Dirk Bossemeyer

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 imidodiphosphate and inhibitor peptide PKI(5-24).

Dirk Bossemeyer, Richard A. Engh, V. Kinzel et al. · The EMBO Journal · 1993 · 396 citations · Full text

Cardiac Muscle, Cardiomyopathy, Protein Function +9

Crystal Structures of Catalytic Subunit of cAMP-dependent Protein Kinase in Complex with Isoquinolinesulfonyl Protein Kinase Inhibitors H7, H8, and H89

Richard A. Engh, Andreas Girod, V. Kinzel et al. · Journal of Biological Chemistry · 1996 · 259 citations · Full text

Biochemistry, Natural Sciences, Protein X-ray Crystallography +7

Analysis of Protein Phosphorylation by a Combination of Elastase Digestion and Neutral Loss Tandem Mass Spectrometry

Andreas Schlösser, Ruediger Pipkorn, Dirk Bossemeyer et al. · Analytical Chemistry · 2000 · 177 citations

Protein Chemistry, Phosphoric Acid, Elastase Digestion +14

Protein Kinase A in Complex with Rho-Kinase Inhibitors Y-27632, Fasudil, and H-1152P

C.B. Breitenlechner, M. Gaßel, Hiroyoshi Hidaka et al. · Structure · 2003 · 158 citations · Full text

Molecular Pharmacology, Protein Kinase A, Signal Transduction +10

Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential

Lars Prade, Richard A. Engh, Andreas Girod et al. · Structure · 1997 · 148 citations · Full text

Protein Function, Signal Transduction, Biochemistry +12