N-Glycans Stabilize Human Erythropoietin through Hydrophobic Interactions with the Hydrophobic Protein Surface: Studies by Surface Plasmon Resonance Analysis
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/131/4/511/2789752/131-4-511.pdf
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1. BSA- and Elastin-Coated GO, but Not Collagen-Coated GO, Enhance the Biological Performance of Alginate Hydrogels;Pharmaceutics;2020-06-11
2. Oligomannosidic glycans at Asn-110 are essential for secretion of human diamine oxidase;Journal of Biological Chemistry;2018-01
3. Effects of localized interactions and surface properties on stability of protein-based therapeutics;Journal of Pharmacy and Pharmacology;2016-11-10
4. Probing protease sensitivity of recombinant human erythropoietin reveals α3-α4 inter-helical loop as a stability determinant;Proteins: Structure, Function, and Bioinformatics;2015-09-08
5. Nonspecific shielding of unfavorable electrostatic intramolecular interactions in the erythropoietin native-state increase conformational stability and limit non-native aggregation;Protein Science;2015-04-11
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