D. Bossemeyer

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Influence of myristoylation, phosphorylation, and deamidation on the structural behavior of the N-terminus of the catalytic subunit of cAMP-dependent protein kinase.

A. Tholey, R. Pipkorn, D. Bossemeyer, 2001, Biochemistry.

Structural aspects of protein kinase control-role of conformational flexibility.

R. Engh, D. Bossemeyer, Richard A Engh, 2002, Pharmacology & therapeutics.

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

R. Huber, R. Engh, D. Bossemeyer, 1996, The Journal of Biological Chemistry.

K+-transport protein TrkA of Escherichia coli is a peripheral membrane protein that requires other trk gene products for attachment to the cytoplasmic membrane.

D. Bossemeyer, I. Booth, E. Bakker, 1989, The Journal of biological chemistry.

Protein kinase A in complex with Rho-kinase inhibitors Y-27632, Fasudil, and H-1152P: structural basis of selectivity.

R. Huber, H. Hidaka, R. Engh, 2003, Structure.

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).

R. Huber, R. Engh, D. Bossemeyer, 1993, The EMBO journal.

Specific cesium transport via the Escherichia coli Kup (TrkD) K+ uptake system

D. Bossemeyer, E. Bakker, A. Schlösser, 1989, Journal of bacteriology.

Phosphorylation of protein kinase Cdelta (PKCdelta) at threonine 505 is not a prerequisite for enzymatic activity. Expression of rat PKCdelta and an alanine 505 mutant in bacteria in a functional form.

F. Marks, D. Bossemeyer, A. Girod, 1997, The Journal of biological chemistry.

Analysis of protein phosphorylation by a combination of elastase digestion and neutral loss tandem mass spectrometry.

W. Lehmann, R. Pipkorn, D. Bossemeyer, 2001, Analytical chemistry.

Cell surface protein kinases and extracellular phosphorylation

D. Bossemeyer, V. Kinzel, D. Kübler, 2003 .

Analysis of isoaspartate in peptides by electrospray tandem mass spectrometry

W. Lehmann, R. Pipkorn, D. Bossemeyer, 2000, Protein science : a publication of the Protein Society.

Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT).

R. Huber, R. Engh, D. Bossemeyer, 2003, Journal of molecular biology.

Physical mapping of the K+ transport trkA gene of Escherichia coli and overproduction of the TrkA protein

D. Bossemeyer, E. Bakker, A. Hamann, 1987, Journal of bacteriology.

A conserved deamidation site at asn 2 in the catalytic subunit of mammalian cAMP‐dependent protein kinase detected by capillary LC‐MS and tandem mass spectrometry

A. Tholey, D. Bossemeyer, V. Kinzel, 1998, Protein science : a publication of the Protein Society.

Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants.

R. Huber, R. Engh, D. Bossemeyer, 2005, Journal of medicinal chemistry.

Diversity of bisubstrate binding modes of adenosine analogue-oligoarginine conjugates in protein kinase a and implications for protein substrate interactions.

R. Engh, D. Bossemeyer, E. Enkvist, 2010, Journal of molecular biology.

Structural analysis of ARC-type inhibitor (ARC-1034) binding to protein kinase A catalytic subunit and rational design of bisubstrate analogue inhibitors of basophilic protein kinases.

D. Bossemeyer, E. Enkvist, A. Uri, 2009, Journal of medicinal chemistry.

Intracellular Distribution of Mammalian Protein Kinase a Catalytic Subunit Altered by Conserved Asn2 Deamidation

R. Pepperkok, A. Hotz-Wagenblatt, D. Bossemeyer, 2000, The Journal of cell biology.

The protein kinase activity modulation sites: mechanisms for cellular regulation - targets for therapeutic intervention.

R. Engh, D. Bossemeyer, 2001, Advances in enzyme regulation.

Inhibitors of PKA and Related Protein Kinases

R. Engh, D. Bossemeyer, M. Gassel, 2005 .

The Protein Kinase C Inhibitor Bisindolyl Maleimide 2 Binds with Reversed Orientations to Different Conformations of Protein Kinase A*

Robert Huber, Norbert König, R. Huber, 2004, Journal of Biological Chemistry.

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

R. Huber, R. Engh, D. Bossemeyer, 1997, Structure.

Phosphorylation of Protein Kinase Cδ (PKCδ) at Threonine 505 Is Not a Prerequisite for Enzymatic Activity

F. Marks, D. Bossemeyer, A. Girod, 1997, The Journal of Biological Chemistry.

In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild‐type enzyme, evidence for intermolecular cotranslational phosphorylation

D. Bossemeyer, V. Kinzel, A. Girod, 1996, FEBS letters.

Protein kinases — structure and function

D. Bossemeyer, Dirk Bossemeyer, 1995, FEBS letters.

Structural Analysis of Protein Kinase A Mutants with Rho-kinase Inhibitor Specificity*

Stefan Bonn, W. Lehmann, R. Engh, 2006, Journal of Biological Chemistry.

Structural insights into AGC kinase inhibition.

R. Engh, D. Bossemeyer, M. Gassel, 2004, Oncology research.

NAD+ binding to the Escherichia coli K+‐uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport

D. Bossemeyer, E. Schneider, A. Schlosser, 1993, Molecular microbiology.

The protein kinase A catalytic subunit Cbeta2: molecular characterization and distribution of the splice variant.

S. Wiemann, D. Bossemeyer, V. Kinzel, 2000, The Biochemical journal.

The glycine-rich sequence of protein kinases: a multifunctional element.

D. Bossemeyer, D Bossemeyer, 1994, Trends in biochemical sciences.

The amino terminus of PKA catalytic subunit—A site for introduction of posttranslation heterogeneities by deamidation: D‐Asp2 and D‐isoAsp2 containing isozymes

W. Lehmann, R. Pipkorn, D. Bossemeyer, 2000, Protein science : a publication of the Protein Society.

Analysis of autophosphorylation sites in the recombinant catalytic subunit alpha of cAMP-dependent kinase by nano-UPLC–ESI–MS/MS

W. Lehmann, D. Bossemeyer, D. Kübler, 2009, Analytical and bioanalytical chemistry.

Mutants of protein kinase A that mimic the ATP-binding site of Aurora kinase.

R. Engh, D. Bossemeyer, Richard A Engh, 2011, The Biochemical journal.

Uncoupling of bait‐protein expression from the prey protein environment adds versatility for cell and tissue interaction proteomics and reveals a complex of CARP‐1 and the PKA Cβ1 subunit

W. Lehmann, D. Bossemeyer, C. Hung, 2010, Proteomics.

Crystallography for protein kinase drug design: PKA and SRC case studies.

R. Engh, D. Bossemeyer, C. Breitenlechner, 2005, Biochimica et biophysica acta.

The typically disordered N-terminus of PKA can fold as a helix and project the myristoylation site into solution.

R. Huber, R. Engh, D. Bossemeyer, 2004, Biochemistry.

Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy.

R. Huber, T. Holak, R. Engh, 2002, Biochemistry.

Identification of protein phosphorylation sites by combination of elastase digestion, immobilized metal affinity chromatography, and quadrupole‐time of flight tandem mass spectrometry

W. Lehmann, I. Grummt, D. Bossemeyer, 2002, Proteomics.

Inhibitors of Protein Kinases and Protein Phosphates Contributors

L. Meijer, D. Fabbro, M. Yacoub, 2005 .

Specific CesiumTransport viatheEscherichia coli Kup(TrkD) K+ UptakeSystem

D. Bossemeyer, A. Schlosser, 1989 .

Uncoupling of bait‐protein expression from the prey protein environment adds versatility for cell and tissue interaction proteomics and reveals a complex of CARP‐1 and the PKA Cβ1 subunit

W. Lehmann, D. Bossemeyer, C. Hung, 2010, Proteomics.