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Stanley A. Moore
Researcher at University of Saskatchewan
Publications - 33
Citations - 1504
Stanley A. Moore is an academic researcher from University of Saskatchewan. The author has contributed to research in topics: Protein structure & Peptide sequence. The author has an hindex of 16, co-authored 33 publications receiving 1342 citations. Previous affiliations of Stanley A. Moore include University of Alberta & University of British Columbia.
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Journal ArticleDOI
Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution.
TL;DR: Two lysine residues behind the N-lobe iron site of bLf offer new insights into the "dilysine trigger" mechanism proposed for iron release by transferrins, and several well-defined oligosaccharide units which demonstrate the structural factors that stabilise carbohydrate structure are demonstrated.
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Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release.
Ross T. A. MacGillivray,Stanley A. Moore,Jie Chen,Bryan F. Anderson,Heather M. Baker,Yaoguang Luo,Maria C. Bewley,Clyde A. Smith,Michael E. P. Murphy,Yili Wang,Anne B. Mason,Robert C. Woodworth,Gary D. Brayer,Edward N. Baker +13 more
TL;DR: The N-lobe of human serum transferrin (hTF/2N) has been expressed in baby hamster kidney cells and crystallized in both orthorhombic and tetragonal space groups and represents the highest-resolution transferrin structures determined to date.
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Sheep liver cytosolic aldehyde dehydrogenase: the structure reveals the basis for the retinal specificity of class 1 aldehyde dehydrogenases
Stanley A. Moore,Heather M. Baker,Treena J. Blythe,Kathryn E. Kitson,Trevor M. Kitson,Edward N. Baker +5 more
TL;DR: The disorder of Glu268 and the observation that NAD+ binds in two distinct modes indicate that flexibility is a key facet of the enzyme reaction mechanism.
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Getting out what you put in: Copper in mitochondria and its impacts on human disease.
TL;DR: The understanding of the maturation of mitochondrial copper enzymes, the roles of mitochondrial signals in regulating cellular copper content, the proposed mechanisms of copper transport into the organelle and the evolutionary origins of copper homeostasis pathways are detailed.
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Crystal and molecular structures of human progastricsin at 1.62 A resolution.
TL;DR: The structures of hPGC and pPGN indicate that aspartic proteinase zymogens keep themselves inactive at neutral pH by a very similar mechanism in human progastricsin and porcine pepsinogen.