Robert A. Reed
Boston University
5 Papers
131 Citations
Robert A. Reed is an academic researcher from Boston University. The author has contributed to research in topics: Cholera toxin & Protein subunit. The author has an hindex of 4, co-authored 5 publications.
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Papers
The 2.4 Å Crystal Structure of Cholera Toxin B Subunit Pentamer: Choleragenoid
R. Zhang,Mary L. Westbrook,Edwin M. Westbrook,Edwin M. Westbrook,David Scott,Zbyszek Otwinowski,P R Maulik,Robert A. Reed,G. Graham Shipley,G. Graham Shipley +9 more
TL;DR: The structure of the B subunits, and their pentameric arrangement, closely resembles that reported for the intact holotoxin, choleragen, the heat-labile enterotoxin from Escherichia coli, and for a Choleragenoid-GM1 pentasaccharide complex.
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Interaction of cholera toxin with ganglioside GM1 receptors in supported lipid monolayers.
TL;DR: In separate studies, GM1-containing monolayers transferred to electron microscope grids were incubated with solutions containing unlabeled cholera toxin, followed by negative staining with uranyl acetate, which indicated a doughnut-shaped molecule with a central aqueous channel.
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Structure and metastability of N-lignocerylgalactosylsphingosine (cerebroside) bilayers.
Robert A. Reed,G. Graham Shipley +1 more
TL;DR: Differential scanning calorimetry and X-ray diffraction have been used to study hydrated N-lignocerylgalactosylsphingosine (NLGS) bilayers and provide clear evidence of conversions between metastable and stable forms.
50
Crystallization and preliminary x-ray diffraction study of cholera toxin B-subunit.
TL;DR: Diffraction quality crystals of cholera toxin B-subunit have been obtained at room temperature by vapor diffusion with polyethylene glycol in the presence of the nonionic detergent beta-octyl glucoside and can be used to collect three-dimensional crystallographic data.
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Crystallization and preliminary x-ray diffraction study of synthetic apolipoprotein E fragment (residues 129-169).
TL;DR: Precession photographs show that crystals diffract beyond 2.7-A resolution and are stable in the x-ray beam at room temperature for at least 200 h; thus, they can be used to collect three-dimensional data for a detailed crystallographic analysis.
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