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John Michael Beals

Researcher at Eli Lilly and Company

Publications -  51
Citations -  2366

John Michael Beals is an academic researcher from Eli Lilly and Company. The author has contributed to research in topics: Insulin & Insulin lispro. The author has an hindex of 19, co-authored 46 publications receiving 2144 citations.

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Crystal structure of the obese protein leptin-E100.

TL;DR: The crystal structure at 2.4 Å resolution of a human mutant OB protein (leptin-E100) is reported that has comparable biological activity to wild type but which crystallizes more readily and reveals a four-helix bundle similar to that of the long-chain helical cytokine family.
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In Vivo Deamidation Characterization of Monoclonal Antibody by LC/MS/MS

TL;DR: The deamidation half-life of amino acid residue Asn55 in vivo and the ratio of the deamidated derivatives, i.e., isoAsp55 and Asp55 are determined, which is rapid and sensitive with low-nanogram quantities of protein detected in the biological matrix.
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Role of C-terminal B-chain residues in insulin assembly: the structure of hexameric LysB28ProB29-human insulin.

TL;DR: It is hypothesized that the diffusion of the phenolic ligands from the site of injection results in the dissociation of hexamers directly to monomers, thereby maintaining the rapid time-action of the monomeric analog in spite of the hexameric conformation in therapeutic formulations.
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Rational Design of a Fibroblast Growth Factor 21-Based Clinical Candidate, LY2405319

TL;DR: LY2405319 exhibited all the biopharmaceutical and biological properties required for initiation of a clinical program designed to test the hypothesis that administration of exogenous FGF21 would result in effects on disease-related metabolic parameters in humans.
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Glycosylation of erythropoietin affects receptor binding kinetics: role of electrostatic interactions.

TL;DR: The effect of electrostatic forces on EPO binding was studied by measuring binding kinetics in varying NaCl concentrations and it was determined that sialic acid decreased the association rate constant (k(on)) about 3-fold, suggesting that long-range electrostatic interactions are primarily important in determining the rate of association between EPO and EPOR.