J
John E. Hanson
Researcher at University of Puget Sound
Publications - 15
Citations - 1103
John E. Hanson is an academic researcher from University of Puget Sound. The author has contributed to research in topics: Dissociation constant & Sialic acid. The author has an hindex of 10, co-authored 15 publications receiving 1051 citations. Previous affiliations of John E. Hanson include University of California, Berkeley & Howard Hughes Medical Institute.
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Journal ArticleDOI
Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and x-ray crystallography
Nicholas K. Sauter,John E. Hanson,Gary D. Glick,Jerry H. Brown,Robert L. Crowther,Seong Joon Park,John J. Skehel,Don C. Wiley +7 more
TL;DR: X-ray diffraction studies yielded 3 A resolution crystal structures of hemagglutinin in complex with four of the synthetic analogs and with the naturally occurring cell-surface saccharide (alpha 2-3)sialyllactose, which could lead to the design of tight binding inhibitors of possible therapeutic value.
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Hemagglutinins from Two Influenza Virus Variants Bind to Sialic Acid Derivatives with Millimolar Dissociation Constants: A 500 MHz Proton Nuclear Magnetic Resonance Study
Nicholas K. Sauter,Mark D. Bednarski,Beth A. Wurzburg,John E. Hanson,George M. Whitesides,John J. Skehel,Don C. Wiley +6 more
TL;DR: Experiments with sialylated oligosaccharides confirm literature reports that mutations at amino acid 226 change the specificity of hemagglutinin for alpha( 2,6) and alpha(2,3) glycosidic linkages and suggest that sialic acid is the only component that contacts the protein.
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Potent inhibition of pepsin and penicillopepsin by phosphorus-containing peptide analogues
TL;DR: The substitution of a phosphonate ester moiety for the scissile peptide linkage in oligopeptide substrates of pepsin and penicillopepsin leads to potent inhibitors of these enzymes.
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Phosphonate Analogues of Carboxypeptidase A Substrates Are Potent Transition-State Analogue Inhibitors?
TL;DR: Transition-state analogy was shown for a series of 14 tri- and tetrapeptide derivatives containing the structure RCO-AlaP-(O)Ala [RCO-AP(O)A, AP indicates the phosphonic acid analogue of alanine], which supports a transition state for the enzymatic reaction that resembles the tetrahedral intermediate formed upon addition of water to the scissile carbonyl group.
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Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues.
TL;DR: The molecular structures of three phosphorus-based peptide inhibitors of aspartyl proteinases complexed with penicillopepsin are determined and a neutral status is assigned to Asp213 and a partially negatively charged status to AsP33 with reasonable confidence.