Zobrazeno 1 - 10
of 286
pro vyhledávání: '"Elizabeth A, Craig"'
Autor:
Victoria Elizabeth Mabel Craig, Derek Francis McLaughlin, Karen P. Devlin, Aiveen Higgins, Breidge Boyle
Publikováno v:
BMC Digital Health, Vol 2, Iss 1, Pp 1-15 (2024)
Abstract Background Playing Tetris is a relatively new concept when considering how to treat or prevent post-traumatic stress symptoms (PTSS). Benefits have been identified regarding how playing the game can influence traumatic memory processing and
Externí odkaz:
https://doaj.org/article/7a4bcbc19c4f440fabd50d617be7ed95
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:
Olivia A Smith, Elizabeth C Craig
Publikováno v:
Avian Conservation and Ecology, Vol 18, Iss 2, p 1 (2023)
Climate change and associated shifts in marine prey communities can alter food availability for foraging seabirds. This issue is illustrated in the Gulf of Maine by the northward shift of Atlantic butterfish ( Peprilus triacanthus ; hereafter butterf
Externí odkaz:
https://doaj.org/article/964b98fe1f3f4ba4975fb4822a9ce638
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:
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:
Bartlomiej Tomiczek, Wojciech Delewski, Lukasz Nierzwicki, Milena Stolarska, Igor Grochowina, Brenda Schilke, Rafal Dutkiewicz, Marta A Uzarska, Szymon J Ciesielski, Jacek Czub, Elizabeth A Craig, Jaroslaw Marszalek
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 6, p e1007913 (2020)
J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with substrate polypeptides upon hydrolysis of its bound ATP. Although a rec
Externí odkaz:
https://doaj.org/article/6137714d2eb446d5ac4f961e7b40983d
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:
Om Kumar Shrestha, Ruchika Sharma, Bartlomiej Tomiczek, Woonghee Lee, Marco Tonelli, Gabriel Cornilescu, Milena Stolarska, Lukasz Nierzwicki, Jacek Czub, John L Markley, Jaroslaw Marszalek, Szymon J Ciesielski, Elizabeth A Craig
Publikováno v:
PLoS ONE, Vol 14, Iss 5, p e0217098 (2019)
The J-domain protein Zuotin is a multi-domain eukaryotic Hsp70 co-chaperone. Though it is primarily ribosome-associated, positioned at the exit of the 60S subunit tunnel where it promotes folding of nascent polypeptide chains, Zuotin also has off-rib
Externí odkaz:
https://doaj.org/article/b09f12cb237047c2956e4aed7205ec36
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::956d2de4de2ffb4ff0a8f67a7b6cf50f
https://pubmed.ncbi.nlm.nih.gov/36520311
https://pubmed.ncbi.nlm.nih.gov/36520311
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