Matches in Nanopublications for { ?s ?p "Phosphopeptide analysis of Elk-1 indicated that phosphorylation at Ser383 and Ser389 (peptides 1?6), which are homologous to Ser381 and Ser387 in Sap-1a, as well as within the unidentified peptides f and g was much less efficiently catalyzed by p38 MAPK than by ERK-1 in vitro (compare with peptides a?d in Figure 6D)." ?g. }
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- _5 value "Phosphopeptide analysis of Elk-1 indicated that phosphorylation at Ser383 and Ser389 (peptides 1?6), which are homologous to Ser381 and Ser387 in Sap-1a, as well as within the unidentified peptides f and g was much less efficiently catalyzed by p38 MAPK than by ERK-1 in vitro (compare with peptides a?d in Figure 6D)." provenance.
- _5 value "Phosphopeptide analysis of Elk-1 indicated that phosphorylation at Ser383 and Ser389 (peptides 1?6), which are homologous to Ser381 and Ser387 in Sap-1a, as well as within the unidentified peptides f and g was much less efficiently catalyzed by p38 MAPK than by ERK-1 in vitro (compare with peptides a?d in Figure 6D)." provenance.
- _5 value "Phosphopeptide analysis of Elk-1 indicated that phosphorylation at Ser383 and Ser389 (peptides 1?6), which are homologous to Ser381 and Ser387 in Sap-1a, as well as within the unidentified peptides f and g was much less efficiently catalyzed by p38 MAPK than by ERK-1 in vitro (compare with peptides a?d in Figure 6D)." provenance.
- _5 value "Phosphopeptide analysis of Elk-1 indicated that phosphorylation at Ser383 and Ser389 (peptides 1?6), which are homologous to Ser381 and Ser387 in Sap-1a, as well as within the unidentified peptides f and g was much less efficiently catalyzed by p38 MAPK than by ERK-1 in vitro (compare with peptides a?d in Figure 6D)." provenance.