Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Andrew M. Fuchs"'
Autor:
Meranda M. Masse, Valeria Guzman-Luna, Angela E. Varela, Ummay Mahfuza Shapla, Rachel B. Hutchinson, Aniruddha Srivastava, Wanting Wei, Andrew M. Fuchs, Silvia Cavagnero
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-20 (2024)
Abstract In order to become bioactive, proteins must be translated and protected from aggregation during biosynthesis. The ribosome and molecular chaperones play a key role in this process. Ribosome-bound nascent chains (RNCs) of intrinsically disord
Externí odkaz:
https://doaj.org/article/ccccc773fb76407e9c9ea3cd41c47b41
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-17 (2021)
Guzman-Luna et al. present a crosslinking analysis of the interaction of unstructured nascent chains with ribosomal proteins near the nascent polypeptide exit tunnel of the ribosome. They further analyze the dependence of these interactions on the pe
Externí odkaz:
https://doaj.org/article/31ac312184584d059fe46bce8b8d198c
Autor:
Meranda M. Masse, Valeria Guzman-Luna, Angela E. Varela, Rachel B. Hutchinson, Aniruddha Srivast, Wanting Wei, Andrew M. Fuchs, Silvia Cavagnero
In order to become bioactive, proteins must be translated and protected from aggregation during biosynthesis. The ribosome and molecular chaperones play a key role in this process. Ribosome-bound nascent chains (RNCs) of intrinsically disordered prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3563d53ac1a333267b0961701fbf3ff8
https://doi.org/10.21203/rs.3.rs-2734168/v1
https://doi.org/10.21203/rs.3.rs-2734168/v1
Autor:
Meranda M. Masse, Valeria Guzman-Luna, Angela E. Varela, Rachel B. Hutchinson, Aniruddha Srivastava, Wanting Wei, Andrew M Fuchs, Silvia Cavagnero
Publikováno v:
Biophysical Journal. 122:336a
In order to become bioactive, proteins need to be biosynthesized and protected from aggregation during translation. The ribosome and molecular chaperones contribute to both of these tasks. While it is known that some ribosomal proteins (r-proteins) i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34f40dc04b613a77c563fb9a8bd8842
https://doi.org/10.1016/j.bpj.2022.11.1875
https://doi.org/10.1016/j.bpj.2022.11.1875
Publikováno v:
Biophysical Journal. 120:197a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cfe6db02dfa4a08819404f0b82c5e57
https://doi.org/10.1016/j.bpj.2020.11.1357
https://doi.org/10.1016/j.bpj.2020.11.1357
Autor:
Caleb D. Frost, Jonathan M. Koch, Melissa M. Mueller, Christopher T. Veldkamp, Paul G. House, Emily R. Lackner, Justin T. O'Rorke, Heather A. Heinen, Andrew M. Fuchs, Francis C. Peterson, David R. Graupner, Scott J. Schoeller, Kyle P. Gerarden
Publikováno v:
Acta Crystallographica Section F
The solution structure of the cold-shock-like protein from R. rickettsii, the causative agent of Rocky Mountain spotted fever, is reported.
Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitt
Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3251c6ee476ae60467e0047668aefc3e
https://doi.org/10.1107/s174430911203881x
https://doi.org/10.1107/s174430911203881x
Publikováno v:
Biophysical Journal. 114:595a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1eec24b791e96440154709d4caeb74b
https://doi.org/10.1016/j.bpj.2017.11.3251
https://doi.org/10.1016/j.bpj.2017.11.3251
Autor:
Andrew M. Fuchs
Publikováno v:
Biophysical Journal. 110:235a
The initial stages of a protein's life in the cell are crucial for the proper balance between folding, misfolding and aggregation. While an appreciable amount of information is known about protein folding/unfolding after biosynthesis, we lack a clear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e000dddff55d05a94c0be9d9b10ef123
https://doi.org/10.1016/j.bpj.2015.11.1296
https://doi.org/10.1016/j.bpj.2015.11.1296