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Douglas R. Houston

Researcher at University of Edinburgh

Publications -  50
Citations -  2158

Douglas R. Houston is an academic researcher from University of Edinburgh. The author has contributed to research in topics: Chitinase & Virtual screening. The author has an hindex of 23, co-authored 46 publications receiving 1873 citations. Previous affiliations of Douglas R. Houston include University of Dundee & McGill University.

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Oligopeptide signaling through TbGPR89 drives Trypanosome Quorum sensing

TL;DR: Peptidase-generated oligopeptide QS signals being received through TbGPR89 provides a mechanism for both trypanosome SIF production and reception, and generates a paracrine signal that accelerates stumpy formation in vivo.
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Specificity and Affinity of Natural Product Cyclopentapeptide Inhibitors against A. fumigatus, Human, and Bacterial Chitinases

TL;DR: The structures of these enzymes in complex with argifin and argadin, together with mutagenesis, fluorescence, and enzymology, reveal that subtle changes in the binding site dramatically affect affinity and selectivity and show that it may be possible to develop specific chitinase inhibitors based on the argifIn/argadin scaffolds.
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High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors: mimicry of carbohydrate substrate.

TL;DR: High-resolution crystal structures are described that reveal the details of the interactions of these cyclopeptides with a family 18 chitinase and provide a basis for structure-based design of potent chit inase inhibitors, accessible by standard peptide chemistry.
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Crystal structures of allosamidin derivatives in complex with human macrophage chitinase.

TL;DR: A high resolution structure of chitotriosidase, the human macrophage chitinase, in complex with allosamidin is presented and complexes of the allosamsidin derivatives demethylallosamIDin, methylallos amidin, and glucoallosAMidin B are described, together with their inhibitory properties.
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Structure of the D142N Mutant of the Family 18 Chitinase Chib from Serratia Marcescens and its Complex with Allosamidin

TL;DR: The reduced allosamidin affinity in the D142N mutant is not caused by structural changes but solely by the loss of electrostatic interactions with Asp142, confirming the importance of electrostatics.