Linked Life Data

20593476

Source:http://linkedlifedata.com/resource/pubmed/id/20593476

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-7-12
pubmed:abstractText
Eukaryotic cell surface proteins are often modified by a glycosylphosphatidylinositol (GPI) anchor. More than 200 of these post-translationally altered proteins are presently known, a prominent example being the prion protein (PrP). Although the significance of the GPI anchor is well recognized, efforts to study its function are hampered due to its complex chemical nature, which combines hydrophilic glycosyl chains with hydrophobic lipid moieties. Here we describe a general method for the synthesis of a GPI-anchored peptide containing an N-terminal Cys. This module can be employed for the production of proteins containing a natural GPI anchor using expressed protein ligation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2010 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
457-64
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Synthesis of a GPI anchor module suitable for protein post-translational modification.
pubmed:affiliation
Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, Dortmund 44227, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't