Zobrazeno 1 - 9
of 9
pro vyhledávání: '"O P, Kuipers"'
Autor:
M G, Gunnewijk, P T, van den Bogaard, L M, Veenhoff, E H, Heuberger, W M, de Vos, M, Kleerebezem, O P, Kuipers, B, Poolman
Publikováno v:
Journal of molecular microbiology and biotechnology. 3(3)
The involvement of phosphoeno/pyruvate:sugar phosphotransferase (PTS) proteins, like HPr and IIA(Glc), in the regulation of carbohydrate utilization has been well established in Gram-negative and Gram-positive bacteria. The majority of the studies of
Autor:
C, van Kraaij, E, Breukink, H S, Rollema, R S, Bongers, H A, Kosters, B, de Kruijff, O P, Kuipers
Publikováno v:
European journal of biochemistry. 267(3)
The antimicrobial peptide nisin contains the uncommon amino acid residues lanthionine and methyl-lanthionine, which are post-translationally formed from Ser, Thr and Cys residues. To investigate the importance of these uncommon residues for nisin act
Publikováno v:
Antonie van Leeuwenhoek. 76(1-4)
Autor:
O P, Kuipers
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 57
Publikováno v:
Developments in biological standardization. 85
Publikováno v:
Developments in biological standardization. 85
Publikováno v:
The Journal of biological chemistry. 269(5)
Structural genes for small lanthionine-containing antimicrobial peptides, known as lantibiotics, encode N-terminal leader sequences which are not present in the mature peptide, but are cleaved off at some stage in the maturation process. Leader seque
Publikováno v:
The Journal of biological chemistry. 267(34)
The small antimicrobial peptide nisin, produced by Lactococcus lactis, contains the uncommon amino acid residues dehydroalanine and dehydrobutyrine and five thio ether bridges. Since these structures are posttranslationally formed from Ser, Thr, and
Publikováno v:
Advances in experimental medicine and biology. 279