikováno v:
Nature Structural & Molecular Biology. 24:1021-1027
During protein synthesis, the mRNA and tRNAs must be moved rapidly through the ribosome while precisely maintaining the translational reading frame. This complex dynamic process is coupled to large- and small-scale conformational rearrangements in th
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 16
The elongation factor G (EF-G)–catalyzed translocation of mRNA and tRNA through the ribosome is essential for vacating the ribosomal A site for the next incoming aminoacyl-tRNA, while precisely maintaining the translational reading frame. Here, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56d7db3de933fbb69a95abe72c1d381e
https://europepmc.org/articles/PMC6475402/
https://europepmc.org/articles/PMC6475402/
Publikováno v:
Quarterly Reviews of Biophysics. 50
Ribosomes are remarkable ribonucleoprotein complexes that are responsible for protein synthesis in all forms of life. They polymerize polypeptide chains programmed by nucleotide sequences in messenger RNA in a mechanism mediated by transfer RNA. One
Autor:
Harry F. Noller, Filipp Frank, Carlos Bustamante, Maurizio Righini, Laura Lancaster, Varsha P. Desai, Ignacio Tinoco, Antony Lee
Publikováno v:
Molecular Cell. 75:1007-1019.e5
The movement of ribosomes on mRNA is often interrupted by secondary structures that present mechanical barriers and play a central role in translation regulation. We investigate how ribosomes couple their internal conformational changes with the acti