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of 10
pro vyhledávání: '"Wolfgang Benetka"'
Autor:
Sebastian Maurer-Stroh, Manfred Koranda, Wolfgang Benetka, Georg Schneider, Fernanda L Sirota, Frank Eisenhaber
Publikováno v:
PLoS Computational Biology, Vol 3, Iss 4, p e66 (2007)
Three different prenyltransferases attach isoprenyl anchors to C-terminal motifs in substrate proteins. These lipid anchors serve for membrane attachment or protein-protein interactions in many pathways. Although well-tolerated selective prenyltransf
Externí odkaz:
https://doaj.org/article/4577f5c67d9a40e1bbc30971d1063474
Publikováno v:
Nuclear Medicine and Biology. :S121
Publikováno v:
Drug Testing and Analysis. 8:1131-1137
The two mouse monoclonal anti-erythropoietin (EPO) antibodies clone AE7A5 (generated by using a 26 amino acid N-terminal EPO-peptide) and 9G8A (developed by immunizing mice with full length human EPO) are both directed against linear epitopes at the
Publikováno v:
Drug testing and analysis. 8(11-12)
The two mouse monoclonal anti-erythropoietin (EPO) antibodies clone AE7A5 (generated by using a 26 amino acid N-terminal EPO-peptide) and 9G8A (developed by immunizing mice with full length human EPO) are both directed against linear epitopes at the
Autor:
Wai Heng Lua, Lai Ling Liew, Frank Eisenhaber, Manfred Koranda, Weimiao Yu, Hwee Kuan Lee, Wolfgang Benetka, Birgit Eisenhaber, Michaela Sammer, Sharmila Adhikari
Publikováno v:
Cell Cycle. 10:3897-3911
Lipid-modified transcription factors (TFs) are biomolecular oddities, since their reduced mobility and membrane attachment appear to contradict nuclear import required for their gene-regulatory function. NFAT5 isoform a (selected from an in silico sc
Publikováno v:
Monatshefte für Chemie - Chemical Monthly. 137:1241-1281
Since 1979, when prenylation has been first discovered as chemical oddity of a yeast mating factor, the two forms of this posttranslational modification of proteins (farnesylation and geranylgeranylation) have been found as wide spread among proteins
Autor:
Norbert Mehlmer, Michaela Sammer, Frank Eisenhaber, Jörg Betschinger, Jürgen A. Knoblich, Manfred Koranda, Wolfgang Benetka, Markus Teige, Ralph A. Neumüller, Sebastian Maurer-Stroh
Publikováno v:
Cell Cycle
ResearcherID
ResearcherID
Evolutionary conservation of N-terminal N-myristoylation within protein families indicates significant functional impact of this lipid posttranslational modification for function. In the MYRbase study (Maurer-Stroh et al., (2004) Genome Biology 5, R2
Publikováno v:
BMC Biochemistry, Vol 7, Iss 1, p 6 (2006)
BMC Biochemistry
BMC Biochemistry
Background Available in vitro and in vivo methods for verifying protein substrates for posttranslational modifications via farnesylation or geranylgeranylation (for example, autoradiography with 3H-labeled anchor precursors) are time consuming (weeks
Autor:
Wolfgang Benetka, Norbert Mehlmer, Sebastian Maurer-Stroh, Michaela Sammer, Manfred Koranda, Ralph Neumüller, Jörg Betschinger, Jürgen A. Knoblich, Markus Teige, Frank Eisenhaber
Publikováno v:
Cell Cycle. 8:508-509
Autor:
Frank Eisenhaber, Sebastian Maurer-Stroh, Georg Schneider, Manfred Koranda, Wolfgang Benetka, Fernanda L. Sirota
Publikováno v:
PLoS Computational Biology
PLoS computational biology, 3 (4
PLoS Computational Biology, Vol 3, Iss 4, p e66 (2007)
PLoS computational biology, 3 (4
PLoS Computational Biology, Vol 3, Iss 4, p e66 (2007)
Three different prenyltransferases attach isoprenyl anchors to C-terminal motifs in substrate proteins. These lipid anchors serve for membrane attachment or protein-protein interactions in many pathways. Although well-tolerated selective prenyltransf