Search Results - "BOSSEMEYER, D"
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Analysis of Protein Phosphorylation by a Combination of Elastase Digestion and Neutral Loss Tandem Mass Spectrometry
Published in Analytical chemistry (Washington) (15-01-2001)“…Loss of phosphoric acid is the most effective fragmentation reaction of pSer- and pThr-containing phosphopeptides of small size (up to 10−15 residues) in…”
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Analysis of isoaspartate in peptides by electrospray tandem mass spectrometry
Published in Protein science (01-11-2000)“…In view of the significance of Asn deamidation and Asp isomerization to isoAsp at certain sites for protein aging and turnover, it was desirable to challenge…”
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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
Published in Biochemistry (Easton) (09-01-2001)“…A number of isoenzymes of the catalytic subunit of cAMP-dependent protein kinase arise through posttranslational modifications of the enzyme outside the…”
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The amino terminus of PKA catalytic subunit— A site for introduction of posttranslational heterogeneities by deamidation: d-Asp2 and d-isoAsp2 containing isozymes
Published in Protein science (01-11-2000)“…Conserved deamidation of PKA catalytic subunit isozymes Cα and Cβ—more than 25% at Asn2 in vivo in both cases—has been shown to yield Asp2- and…”
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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
Published in Protein science (01-02-1998)“…The N‐terminal sequence myr‐Gly‐Asn is conserved among the myristoylated cAPK (protein kinase A) catalytic subunit isozymes C, Cβ, and O. By capillary LC‐MS…”
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Specific cesium transport via the Escherichia coli Kup (TrkD) K+ uptake system
Published in Journal of Bacteriology (01-04-1989)“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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K+-transport Protein TrkA of Escherichia coli Is a Peripheral Membrane Protein That Requires other trk Gene Products for Attachment to the Cytoplasmic Membrane
Published in The Journal of biological chemistry (05-10-1989)“…The TrkA protein, which is essential for the activity of the constitutive Trk K+-uptake system of Escherichia coli, is a peripheral membrane protein. The…”
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Protein Kinase A in Complex with Rho-Kinase Inhibitors Y-27632, Fasudil, and H-1152P: Structural Basis of Selectivity
Published in Structure (London) (01-12-2003)“…Protein kinases require strict inactivation to prevent spurious cellular signaling; overactivity can cause cancer or other diseases and necessitates selective…”
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Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity
Published in The Journal of biological chemistry (18-10-1996)“…The discovery of several hundred different protein kinases involved in highly diverse cellular signaling pathways is in stark contrast to the much smaller…”
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Physical mapping of the K+ transport trkA gene of Escherichia coli and overproduction of the TrkA protein
Published in Journal of Bacteriology (01-07-1987)“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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12
The glycine-rich sequence of protein kinases: a multifunctional element
Published in Trends in biochemical sciences (Amsterdam. Regular ed.) (01-05-1994)“…Evolution favours the use of glycine-rich loops for nucleotide binding in proteins. In the large family of protein kinases, the catalytic domain of which has…”
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13
Structural aspects of protein kinase control—role of conformational flexibility
Published in Pharmacology & therapeutics (Oxford) (01-02-2002)“…Protein kinases catalyze the phosphotransfer reaction fundamental to most signaling and regulatory processes in the eukaryotic cell. Absolute control of…”
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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)
Published in The EMBO journal (01-03-1993)“…The crystal structure of the porcine heart catalytic subunit of cAMP‐dependent protein kinase in a ternary complex with the MgATP analogue MnAMP‐PNP and a…”
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Protein kinases — structure and function
Published in FEBS Letters (01-08-1995)“…The solution of crystal structures from half a dozen protein kinases during the last four years in different laboratories has deepened our understanding of the…”
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Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential
Published in Structure (London) (15-12-1997)“…Background: Staurosporine inhibits most protein kinases at low nanomolar concentrations. As most tyrosine kinases, along with many serine/threonine kinases,…”
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Design and Crystal Structures of Protein Kinase B-Selective Inhibitors in Complex with Protein Kinase A and Mutants
Published in Journal of medicinal chemistry (13-01-2005)“…Protein kinase B (PKB)-selective inhibitors were designed, synthesized, and cocrystallized using the AGC kinase family protein kinase A (PKA, often called…”
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Phosphorylation of protein kinase C delta (PKC delta ) at threonine 505 is not a prerequisite for enzymatic activity: Expression of rat PKC delta and an alanine 505 mutant in bacteria in a functional form
Published in The Journal of biological chemistry (07-03-1997)“…A structural feature shared by many protein kinases is the requirement for phosphorylation of threonine or tyrosine in the so-called activation loop for full…”
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Mutants of Protein Kinase A that Mimic the ATP-binding Site of Protein Kinase B (AKT)
Published in Journal of molecular biology (20-06-2003)“…The mutation of well behaved enzymes in order to simulate less manageable cognates is the obvious approach to study specific features of the recalcitrant…”
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The Protein Kinase C Inhibitor Bisindolyl Maleimide 2 Binds with Reversed Orientations to Different Conformations of Protein Kinase A
Published in The Journal of biological chemistry (28-05-2004)“…As the key mediators of eukaryotic signal transduction, the protein kinases often cause disease, and in particular cancer, when disregulated. Appropriately…”
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