R
Raymond S. Norton
Researcher at Monash University
Publications - 395
Citations - 17078
Raymond S. Norton is an academic researcher from Monash University. The author has contributed to research in topics: Protein structure & Conotoxin. The author has an hindex of 63, co-authored 382 publications receiving 15545 citations. Previous affiliations of Raymond S. Norton include Walter and Eliza Hall Institute of Medical Research & Cooperative Research Centre.
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Journal ArticleDOI
The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms
Bryan G. Fry,Kim Roelants,Donald E. Champagne,Holger Scheib,Joel D. A. Tyndall,Glenn F. King,Timo J. Nevalainen,Janette A Norman,Richard J. Lewis,Raymond S. Norton,Raymond S. Norton,Camila Renjifo,Ricardo C. Rodríguez de la Vega +12 more
TL;DR: A number of overarching structural, functional, and evolutionary generalities of the protein families from which these toxins have been frequently recruited are discussed and a revised and expanded working definition for venom is proposed.
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Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits
Cyril C. Curtain,Feda Ali,Irene Volitakis,Robert A. Cherny,Raymond S. Norton,Konrad Beyreuther,Colin J. Barrow,Colin L. Masters,Ashley I. Bush,Kevin Barnham +9 more
TL;DR: In this paper, it was shown that metal binding to Aβ generated an allosterically ordered membrane-penetrating oligomer linked by superoxide dismutase-like bridging histidine residues.
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A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides.
TL;DR: This structural motif appears to be one of the smallest stable globular domains found in proteins and is commonly used in toxins and inhibitors that act by blocking the function of larger protein receptors such as ion channels or proteases.
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The cystine knot structure of ion channel toxins and related polypeptides
TL;DR: The compact and robust nature of this motif makes it an excellent scaffold for the design and engineering of novel polypeptides with enhanced activity against existing targets, or with activity against novel targets.
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Organic Osmoregulatory Solutes in Cyanobacteria
TL;DR: The results suggest that the presence of certain major organic osmoregulatory solutes may be useful in the numerical taxonomy of cyanobacteria, and in the identification of some ionic characteristics of the environment of origin of each isolate.