Structural Identification of Modified Amino Acids on the Interface between EPO and Its Receptor from EPO BRP, Human Recombinant Erythropoietin by LC/MS Analysis-Reference-Cited by-同舟云学术

Structural Identification of Modified Amino Acids on the Interface between EPO and Its Receptor from EPO BRP, Human Recombinant Erythropoietin by LC/MS Analysis

Published:2014-09-30 Issue:11 Volume:37 Page:819-826
ISSN:1016-8478
Container-title:Molecules and Cells
language:en
Short-container-title:

Author:

Song Kwang-Eun,Byeon Jaehee,Moon Dae-Bong,Kim Hyong-Ha,Choi Yoo-Joo,Suh Jung-Keun

Publisher

Korean Society for Molecular and Cellular Biology

Subject

Cell Biology,Molecular Biology,General Medicine

Link

http://ocean.kisti.re.kr/downfile/crosscheck/ksmcb/JAKO201401458923458.pdf

Reference13 articles.

1. Nonerythropoietic, tissue-protective peptides derived from the tertiary structure of erythropoietin

2. Quality of Original and Biosimilar Epoetin Products

3. Analysis of the Structure and Stability of Erythropoietin by pH and Temperature Changes using Various LC/MS

4. NMR structure of human erythropoietin and a comparison with its receptor bound conformation

5. Characterization of recombinant human erythropoietin produced in Chinese hamster ovary cells

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3. Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin;Analytical Chemistry;2020-06-24

4. Multi-Attribute Monitoring of Complex Erythropoetin Beta Glycosylation by GluC Liquid Chromatography–Mass Spectrometry Peptide Mapping;Analytical Chemistry;2020-05-19

5. Comprehensive Characterization ofN‐Glycosylation in Darbepoetin Alfa;Bulletin of the Korean Chemical Society;2019-08-30