Genome Biology

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Protein prenyltransferases

Sebastian Maurer-Stroh*, Stefan Washietl and Frank Eisenhaber

Genome Biology 2003, 4:212 doi:10.1186/gb-2003-4-4-212

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BioMed Central: 4 citations

Research article   Open Access

Multiple domain insertions and losses in the evolution of the Rab prenylation complex

Rita Rasteiro, Jose B Pereira-Leal BMC Evolutionary Biology 2007, 7:140 (17 August 2007)

Methodology article   Open Access Highly Accessed

Farnesylation or geranylgeranylation? Efficient assays for testing protein prenylation in vitro and in vivo

Wolfgang Benetka, Manfred Koranda, Sebastian Maurer-Stroh, Fritz Pittner, Frank Eisenhaber BMC Biochemistry 2006, 7:6 (28 February 2006)

Software   Open Access

Refinement and prediction of protein prenylation motifs

Sebastian Maurer-Stroh, Frank Eisenhaber Genome Biology 2005, 6:R55 (27 May 2005)

Three prenylation motif predictors are presented that allow discrimination between proteins that are unique substrates of farnesyltransferase (FT) and those that can be alternatively processed by geranylgeranyltransferase I (GGT1).

Software   Open Access

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

Sebastian Maurer-Stroh, Masaki Gouda, Maria Novatchkova, Alexander Schleiffer, Georg Schneider, Fernanda L Sirota, Michael Wildpaner, Nobuhiro Hayashi, Frank Eisenhaber Genome Biology 2004, 5:R21 (13 February 2004)

MYRbase is a database of glycine myristoylation in eukaryotes. This study shows that the functional spectrum of myristoylated proteins has been underestimated and five membrane-attachment factors that occur frequently with myristoylation have been classified.