Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Wojciech Delewski"'
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:
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:
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efecbbdba4d8e75d896460dd593d9d2f
https://doaj.org/article/101d4b2643d04db4b8351919b8a8bf11
https://doaj.org/article/101d4b2643d04db4b8351919b8a8bf11
Autor:
Szymon J. Ciesielski, Brenda Schilke, Bartlomiej Tomiczek, Wojciech Delewski, Rafal Dutkiewicz, Milena Stolarska, Jaroslaw Marszalek, Jacek Czub, Igor Grochowina, Lukasz Nierzwicki, Elizabeth A. Craig, Marta A. Uzarska
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 6, p e1007913 (2020)
PLoS Computational Biology
PLoS Computational Biology
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://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6cc4a7733677c6e2c726877b0ad76b9
https://doi.org/10.1371/journal.pcbi.1007913
https://doi.org/10.1371/journal.pcbi.1007913
Autor:
Mateusz Manicki, Brenda Schilke, Lukasz Nierzwicki, Jaroslaw Marszalek, Bartlomiej Tomiczek, Wojciech Delewski, Bogumiła Paterkiewicz, Rafal Dutkiewicz, Szymon J. Ciesielski, Elizabeth A. Craig, Jacek Czub
Publikováno v:
Molecular Biology and Evolution. 33:643-656
Biogenesis of iron-sulfur clusters (FeS) is a highly conserved process involving Hsp70 and J-protein chaperones. However, Hsp70 specialization differs among species. In most eukaryotes, including Schizosaccharomyces pombe, FeS biogenesis involves int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ca4c396f7a60e558504b11e919bb59
https://doi.org/10.1093/molbev/msv254
https://doi.org/10.1093/molbev/msv254
Autor:
Ji-Yoon Song, Brenda Schilke, Rafal Dutkiewicz, Anna Blenska, Jaroslaw Marszalek, Elizabeth A. Craig, Julia Majewska, Szymon J. Ciesielski, Jacek Kominek, Wojciech Delewski
Publikováno v:
The Journal of biological chemistry. 288(40)
Biogenesis of mitochondrial iron-sulfur (Fe/S) cluster proteins requires the interaction of multiple proteins with the highly conserved 14-kDa scaffold protein Isu, on which clusters are built prior to their transfer to recipient proteins. For exampl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::556a840ed5e625d673ca5b8718079796
https://pubmed.ncbi.nlm.nih.gov/23946486
https://pubmed.ncbi.nlm.nih.gov/23946486