Toward Homogeneous Erythropoietin: Fine Tuning of the C-Terminal Acyl Donor in the Chemical Synthesis of the Cys29−Gly77 Glycopeptide Domain
Author:
Affiliation:
1. Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, 1275 York Avenue, New York, New York 10065, and Department of Chemistry, Columbia University, Havemeyer Hall, 3000 Broadway, New York, New York 10027
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja808705v
Reference22 articles.
1. Toward Homogeneous Erythropoietin: Non-NCL-Based Chemical Synthesis of the Gln78−Arg166 Glycopeptide Domain
2. Promising agents at the interface of biology and oncology derived through chemical synthesis
3. Development of Efficient Methods for Accomplishing Cysteine-Free Peptide and Glycopeptide Coupling
4. Studies Related to the Relative Thermodynamic Stability of C-Terminal Peptidyl Esters of O-Hydroxy Thiophenol: Emergence of a Doable Strategy for Non-Cysteine Ligation Applicable to the Chemical Synthesis of Glycopeptides
5. A route to cyclic peptides and glycopeptides by native chemical ligation using in situ derived thioesters
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