Phosphotransferase and substrate binding mechanism of the cAMP‐dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl…

By D. Bossemeyer, Richard A. Engh, V. Kinzel, H. Ponstingl, R. Huber. 1993

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1. Lars Rosenbaum
2. Georg Hinselmann
3. Andreas Jahn
4. Andreas Zell
5. J. Kuriyan
6. M. Huse
7. Z. Du
8. R. Roskoski

Citations in the corpus

• Interpreting linear support vector machine models with heat map molecule coloring (2011, background): “Compound C B is toxic because the red chlorobenzene substructure is not a detoxifying substructure. the binding pocket by hydrogen bonds to three protein residues: Glu121, Val123 and Thr183 [27,28].”
• The conformational plasticity of protein kinases. (2002, background): “…ylation of specific serine, threonine, or tyrosine residues that is primed and ready for phosphotransfer (Knighton is crucial to cellular growth and development, and this et al., 1991; Bossemeyer et al., 1993; Zheng et al., 1993). control relies on the proper regulation of protein kinases.”