Zobrazeno 1 - 10
of 302
pro vyhledávání: '"Lila M. Gierasch"'
Autor:
Erik B. Nordquist, Charles A. English, Eugenia M. Clerico, Woody Sherman, Lila M. Gierasch, Jianhan Chen
Publikováno v:
PLoS Computational Biology, Vol 17, Iss 11 (2021)
To help cells cope with protein misfolding and aggregation, Hsp70 molecular chaperones selectively bind a variety of sequences (“selective promiscuity”). Statistical analyses from substrate-derived peptide arrays reveal that DnaK, the E. coli Hsp
Externí odkaz:
https://doaj.org/article/ad3b0c700af84c299fcbf138aa4bb030
Publikováno v:
Journal of Lipid Research, Vol 61, Iss 4, Pp 465- (2020)
Externí odkaz:
https://doaj.org/article/0e219db6e3694c8295d71695e67d471f
Publikováno v:
Journal of Lipid Research, Vol 61, Iss 7, Pp 969-970 (2020)
Externí odkaz:
https://doaj.org/article/57775e5fa3d74dfa9875d8ac19f1db17
Publikováno v:
Journal of Lipid Research, Vol 60, Iss 4, Pp 719-720 (2019)
Externí odkaz:
https://doaj.org/article/609afc84676148418e43cb4414f42001
Autor:
Younhee Cho, Xin Zhang, Kristine Faye R. Pobre, Yu Liu, David L. Powers, Jeffery W. Kelly, Lila M. Gierasch, Evan T. Powers
Publikováno v:
Cell Reports, Vol 11, Iss 2, Pp 321-333 (2015)
The folding fate of a protein in vivo is determined by the interplay between a protein’s folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual comp
Externí odkaz:
https://doaj.org/article/91b493a5c85e427482a2079d643a323c
Publikováno v:
Cell Reports, Vol 1, Iss 3, Pp 265-276 (2012)
To gain insight into the interplay of processes and species that maintain a correctly folded, functional proteome, we have developed a computational model called FoldEco. FoldEco models the cellular proteostasis network of the E. coli cytoplasm, incl
Externí odkaz:
https://doaj.org/article/13cc089476ab47478bc2785c13568b47
Publikováno v:
The Journal of Physical Chemistry B. 126:6780-6791
Hsp70 molecular chaperones play central roles in maintaining a healthy cellular proteome. Hsp70s function by binding to short peptide sequences in incompletely folded client proteins, thus preventing them from misfolding and/or aggregating, and in ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6da807218023964cdab678c7515b4dd
https://doi.org/10.1021/acs.jpcb.2c03806
https://doi.org/10.1021/acs.jpcb.2c03806
Autor:
Upneet Kaur, Kyle C. Kihn, Haiping Ke, Weiwei Kuo, Lila M. Gierasch, Daniel N. Hebert, Patrick L. Wintrode, Daniel Deredge, Anne Gershenson
Many multi-domain proteins including the serpin family of serine protease inhibitors contain non-sequential domains composed of regions that are far apart in sequence. Because proteins are translated vectorially from N-to C-terminus, such domains pos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2de98a94a1a2dfc8cfa68e0d48ae20c
https://doi.org/10.1101/2023.04.24.537978
https://doi.org/10.1101/2023.04.24.537978
Autor:
Haiping Ke, Kevin P. Guay, Terence R. Flotte, Lila M. Gierasch, Anne Gershenson, Daniel N. Hebert
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Heterologous expression of proteins is used widely for the biosynthesis of biologics, many of which are secreted from cells. In addition, gene therapy and messenger RNA (mRNA) vaccines frequently direct the expression of secretory proteins to nonnati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26380ce40dedf9db7c12f58070ca5f69
https://doi.org/10.1073/pnas.2206103119
https://doi.org/10.1073/pnas.2206103119
Publikováno v:
The FASEB Journal. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d1566889491e773229a38fe2c482f7a
https://doi.org/10.1096/fasebj.2022.36.s1.r3782
https://doi.org/10.1096/fasebj.2022.36.s1.r3782