Zobrazeno 1 - 10
of 115
pro vyhledávání: '"Silvia Cavagnero"'
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
Autor:
Meranda M. Masse, Rachel B. Hutchinson, Christopher E. Morgan, Heather J. Allaman, Hongqing Guan, Edward W. Yu, Silvia Cavagnero
Publikováno v:
ACS Central Science, Vol 10, Iss 2, Pp 385-401 (2024)
Externí odkaz:
https://doaj.org/article/fe084fcd321b4364800f60a8496315f7
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:
Rayna M. Addabbo, Rachel B. Hutchinson, Heather J. Allaman, Matthew D. Dalphin, Miranda F. Mecha, Yue Liu, Alexios Staikos, Silvia Cavagnero
Publikováno v:
The Journal of Physical Chemistry B. 127:3990-4014
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a13795cc54f88daf034f3034dc17bcb7
https://doi.org/10.1021/acs.jpcb.2c08485
https://doi.org/10.1021/acs.jpcb.2c08485
Publikováno v:
Applied Magnetic Resonance. 54:59-75
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::854f3d9e0ed4e70244236d5d5690e39f
https://doi.org/10.1007/s00723-022-01506-7
https://doi.org/10.1007/s00723-022-01506-7
Selective Isotope Labeling and LC-Photo-CIDNP Enable NMR Spectroscopy at Low-Nanomolar Concentration
Autor:
Hanming Yang, Siyu Li, Clayton A. Mickles, Valeria Guzman-Luna, Kenji Sugisaki, Clayton M. Thompson, Hung H. Dang, Silvia Cavagnero
Publikováno v:
J Am Chem Soc
NMR spectroscopy is a powerful tool to investigate molecular structure and dynamics. The poor sensitivity of this technique, however, limits its ability to tackle questions requiring dilute samples. Low-concentration photo-chemically induced dynamic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bf91c5d14c9b057fdf842d009a5ed30
https://doi.org/10.1021/jacs.2c01809
https://doi.org/10.1021/jacs.2c01809
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:
James Eills, Dmitry Budker, Silvia Cavagnero, Eduard Y. Chekmenev, Stuart J. Elliott, Sami Jannin, Anne Lesage, Jörg Matysik, Thomas Meersmann, Thomas Prisner, Jeffrey A. Reimer, Hanming Yang, Igor V. Koptyug
Publikováno v:
Chemical reviews, vol 123, iss 4
Magnetic resonance techniques are successfully utilized in a broad range of scientific disciplines and in a number of practical applications, with medical MRI being the most widely-known example. Currently, both fundamental and applied magnetic reson
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0ff73ad83f717f7887432f493515e12
https://escholarship.org/uc/item/9r65h6z5
https://escholarship.org/uc/item/9r65h6z5
Publikováno v:
ProteinsREFERENCES.
Many proteins must interact with molecular chaperones to achieve their native state in the cell. Yet, how chaperone binding-site characteristics affect the folding process is poorly understood. The ubiquitous Hsp70 chaperone system prevents client-pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b931e06452ff99586e64681074c25c8
https://pubmed.ncbi.nlm.nih.gov/36539330
https://pubmed.ncbi.nlm.nih.gov/36539330
Autor:
Alexios Staikos, Yue Liu, Rayna M. Addabbo, Valeria Guzman-Luna, Miranda F. Mecha, Matthew D. Dalphin, Silvia Cavagnero
Publikováno v:
The Journal of Physical Chemistry B. 124:6488-6507
The relation between co- and post-translational protein folding and aggregation in the cell is poorly understood. Here, we employ a combination of fluorescence anisotropy decays in the frequency domain, fluorescence-detected solubility assays, and NM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c71c0c525747d2f87740a53561e53d6
https://doi.org/10.1021/acs.jpcb.0c03039
https://doi.org/10.1021/acs.jpcb.0c03039