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Concanamycin A, the Specific Inhibitor of V-ATPases, Binds to the Vo Subunit c*
- M. Huss, G. Ingenhorst, H. Wieczorek
- Chemistry, BiologyJournal of Biological Chemistry
- 25 October 2002
Binding of J-concanolide A to subunit c was prevented in a concentration-dependent manner by concanamycin A, indicating that labeling was specific, and binding was also prevented by the plecomacrolides bafilomycin A1 and B1, respectively.
The novel isoxazoline ectoparasiticide fluralaner: selective inhibition of arthropod γ-aminobutyric acid- and L-glutamate-gated chloride channels and insecticidal/acaricidal activity.
Mutants of protein kinase A that mimic the ATP-binding site of protein kinase B (AKT).
Expression of the recE gene during induction of the SOS response in Bacillus subtilis recombination‐deficient strains
A transcriptional fusion of the recE gene to a reporter gene has been constructed and de‐repression of recE seems to be independent of the ATP‐dependent DNase activity of the exonuclease V enzyme.
The KdpF Subunit Is Part of the K+-translocating Kdp Complex of Escherichia coli and Is Responsible for Stabilization of the Complex in Vitro *
- M. Gassel, Thomas Möllenkamp, W. Puppe, K. Altendorf
- BiologyJournal of Biological Chemistry
- 31 December 1999
Upon expression of this operon in minicells, a so far unrecognized small hydrophobic polypeptide, KdpF, could be identified on high resolution SDS-polyacrylamide gels and proved to be indispensable for a functional enzyme complex in vitro.
Protein kinase A in complex with Rho-kinase inhibitors Y-27632, Fasudil, and H-1152P: structural basis of selectivity.
Design and crystal structures of protein kinase B-selective inhibitors in complex with protein kinase A and mutants.
- C. Breitenlechner, W. Friebe, B. Masjost
- Biology, ChemistryJournal of medicinal chemistry
- 17 September 2005
The PKA to PKB exchanges F187L and Q84E enable the design of the selective inhibitors described herein which mimic ATP but extend further into a site not occupied by ATP, in which selectivity over PKA can be achieved by the introduction of bulkier substituents.
Structural Analysis of Protein Kinase A Mutants with Rho-kinase Inhibitor Specificity*
Kinetic results corroborate the hypothesis that side-chain identities form the major determinants of selectivity in Rho-kinase and suggest that PKA mutants are valuable for use as surrogate kinases for structure-based inhibitor design.
Head morphogenesis genes of the Bacillus subtilis bacteriophage SPP1.
The organization of the DNA packaging and head genes of SPP1 resembles the organization of genes in the analogous regions of phage lambda and P22.
Semisynthetic derivatives of concanamycin A and C, as inhibitors of V- and P-type ATPases: structure-activity investigations and developments of photoaffinity probes.
- S. Dröse, C. Boddien, M. Gassel, G. Ingenhorst, A. Zeeck, K. Altendorf
- Chemistry, BiologyBiochemistry
- 6 March 2001
V-type ATPases are inhibited by the plecomacrolides bafilomycin and concanamycin, which exert their inhibitory potential at nanomolar concentrations. In addition, some P-type ATPases are inhibited at…