Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Evans Boateng Sarbeng"'
Autor:
Qinglian Liu, Evans Boateng Sarbeng, Ying Yang, Charles E. Lyons, Hongtao Li, Huanyu Zhu, Lei Zhou, Qingdai Liu, Xueli Tian
Publikováno v:
J Biol Chem
Heat shock proteins of 70 kDa (Hsp70s) are ubiquitous and highly conserved molecular chaperones. They play multiple essential roles in assisting with protein folding and maintaining protein homeostasis. Their chaperone activity has been proposed to r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad0aa5170faac5b77e079beccbc7a7ab
https://pubmed.ncbi.nlm.nih.gov/31806707
https://pubmed.ncbi.nlm.nih.gov/31806707
Autor:
Ruifeng Qi, Wayne A. Hendrickson, Katherine Quynh Le, Christina Vorvis, Lei Zhou, Jennifer Li Wong, Xinping Xu, Qun Liu, Jiao Yang, Qinglian Liu, Hongya Xu, Evans Boateng Sarbeng
Publikováno v:
Nature Structural & Molecular Biology. 20:900-907
The 70 kD heat shock proteins (Hsp70s) are ubiquitous and highly conserved molecular chaperones essential for cellular protein folding and proteostasis. Each Hsp70 has two functional domains: a nucleotide-binding domain (NBD) that binds and hydrolyze
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::881f8f709071389becb76408884216b0
https://doi.org/10.1038/nsmb.2583
https://doi.org/10.1038/nsmb.2583
Publikováno v:
Journal of Biological Chemistry. 287:5661-5672
The molecular chaperone 70-kDa heat-shock proteins (Hsp70s) play essential roles in maintaining protein homeostasis. Hsp110, an Hsp70 homolog, is highly efficient in preventing protein aggregation but lacks the hallmark folding activity seen in Hsp70
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::457f528b7986447cb6a419a8b6d91867
https://doi.org/10.1074/jbc.m111.275057
https://doi.org/10.1074/jbc.m111.275057
Autor:
Christina Vorvis, John Eric Willis, Divya P. Kumar, Evans Boateng Sarbeng, Qinglian Liu, Vanessa C. Cabra Ledesma
Publikováno v:
Journal of Molecular Biology. 411:1099-1113
The ubiquitous molecular chaperone 70-kDa heat shock proteins (Hsp70) play key roles in maintaining protein homeostasis. Hsp70s contain two functional domains: a nucleotide binding domain and a substrate binding domain. The two domains are connected
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f62b1c05fa660c79cb0a1b28594bed9
https://doi.org/10.1016/j.jmb.2011.07.001
https://doi.org/10.1016/j.jmb.2011.07.001
Autor:
Jiao Yang, Qinglian Liu, Evans Boateng Sarbeng, Jennifer Li Wong, Hongtao Li, Qingdai Liu, Lei Zhou, Xueli Tian
Publikováno v:
The Journal of biological chemistry. 290(14)
Highly conserved molecular chaperone Hsp70 heat shock proteins play a key role in maintaining protein homeostasis (proteostasis). DnaK, a major Hsp70 in Escherichia coli, has been widely used as a paradigm for studying Hsp70s. In the absence of ATP,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c7b89caeb9a56b9eabde198281c2dc8
https://pubmed.ncbi.nlm.nih.gov/25635056
https://pubmed.ncbi.nlm.nih.gov/25635056