Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Christina M. Hurley"'
Autor:
Mary D. Cundiff, Christina M. Hurley, Jeremy D. Wong, Joseph A. Boscia, Aarti Bashyal, Jake Rosenberg, Eden L. Reichard, Nicholas D. Nassif, Jennifer S. Brodbelt, Daniel A. Kraut
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-17 (2019)
Abstract The ubiquitin-proteasome system (UPS) is responsible for the bulk of protein degradation in eukaryotic cells, but the factors that cause different substrates to be unfolded and degraded to different extents are still poorly understood. We pr
Externí odkaz:
https://doaj.org/article/88efcdeee9f84f3485e5d78c2f85812e
Autor:
Michael B. Cory, Chloe M. Jones, Kyle D. Shaffer, Yarra Venkatesh, Sam Giannakoulias, Ryann M. Perez, Marshall G. Lougee, Eshe Hummingbird, Vinayak V. Pagar, Christina M. Hurley, Allen Li, Robert H. Mach, Rahul M. Kohli, E. James Petersson
Publikováno v:
Protein Science. 32
Autor:
Michael B. Cory, Allen Li, Christina M. Hurley, Zachary M. Hostetler, Yarra Venkatesh, Chloe M. Jones, E. James Petersson, Rahul M. Kohli
The SOS response is a bacterial DNA damage response pathway that has been heavily implicated in bacteria’s ability to evolve resistance to antibiotics. Activation of the SOS response is dependent on the interaction between two bacterial proteins, R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::812a4304f01c14cb4667cf4ade1275e8
https://doi.org/10.1101/2022.09.30.510415
https://doi.org/10.1101/2022.09.30.510415
Autor:
Christina M, Hurley, Daniel A, Kraut
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2365
We use an in vitro degradation assay with a model substrate to assess proteasomal unfolding ability. Our substrate has an unstructured region that is the site of ubiquitination, followed by an easy-to-unfold domain and a difficult-to-unfold domain. D
Autor:
Christopher Eric Braganca, Julianna Rose Cresti, Joseph A. Boscia, Abramo J. Manfredonia, Christina M. Hurley, Mary D. Cundiff, Daniel A. Kraut
Publikováno v:
Proc Natl Acad Sci U S A
The 26S proteasome is the macromolecular machine responsible for the bulk of protein degradation in eukaryotic cells. As it degrades a ubiquitinated protein, the proteasome transitions from a substrate-accepting conformation (s1) to a set of substrat
Autor:
Christina M. Hurley, Daniel A. Kraut
Publikováno v:
Targeted Protein Degradation ISBN: 9781071616642
We use an in vitro degradation assay with a model substrate to assess proteasomal unfolding ability. Our substrate has an unstructured region that is the site of ubiquitination, followed by an easy-to-unfold domain and a difficult-to-unfold domain. D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f77d523db090d3522ef638918f7bce0
https://doi.org/10.1007/978-1-0716-1665-9_12
https://doi.org/10.1007/978-1-0716-1665-9_12
Autor:
Jake Rosenberg, Christina M. Hurley, Eden L. Reichard, Jeremy D. Wong, Nicholas D. Nassif, Mary D. Cundiff, Joseph A. Boscia, Aarti Bashyal, Daniel A. Kraut, Jennifer S. Brodbelt
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-17 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-17 (2019)
The ubiquitin-proteasome system (UPS) is responsible for the bulk of protein degradation in eukaryotic cells, but the factors that cause different substrates to be unfolded and degraded to different extents are still poorly understood. We previously