Nonspecific shielding of unfavorable electrostatic intramolecular interactions in the erythropoietin native-state increase conformational stability and limit non-native aggregation-Reference-Cited by-同舟云学术

Nonspecific shielding of unfavorable electrostatic intramolecular interactions in the erythropoietin native-state increase conformational stability and limit non-native aggregation

Published:2015-04-11 Issue:5 Volume:24 Page:803-811
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Banks Douglas D.¹

Affiliation:

1. Department of Process and Product Development; Amgen Inc.; Seattle Washington 98119-3105

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2651/fullpdf

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4. Aggregation of granulocyte colony stimulating factor under physiological conditions: characterization and thermodynamic inhibition;Krishnan;Biochemistry,2002

5. Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state;Raso;Protein Sci,2005

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1. Science and art of protein formulation development;International Journal of Pharmaceutics;2019-09

2. Surface patches on recombinant erythropoietin predict protein solubility: engineering proteins to minimise aggregation;BMC Biotechnology;2019-05-09

3. Optimization of high-concentration endostatin formulation: Harmonization of excipients’ contributions on colloidal and conformational stabilities;International Journal of Pharmaceutics;2017-09