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David J. Craik

Researcher at University of Queensland

Publications -  866
Citations -  43046

David J. Craik is an academic researcher from University of Queensland. The author has contributed to research in topics: Cyclotides & Cyclotide. The author has an hindex of 100, co-authored 866 publications receiving 38492 citations. Previous affiliations of David J. Craik include University of Washington & University of California, Los Angeles.

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Ribosomally synthesized and post-translationally modified peptide natural products: Overview and recommendations for a universal nomenclature

Paul G. Arnison, +65 more
TL;DR: This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products.
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The Future of Peptide‐based Drugs

TL;DR: The suite of currently used drugs can be divided into two categories - traditional'small molecule' drugs with typical molecular weights of 5000 Da that are not orally bioavailable and need to be delivered via injection as mentioned in this paper.
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Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif

TL;DR: The structural features of the two apparent subfamilies of the CCK peptides which may be significant for the likely defense related role of these peptides within plants are defined.
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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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Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?

TL;DR: The structural biology described herein for Abeta(1-40) suggests that the C-terminal two-thirds of the peptide is an alpha-helix in membrane-like environments, deprotonation of two acidic amino acids in the helix promotes a helix-coil conformational transition that precedes aggregation.