Zobrazeno 1 - 10
of 286
pro vyhledávání: '"Elizabeth A. Craig"'
Autor:
Samantha J. Ganser, Bridget A. McNish, Gillian L. Schwanitz, John L. Delaney, Bridget A. Corpus, Brenda A. Schilke, Anup K. Biswal, Chandan Sahi, Elizabeth A. Craig, Justin K. Hines
Publikováno v:
Frontiers in Molecular Biosciences, Vol 11 (2024)
J-domain proteins (JDPs) are obligate cochaperones of Hsp70s. The Class A JDP Apj1 of the yeast cytosol has an unusually complex region between the N-terminal J-domain and the substrate binding region—often called the Grich or GF region in Class A
Externí odkaz:
https://doaj.org/article/d1fe474f7674468bb48d114d8a70c204
Autor:
Jaroslaw Marszalek, Elizabeth A. Craig
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
In cells molecular chaperone systems consisting of Hsp70 and its obligatory J-domain protein (JDP) co-chaperones transiently interact with a myriad of client proteins—with JDPs typically recruiting their partner Hsp70 to interact with particular cl
Externí odkaz:
https://doaj.org/article/733e4668594f455bb517b2a41c94e9a9
Autor:
Kanghyun Lee, Thomas Ziegelhoffer, Wojciech Delewski, Scott E. Berger, Grzegorz Sabat, Elizabeth A. Craig
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Here, the authors use in vivo site-specific crosslinking to provide molecular-level insight into how the fungal Hsp70 chaperone system — the Ssb:Ssz1:Zuo1 triad — assists the folding process for the nascent peptide chain emerging from the ribosom
Externí odkaz:
https://doaj.org/article/101d4b2643d04db4b8351919b8a8bf11
Autor:
Elizabeth A. Craig
Publikováno v:
BMC Biology, Vol 16, Iss 1, Pp 1-11 (2018)
Abstract Efficient movement of proteins across membranes is required for cell health. The translocation process is particularly challenging when the channel in the membrane through which proteins must pass is narrow—such as those in the membranes o
Externí odkaz:
https://doaj.org/article/a1ddfae2984d42488085aa34fa8f052c
Autor:
Malgorzata Kleczewska, Aneta Grabinska, Marcin Jelen, Milena Stolarska, Brenda Schilke, Jaroslaw Marszalek, Elizabeth A. Craig, Rafal Dutkiewicz
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 9, p 3326 (2020)
Mitochondria play a central role in the biogenesis of iron–sulfur cluster(s) (FeS), protein cofactors needed for many cellular activities. After assembly on scaffold protein Isu, the cluster is transferred onto a recipient apo-protein. Transfer req
Externí odkaz:
https://doaj.org/article/9117244329db4033804783fab3a6c884
Publikováno v:
PLoS Genetics, Vol 7, Iss 2 (2011)
Externí odkaz:
https://doaj.org/article/c98e988c72ec4df7b6f17ab647b97f80
Publikováno v:
Sub-cellular biochemistry. 101
Mitochondrial J-domain protein (JDP) co-chaperones orchestrate the function of their Hsp70 chaperone partner(s) in critical organellar processes that are essential for cell function. These include folding, refolding, and import of mitochondrial prote
Autor:
Thomas Ziegelhoffer, Grzegorz Sabat, Scott E Berger, Wojciech Delewski, Elizabeth A. Craig, Kanghyun Lee
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Nature Communications
Nature Communications
In eukaryotes, an Hsp70 molecular chaperone triad assists folding of nascent chains emerging from the ribosome tunnel. In fungi, the triad consists of canonical Hsp70 Ssb, atypical Hsp70 Ssz1 and J-domain protein cochaperone Zuo1. Zuo1 binds the ribo
Publikováno v:
Wildlife Society Bulletin. 46
It's a painful reality for many pet owners that at some point there will come a time when they must grieve the loss of their animal companion. In fact, the death of a pet is perhaps one of the most common sources of stress that families experience, o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::451ed05367a8b7e56354ea9a153d1fea
https://doi.org/10.4018/978-1-7998-9125-3.ch023
https://doi.org/10.4018/978-1-7998-9125-3.ch023