Probing the frontiers of glycoprotein synthesis: The fully elaborated β-subunit of the human follicle-stimulating hormone Journal Article
| Authors: | Nagorny, P.; Sane, N.; Fasching, B.; Aussedat, B.; Danishefsky, S. J. |
| Article Title: | Probing the frontiers of glycoprotein synthesis: The fully elaborated β-subunit of the human follicle-stimulating hormone |
| Abstract: | Ambitious undertaking: The β-subunit of the human follicle-stimulating hormone (hFSH) displaying a N-linked consensus sequence oligosaccharide at each of the two wild-type sites was synthesized. The glycoprotein has been designed with acetamidomethyl protected cysteine residues, anticipating folding and association with the α-subunit. This represents the largest realistically glycosylated homogeneous glycoprotein obtained by using strictly chemical methods. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
| Keywords: | chemistry; glycosylation; wild types; polysaccharide; amino acids; polysaccharides; glycoproteins; synthesis; glycopeptide; glycopeptides; cysteine; n-linked; native chemical ligation; follicle stimulating hormone; glycosylated; solid phase synthesis; consensus sequence; follicle-stimulating hormone; solid-phase peptide synthesis; chemical method; cysteine residues; follitropin beta subunit; follicle stimulating hormone, beta subunit; solid-phase synthesis techniques |
| Journal Title: | Angewandte Chemie - International Edition |
| Volume: | 51 |
| Issue: | 4 |
| ISSN: | 1433-7851 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2012-01-23 |
| Start Page: | 975 |
| End Page: | 979 |
| Language: | English |
| DOI: | 10.1002/anie.201107482 |
| PROVIDER: | scopus |
| PMCID: | PMC3285374 |
| PUBMED: | 22162182 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 1 March 2012" - "CODEN: ACIEA" - "Source: Scopus" |
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8Nagorny -
3
Fasching -
17
Aussedat -
539Danishefsky -
2
Sane
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