Bossemeyer D - Search Results

1

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

Tholey A, Pipkorn R, Bossemeyer D, Kinzel V, Reed J. Tholey A, et al. Among authors: bossemeyer d. Biochemistry. 2001 Jan 9;40(1):225-31. doi: 10.1021/bi0021277. Biochemistry. 2001. PMID: 11141074

2

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

Breitenlechner C, Engh RA, Huber R, Kinzel V, Bossemeyer D, Gassel M. Breitenlechner C, et al. Among authors: bossemeyer d. Biochemistry. 2004 Jun 22;43(24):7743-9. doi: 10.1021/bi0362525. Biochemistry. 2004. PMID: 15196017

3

Analysis of isoaspartate in peptides by electrospray tandem mass spectrometry.

Lehmann WD, Schlosser A, Erben G, Pipkorn R, Bossemeyer D, Kinzel V. Lehmann WD, et al. Among authors: bossemeyer d. Protein Sci. 2000 Nov;9(11):2260-8. doi: 10.1110/ps.9.11.2260. Protein Sci. 2000. PMID: 11152137 Free PMC article.

4

The amino terminus of PKA catalytic subunit--a site for introduction of posttranslational heterogeneities by deamidation: D-Asp2 and D-isoAsp2 containing isozymes.

Kinzel V, König N, Pipkorn R, Bossemeyer D, Lehmann WD. Kinzel V, et al. Among authors: bossemeyer d. Protein Sci. 2000 Nov;9(11):2269-77. doi: 10.1110/ps.9.11.2269. Protein Sci. 2000. PMID: 11152138 Free PMC article.

L-Succinimide is prone to racemization to D-succinimide, which may hydrolyze to D-isoAsp- and D-Asp-containing diastereomers with, respectively, no and poor substrate character for PIMT. ...The results demonstrate the occurrence of D-isoAsp- and D …

L-Succinimide is prone to racemization to D-succinimide, which may hydrolyze to D-isoAsp- and D-Asp-containing diastere …

5

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

Girod A, Kinzel V, Bossemeyer D. Girod A, et al. Among authors: bossemeyer d. FEBS Lett. 1996 Aug 5;391(1-2):121-5. doi: 10.1016/0014-5793(96)00717-x. FEBS Lett. 1996. PMID: 8706898 Free article.

6

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.

Jedrzejewski PT, Girod A, Tholey A, König N, Thullner S, Kinzel V, Bossemeyer D. Jedrzejewski PT, et al. Among authors: bossemeyer d. Protein Sci. 1998 Feb;7(2):457-69. doi: 10.1002/pro.5560070227. Protein Sci. 1998. PMID: 9521123 Free PMC article.

7

Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation.

Pepperkok R, Hotz-Wagenblatt A, König N, Girod A, Bossemeyer D, Kinzel V. Pepperkok R, et al. Among authors: bossemeyer d. J Cell Biol. 2000 Feb 21;148(4):715-26. doi: 10.1083/jcb.148.4.715. J Cell Biol. 2000. PMID: 10684253 Free PMC article.

Tholey, N. Konig, S. Thullner, V. Kinzel, and D. Bossemeyer. 1998. Protein Sci. 7:457-469). Because of the increase of electronegativity by generation of Asp2, it is reminiscent of a myristoyl-electrostatic switch. ...

Tholey, N. Konig, S. Thullner, V. Kinzel, and D. Bossemeyer. 1998. Protein Sci. 7:457-469). Because of the increase of electro …

8

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

Thullner S, Gesellchen F, Wiemann S, Pyerin W, Kinzel V, Bossemeyer D. Thullner S, et al. Among authors: bossemeyer d. Biochem J. 2000 Oct 1;351(Pt 1):123-32. doi: 10.1042/0264-6021:3510123. Biochem J. 2000. PMID: 10998354 Free PMC article.

9

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

Schlosser A, Pipkorn R, Bossemeyer D, Lehmann WD. Schlosser A, et al. Among authors: bossemeyer d. Anal Chem. 2001 Jan 15;73(2):170-6. doi: 10.1021/ac000826j. Anal Chem. 2001. PMID: 11199962

10

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.

Engh RA, Girod A, Kinzel V, Huber R, Bossemeyer D. Engh RA, et al. Among authors: bossemeyer d. J Biol Chem. 1996 Oct 18;271(42):26157-64. doi: 10.1074/jbc.271.42.26157. J Biol Chem. 1996. PMID: 8824261 Free article.

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