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Unique organization of the dnaA region from Prochlorococcus marinus CCMP1375, a marine cyanobacterium.
Richter S, Hess WR, Krause M, Messer W. Richter S, et al. Among authors: krause m. Mol Gen Genet. 1998 Mar;257(5):534-41. doi: 10.1007/s004380050679. Mol Gen Genet. 1998. PMID: 9563839
Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis.
Lucka L, Krause M, Danker K, Reutter W, Horstkorte R. Lucka L, et al. Among authors: krause m. FEBS Lett. 1999 Jul 9;454(3):341-4. doi: 10.1016/s0014-5793(99)00837-6. FEBS Lett. 1999. PMID: 10431835
Bacterial replication initiator DnaA. Rules for DnaA binding and roles of DnaA in origin unwinding and helicase loading.
Messer W, Blaesing F, Jakimowicz D, Krause M, Majka J, Nardmann J, Schaper S, Seitz H, Speck C, Weigel C, Wegrzyn G, Welzeck M, Zakrzewska-Czerwinska J. Messer W, et al. Among authors: krause m. Biochimie. 2001 Jan;83(1):5-12. doi: 10.1016/s0300-9084(00)01216-5. Biochimie. 2001. PMID: 11254968 Review.
Cloning of the tyrocidine synthetase 1 gene from Bacillus brevis and its expression in Escherichia coli.
Marahiel MA, Krause M, Skarpeid HJ. Marahiel MA, et al. Among authors: krause m. Mol Gen Genet. 1985;201(2):231-6. doi: 10.1007/BF00425664. Mol Gen Genet. 1985. PMID: 3003526
Complexes at the replication origin of Bacillus subtilis with homologous and heterologous DnaA protein.
Krause M, Rückert B, Lurz R, Messer W. Krause M, et al. J Mol Biol. 1997 Dec 5;274(3):365-80. doi: 10.1006/jmbi.1997.1404. J Mol Biol. 1997. PMID: 9405146
Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases.
Krätzschmar J, Krause M, Marahiel MA. Krätzschmar J, et al. Among authors: krause m. J Bacteriol. 1989 Oct;171(10):5422-9. doi: 10.1128/jb.171.10.5422-5429.1989. J Bacteriol. 1989. PMID: 2477357 Free PMC article.
Three open reading frames were identified; the corresponding genes, called grsT, grsA, and grsB, were found to be organized in one transcriptional unit, not two as previously reported (M. Krause and M. A. Marahiel, J. Bacteriol. 170:4669-4674, 1988). The enti …
Three open reading frames were identified; the corresponding genes, called grsT, grsA, and grsB, were found to be organized in one transcrip …
Organization of the biosynthesis genes for the peptide antibiotic gramicidin S.
Krause M, Marahiel MA. Krause M, et al. J Bacteriol. 1988 Oct;170(10):4669-74. doi: 10.1128/jb.170.10.4669-4674.1988. J Bacteriol. 1988. PMID: 2459107 Free PMC article.
Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes.
Turgay K, Krause M, Marahiel MA. Turgay K, et al. Among authors: krause m. Mol Microbiol. 1992 Feb;6(4):529-46. doi: 10.1111/j.1365-2958.1992.tb01498.x. Mol Microbiol. 1992. PMID: 1560782
An active serine is involved in covalent substrate amino acid binding at each reaction center of gramicidin S synthetase.
Schlumbohm W, Stein T, Ullrich C, Vater J, Krause M, Marahiel MA, Kruft V, Wittmann-Liebold B. Schlumbohm W, et al. Among authors: krause m. J Biol Chem. 1991 Dec 5;266(34):23135-41. J Biol Chem. 1991. PMID: 1744112
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