dc.contributor.author |
Lutteroth, Katherine |
en |
dc.contributor.author |
Williams, Geoffrey |
en |
dc.contributor.author |
Cooper, Garth |
en |
dc.contributor.author |
Brimble, Margaret |
en |
dc.coverage.spatial |
England |
en |
dc.date.accessioned |
2016-01-21T22:06:50Z |
en |
dc.date.issued |
2012-02 |
en |
dc.identifier.citation |
Organic and Biomolecular Chemistry, 2012, 10 (6), pp. 1137 - 1144 |
en |
dc.identifier.issn |
1477-0520 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/28073 |
en |
dc.description.abstract |
The synthesis of naturally occurring glycosylated (2S,5R)-hydroxylysine still remains a challenge. This perspective highlights the importance of this post-translationally modified amino acid residue in the observed bioactivity of collagen and related collagen-like proteins such as adiponectin, an important target for the treatment of type II diabetes. Strategies employed to date for the syntheses of (2S,5R)-hydroxylysine and the methods to effect glycosylation of this modified amino acid are also summarized herein. |
en |
dc.description.uri |
http://pubs.rsc.org/en/Content/ArticleLanding/2012/OB/c1ob06394d#!divAbstract |
en |
dc.language |
eng |
en |
dc.publisher |
Royal Society of Chemistry |
en |
dc.relation.ispartofseries |
Organic and Biomolecular Chemistry |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1477-0520/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Adiponectin |
en |
dc.subject |
Glycosylation |
en |
dc.subject |
Hydroxylysine |
en |
dc.subject |
Molecular Conformation |
en |
dc.subject |
Stereoisomerism |
en |
dc.title |
Synthesis of glycosylated 5-hydroxylysine, an important amino acid present in collagen-like proteins such as adiponectin |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1039/c1ob06394d |
en |
pubs.issue |
6 |
en |
pubs.begin-page |
1137 |
en |
pubs.volume |
10 |
en |
dc.description.version |
AM - Accepted Manuscript |
en |
dc.rights.holder |
Copyright:
Royal Society of Chemistry |
en |
dc.identifier.pmid |
22218394 |
en |
pubs.author-url |
http://pubs.rsc.org/en/content/articlepdf/2012/ob/c1ob06394d |
en |
pubs.end-page |
1144 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/OpenAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
267522 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Chemistry |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1477-0539 |
en |
pubs.record-created-at-source-date |
2012-12-17 |
en |
pubs.dimensions-id |
22218394 |
en |