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of 4
pro vyhledávání: '"Brenda A. Schilke"'
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:
Brenda A Schilke, Szymon J Ciesielski, Thomas Ziegelhoffer, Erina Kamiya, Marco Tonelli, Woonghee Lee, Gabriel Cornilescu, Justin K Hines, John L Markley, Elizabeth A Craig
Publikováno v:
PLoS Genetics, Vol 13, Iss 10, p e1007084 (2017)
By binding to a multitude of polypeptide substrates, Hsp70-based molecular chaperone systems perform a range of cellular functions. All J-protein co-chaperones play the essential role, via action of their J-domains, of stimulating the ATPase activity
Externí odkaz:
https://doaj.org/article/3b39ed135dee43bd8878ef4ccb38a39f
Publikováno v:
eLife, Vol 6 (2017)
Proteins destined for the mitochondrial matrix are targeted to the inner membrane Tim17/23 translocon by their presequences. Inward movement is driven by the matrix-localized, Hsp70-based motor. The scaffold Tim44, interacting with the matrix face of
Externí odkaz:
https://doaj.org/article/0104b2f18b76410d93481b1db0836fac
Autor:
Brenda A. Schilke, Elizabeth A. Craig
Publikováno v:
Molecular biology of the cell. 33(3)
Why Sis1 is the only essential J-domain protein cochaperone of the yeast cytosol/nucleus is unknown. We isolated suppressors having substitutions in Tti1, a component of the TTT complex, which is a specialized chaperone system for PIKK proteins, sugg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa79232d73bfa9bf0fb1577a20fb22d1
https://pubmed.ncbi.nlm.nih.gov/34935410
https://pubmed.ncbi.nlm.nih.gov/34935410