Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Elizabeth C. Duran"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 4 (2017)
Cellular proteostasis involves not only the expression of proteins in response to environmental needs, but also the timely repair or removal of damaged or unneeded proteins. AAA+ motor proteins are critically involved in these pathways. Here, we revi
Externí odkaz:
https://doaj.org/article/48b6bd477c5c4de7bac04341afb702ed
Autor:
Aaron T. Blanchard, Zi Li, Elizabeth C. Duran, Catherine E. Scull, J. Damon Hoff, Keenan R. Wright, Victor Pan, Nils G. Walter
Publikováno v:
Nano Lett
DNA-based FluoroCubes were recently developed as a solution to photobleaching, a ubiquitous limitation of fluorescence microscopy (Niekamp, Stuurman, & Vale, Nature Methods, 2020). FluoroCubes – compact ~4×4×5.4nm(3) four-helix bundles bound by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e1ea601bdd4988a7bd4866ec0325667
https://europepmc.org/articles/PMC10080265/
https://europepmc.org/articles/PMC10080265/
Autor:
Aaron L. Lucius, Elizabeth C. Duran
Publikováno v:
Protein Sci
Escherichia coli ClpA is a AAA+ (ATPase Associated with diverse cellular Activities) chaperone that catalyzes the ATP-dependent unfolding and translocation of substrate proteins targeted for degradation by a protease, ClpP. ClpA hexamers associate wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75e4a99df30304fd29c8a43562c15224
https://doi.org/10.1002/pro.3638
https://doi.org/10.1002/pro.3638
Autor:
Aaron T. Blanchard, Zi Li, Elizabeth C. Duran, Catherine E. Scull, J. Damon Hoff, Keenan R. Wright, Victor Pan, Nils G. Walter
Publikováno v:
Nano Letters. 22:8032-8032
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9487c9a4dc379aee1cfc6a1f14bb52b2
https://doi.org/10.1021/acs.nanolett.2c03349
https://doi.org/10.1021/acs.nanolett.2c03349
Autor:
JiaBei Lin, Meredith E. Jackrel, Elizabeth A. Sweeny, Elizabeth C. Duran, Korrie L. Mack, Clarissa L. Weaver, James Shorter, Aaron L. Lucius
Publikováno v:
Biochemistry. 56:2071-2075
Recent Hsp104 structural studies have reported both planar and helical models of the hexameric structure. The conformation of Hsp104 monomers within the hexamer is affected by nucleotide ligation. After nucleotide-driven hexamer formation, Hsp104-cat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c16c2ea75f2f53eead5b5438a5234b2c
https://doi.org/10.1021/acs.biochem.7b00225
https://doi.org/10.1021/acs.biochem.7b00225
Autor:
Elizabeth C. Duran, Nils G. Walter
Publikováno v:
Biophysical Journal. 118:223a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e1ac6588ebc75c80992013abd91020a3
https://doi.org/10.1016/j.bpj.2019.11.1322
https://doi.org/10.1016/j.bpj.2019.11.1322
Publikováno v:
Biochemistry. 57(26)
ClpB and DnaKJE provide protection to Escherichia coli cells during extreme environmental stress. Together, this co-chaperone system can resolve protein aggregates, restoring misfolded proteins to their native form and function in solubilizing damage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd0a466fcb8a88832b9f598556227064
https://pubmed.ncbi.nlm.nih.gov/29812913
https://pubmed.ncbi.nlm.nih.gov/29812913
Autor:
Elizabeth C. Duran, Aaron L. Lucius
Publikováno v:
Biophysical chemistry. 242
E. coli ClpA is an AAA+ (ATPase Associated with diverse cellular Activities) chaperone that catalyzes the ATP-dependent unfolding and translocation of substrate proteins for the purposes of proper proteome maintenance. Biologically active ClpA hexame
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92b88e8e0de58e683c8ac373013689eb
https://pubmed.ncbi.nlm.nih.gov/30173103
https://pubmed.ncbi.nlm.nih.gov/30173103
Autor:
Aaron L. Lucius, JiaBei Lin, Clarissa L. Weaver, Tao Li, Elizabeth C. Duran, Justin M. Miller
Publikováno v:
Biochemical Journal
Here we show that ClpB is a non-processive translocase that takes, at most, two steps on the polypeptide backbone before dissociation. These findings indicate that ClpB is not likely to translocate polypeptide through its axial channel as previously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22441b481f49a746a45fb22f484cfa5b
http://europepmc.org/articles/PMC4692069
http://europepmc.org/articles/PMC4692069
Publikováno v:
Frontiers in Molecular Biosciences, Vol 4 (2017)
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
Cellular proteostasis involves not only the expression of proteins in response to environmental needs, but also the timely repair or removal of damaged or unneeded proteins. AAA+ motor proteins are critically involved in these pathways. Here, we revi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::703cbe5124e23d8ab7f966bbb8903425
http://journal.frontiersin.org/article/10.3389/fmolb.2017.00054/full
http://journal.frontiersin.org/article/10.3389/fmolb.2017.00054/full