E
Etsuko Sugawara
Researcher at University of California, Berkeley
Publications - 15
Citations - 1567
Etsuko Sugawara is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Porin & Bacterial outer membrane. The author has an hindex of 13, co-authored 15 publications receiving 1354 citations.
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Journal ArticleDOI
Properties of AdeABC and AdeIJK Efflux Systems of Acinetobacter baumannii Compared with Those of the AcrAB-TolC System of Escherichia coli
Etsuko Sugawara,Hiroshi Nikaido +1 more
TL;DR: Both A. baumannii efflux systems pumped out a wide range of compounds, but AdeABC was less effective than AcrAB-TolC in the extrusion of lipophilic β-lactams, novobiocin, and ethidium bromide, although it was more effective at tetracycline efflux.
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Pore-forming activity of OmpA protein of Escherichia coli.
Etsuko Sugawara,Hiroshi Nikaido +1 more
TL;DR: When proteoliposomes reconstituted from the purified OmpA, phospholipids, and lithium dodecyl sulfate were tested for permeability to small molecules by osmotic swelling, it was found that OMPA produced apparently nonspecific diffusion channels that allowed the penetration of various solutes.
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Export of autotransported proteins proceeds through an oligomeric ring shaped by C‐terminal domains
TL;DR: It is reported that purified C‐IgAP forms an oligomeric complex of ∼500 kDa with a ring‐like structure containing a central cavity of ∼2 nm diameter that is the conduit for the export of the N‐doms.
Journal ArticleDOI
OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms.
Etsuko Sugawara,Hiroshi Nikaido +1 more
TL;DR: Denaturation of open form OmpA and its subsequent renaturation converted it into a nonfunctional or closed form, suggesting that the open and closed forms represent two alternative conformers of this protein.
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Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa.
TL;DR: When purified without the use of ionic detergents, both OmpA and OprF proteins contained nearly 20% alpha-helical structures, which disappeared completely upon the addition of sodium dodecyl sulfate, suggesting that the proteins fold in a similar manner.