MYRbase: analysis of genome-wide glycine myristoylation enlarges the functional spectrum of eukaryotic myristoylated proteins View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2004-02

AUTHORS

Sebastian Maurer-Stroh, Masaki Gouda, Maria Novatchkova, Alexander Schleiffer, Georg Schneider, Fernanda L Sirota, Michael Wildpaner, Nobuhiro Hayashi, Frank Eisenhaber

ABSTRACT

We evaluated the evolutionary conservation of glycine myristoylation within eukaryotic sequences. Our large-scale cross-genome analyses, available as MYRbase, show that the functional spectrum of myristoylated proteins is currently largely underestimated. We give experimental evidence for in vitro myristoylation of selected predictions. Furthermore, we classify five membrane-attachment factors that occur most frequently in combination with, or even replacing, myristoyl anchors, as some protein family examples show. More... »

PAGES

r21

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/gb-2004-5-3-r21

DOI

http://dx.doi.org/10.1186/gb-2004-5-3-r21

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1024144794

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15003124


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