S
Susanne C. Feil
Researcher at St. Vincent's Institute of Medical Research
Publications - 40
Citations - 3216
Susanne C. Feil is an academic researcher from St. Vincent's Institute of Medical Research. The author has contributed to research in topics: Protein structure & Cholesterol-dependent cytolysin. The author has an hindex of 23, co-authored 40 publications receiving 3044 citations. Previous affiliations of Susanne C. Feil include St. Vincent's Health System & University of Melbourne.
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Journal ArticleDOI
Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form.
TL;DR: The first crystal structure of a thiol-activated cytolysin, perfringolysin O, a member of a large family of toxins that kill eukaryotic cells by punching holes in their membranes is presented.
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Pore-forming protein toxins: from structure to function.
TL;DR: Recent work suggests a number of common features in the mechanism of membrane insertion may exist for each class of PFTs, and nearly all can be classified into one of two families based on the types of pores they are thought to form: alpha-P FTs or beta-PFTs.
Journal ArticleDOI
AMPK β Subunit Targets Metabolic Stress Sensing to Glycogen
Galina Polekhina,Abhilasha Gupta,Belinda J. Michell,Bryce J. W. van Denderen,Sid Murthy,Susanne C. Feil,Ian G. Jennings,Duncan J. Campbell,Duncan J. Campbell,Lee A. Witters,Michael W. Parker,Michael W. Parker,Bruce E. Kemp,Bruce E. Kemp,David Stapleton,David Stapleton +15 more
TL;DR: It is shown that the AMPK β subunit contains a functional glycogen binding domain (β-GBD) that is most closely related to isoamylase domains found in glycogen and starch branching enzymes.
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Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein.
Jamie Rossjohn,Roberto Cappai,Roberto Cappai,Susanne C. Feil,Anna Henry,Anna Henry,William J. McKinstry,Denise Galatis,Denise Galatis,Lars Hesse,Gerd Multhaup,Konrad Beyreuther,Colin L. Masters,Colin L. Masters,Michael W. Parker +14 more
TL;DR: Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggests the APP N-terminal domain could function as a growth factor in vivo.
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Crystal structure of a theta-class glutathione transferase.
TL;DR: Surprisingly, the equivalent residue in the theta‐class structure is not in the active site, but its role appears to have been replaced by either a nearby serine or by another tyrosine residue located in the C‐terminal domain of the enzyme.