Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Lisa D. Cabrita"'
Autor:
Tomasz Włodarski, Julian O. Streit, Alkistis Mitropoulou, Lisa D. Cabrita, Michele Vendruscolo, John Christodoulou
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-16 (2024)
Abstract Cryogenic electron microscopy (cryo-EM) has emerged as a powerful method for the determination of structures of complex biological molecules. The accurate characterisation of the dynamics of such systems, however, remains a challenge. To add
Externí odkaz:
https://doaj.org/article/34880de7ddfb434da7db67f9fc377c9f
Autor:
Minkoo Ahn, Tomasz Włodarski, Alkistis Mitropoulou, Sammy H. S. Chan, Haneesh Sidhu, Elena Plessa, Thomas A. Becker, Nediljko Budisa, Christopher A. Waudby, Roland Beckmann, Anaïs M. E. Cassaignau, Lisa D. Cabrita, John Christodoulou
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
The narrow exit tunnel of the ribosome is important for cotranslational protein folding. Here, authors show that their rationally designed and engineered exit tunnel protein loops modulate the free energy of nascent chain dynamics and folding.
Externí odkaz:
https://doaj.org/article/cea56fc2e4f24b7ba30039a8d7fd533e
Autor:
Elena Plessa, Lien P. Chu, Sammy H. S. Chan, Oliver L. Thomas, Anaïs M. E. Cassaignau, Christopher A. Waudby, John Christodoulou, Lisa D. Cabrita
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Alpha-1-antitrypsin (AAT) deficiency results from misfolding-prone AAT variants. Here the authors show that AAT forms co-translational folding intermediates on the ribosome that persist upon release and determine its folding fate. They show too that
Externí odkaz:
https://doaj.org/article/30b1313e15054f30a9de5b5032f07b04
Autor:
Minkoo Ahn, Tomasz Włodarski, Alkistis Mitropoulou, Sammy H. S. Chan, Haneesh Sidhu, Elena Plessa, Thomas A. Becker, Nediljko Budisa, Christopher A. Waudby, Roland Beckmann, Anaïs M. E. Cassaignau, Lisa D. Cabrita, John Christodoulou
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-1 (2022)
Externí odkaz:
https://doaj.org/article/92f54f5ec89546f796f3ac1be4fca799
Autor:
Sammy H. S. Chan, Tomasz Włodarski, Julian O. Streit, Anaïs M. E. Cassaignau, Lauren F. Woodburn, Minkoo Ahn, Georg Johannes Freiherr von Sass, Christopher A. Waudby, Nediljko Budisa, Lisa D. Cabrita, John Christodoulou
Publikováno v:
Nature Chemistry. 14:1165-1173
Co-translational folding is crucial to ensure the production of biologically active proteins. The ribosome can alter the folding pathways of nascent polypeptide chains, yet a structural understanding remains largely inaccessible experimentally. We ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ca652710e3753d3ef25db725aa28acc
https://doi.org/10.1038/s41557-022-01004-0
https://doi.org/10.1038/s41557-022-01004-0
Autor:
Oliver L. Thomas, Lisa D. Cabrita, Sammy H. S. Chan, Lien P. Chu, Christopher A. Waudby, John Christodoulou, Anaïs M. E. Cassaignau, Elena Plessa
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications
Nature Communications
During biosynthesis, proteins can begin folding co-translationally to acquire their biologically-active structures. Folding, however, is an imperfect process and in many cases misfolding results in disease. Less is understood of how misfolding begins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5f7f3de9912b73c17d7b316c968cb63
https://doaj.org/article/30b1313e15054f30a9de5b5032f07b04
https://doaj.org/article/30b1313e15054f30a9de5b5032f07b04
Autor:
Lauren F Woodburn, Christopher A. Waudby, Anaïs M. E. Cassaignau, John Christodoulou, Ivana V Bukvin, Lisa D. Cabrita, Sammy H. S. Chan, Tomasz Wlodarski, Julian O Streit
Publikováno v:
Nature Chemistry
Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that interactions between the emerging polypeptide and the ribosome surface might allow the ribosome itself to modulate co-translational folding. Here we combine p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d47a966a27bccf958d4ead1a53652c6b
https://doi.org/10.1038/s41557-021-00796-x
https://doi.org/10.1038/s41557-021-00796-x
Autor:
Lisa D. Cabrita, Anaïs M. E. Cassaignau, Charles Burridge, Christopher A. Waudby, John Christodoulou, Tomasz Wlodarski
Publikováno v:
Chemical Science
The folding of many proteins can begin during biosynthesis on the ribosome and can be modulated by the ribosome itself. Such perturbations are generally believed to be mediated through interactions between the nascent chain and the ribosome surface,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::709ed17fc2a4f3361b76fade2d310e29
http://europepmc.org/articles/PMC8513902
http://europepmc.org/articles/PMC8513902
Autor:
Annika Deckert, Anaïs M. E. Cassaignau, Xiaolin Wang, Tomasz Włodarski, Sammy H. S. Chan, Christopher A. Waudby, John P. Kirkpatrick, Michele Vendruscolo, Lisa D. Cabrita, John Christodoulou
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Proteins are produced by ribosomes in the cell, and during this process, can begin to adopt their biologically active forms assisted by molecular chaperones such as trigger factor. This fundamental cellular mechanism is crucial to mainta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d21039c47a277be0a4d67f3422c0565f
http://europepmc.org/articles/PMC8719866
http://europepmc.org/articles/PMC8719866
Autor:
Sammy H S, Chan, Tomasz, Włodarski, Julian O, Streit, Anaïs M E, Cassaignau, Lauren F, Woodburn, Minkoo, Ahn, Georg Johannes, Freiherr von Sass, Christopher A, Waudby, Nediljko, Budisa, Lisa D, Cabrita, John, Christodoulou
Publikováno v:
Nature chemistry. 14(10)
Co-translational folding is crucial to ensure the production of biologically active proteins. The ribosome can alter the folding pathways of nascent polypeptide chains, yet a structural understanding remains largely inaccessible experimentally. We ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d1ff61592af0aa5efd1162eb81d23d33
https://pubmed.ncbi.nlm.nih.gov/35927328
https://pubmed.ncbi.nlm.nih.gov/35927328