Loading...
  • inhibitor
  • Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry. (abcam.com)
  • The MEK inhibitor PD 98059 also inhibited phosphorylation of NF-H, NF-M, and microtubule-associated protein (MAP) in primary rat hippocampal cells and caused a decrease in neurite outgrowth, suggesting that Erk1,2 may play an important role in neurite growth and branching. (jneurosci.org)
  • peptides
  • A comparative kinetic study of Erk2 and cdk5 phosphorylation of KSPXK and KSPXXXK peptides revealed that, in contrast to cdk5, which phosphorylated only the KSPXK peptide, Erk2 could phosphorylate both. (jneurosci.org)
  • modification
  • The limiting factor impeding rapid progress in deciphering the biological functions of protein O-GlcNAcylation has been the inability to easily identify exact residues of modification. (pnas.org)
  • Phosphorylation is the most heavily studied regulatory PTM, and proteomic approaches for global enrichment, detection, and characterization of this modification have provided the basis of our current knowledge of the complexity and redundancy in cell signaling networks ( 12 - 16 ). (pnas.org)
  • mammalian
  • The cross-talk with phosphorylation is particularly interesting, as there is only one conserved mammalian O -GlcNAc transferase (OGT), with its extensive tetratricopeptide repeat protein-protein interaction domain, that must cooperate and/or compete with hundreds of protein kinases that recognize their substrates individually ( 7 - 9 ). (pnas.org)
  • primarily
  • Glycoproteins are characterized by the presence of oligosaccharides linked to the peptide backbone primarily through N - or O -glycosidic bonds at asparagine or serine/threonine residues, respectively ( 11 ). (mcponline.org)
  • domain
  • These two iso forms of LMP2 only differ in that LMP2A contains an extra 119 residue N-terminal domain encoded in exon 1. (wikipedia.org)
  • western
  • One of the major reasons for this is the availability of excellent antibodies that recognize phosphorylated tyrosine residues in immunoprecipitation, as well as Western blotting experiments. (mcponline.org)