Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Marija Liutkute"'
Publikováno v:
Frontiers in Microbiology, Vol 11 (2021)
Protein homeostasis of bacterial cells is maintained by coordinated processes of protein production, folding, and degradation. Translational efficiency of a given mRNA depends on how often the ribosomes initiate synthesis of a new polypeptide and how
Externí odkaz:
https://doaj.org/article/b1c838c467e24f9d9e20c99b0b51075d
Publikováno v:
eLife, Vol 9 (2020)
Nascent polypeptides begin to fold in the constrained space of the ribosomal peptide exit tunnel. Here we use force-profile analysis (FPA) and photo-induced energy-transfer fluorescence correlation spectroscopy (PET-FCS) to show how a small α-helica
Externí odkaz:
https://doaj.org/article/05d31da4c01b4590b369fa1ff5ad0199
Publikováno v:
Biomolecules, Vol 10, Iss 1, p 97 (2020)
Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different wa
Externí odkaz:
https://doaj.org/article/8b4f6f4ef0944b409348ff0e9590e470
Autor:
Xabier Agirrezabala, Ekaterina Samatova, Meline Macher, Marija Liutkute, Manisankar Maiti, David Gil‐Carton, Jiri Novacek, Mikel Valle, Marina V Rodnina
Publikováno v:
The EMBO Journal
Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent chains is not only shaped by their amino acid sequence but also by the interactions with the ribosome. Here, we combine biophysical methods with cryo-E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ac7fd4b6df2313930ed5d83924f6ef7
https://hdl.handle.net/21.11116/0000-000A-CA95-A21.11116/0000-000A-CA98-7
https://hdl.handle.net/21.11116/0000-000A-CA95-A21.11116/0000-000A-CA98-7
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
Nascent polypeptides begin to fold in the constrained space of the ribosomal peptide exit tunnel. Here we use force-profile analysis (FPA) and photo-induced energy-transfer fluorescence correlation spectroscopy (PET-FCS) to show how a small α-helica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8be9391ec99495d9693cfb51240265be
https://elifesciences.org/articles/60895
https://elifesciences.org/articles/60895
Publikováno v:
Biophysical Journal. 118:30a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::26fca72bb6509b4583d85a418ee307b9
https://doi.org/10.1016/j.bpj.2019.11.342
https://doi.org/10.1016/j.bpj.2019.11.342
Autor:
Meline Macher, Ekaterina Samatova, Marija Liutkute, Manisankar Maiti, Wolfgang Wintermeyer, Marina V. Rodnina, Evan Mercier
Publikováno v:
Biophysical Journal. 118:319a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8b799a3eda9f284b0112212dea628d3
https://doi.org/10.1016/j.bpj.2019.11.1791
https://doi.org/10.1016/j.bpj.2019.11.1791
Publikováno v:
Biomolecules
Biomolecules, Vol 10, Iss 1, p 97 (2020)
Biomolecules, Vol 10, Iss 1, p 97 (2020)
Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8704d7fa367498eeffd9354318ea716
https://doi.org/10.3390/biom10010097
https://doi.org/10.3390/biom10010097
Autor:
Marija Liutkute, Marina V. Rodnina, Ekaterina Samatova, Manisankar Maiti, Jörg Enderlein, Wolf Holtkamp
Publikováno v:
Biophysical Journal. 116:189a-190a
The ribosome synthesizes proteins according to the sequence of the messenger RNA (mRNA) by progressively adding amino acids to the C-terminus of the nascent peptide. For a protein to become fully functional, it has to fold into a specific three-dimen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::951f7dd484dd2cbf5eac384f73b87e15
https://doi.org/10.1016/j.bpj.2018.11.1050
https://doi.org/10.1016/j.bpj.2018.11.1050