Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Anja, Greule"'
Autor:
Songya Zhang, Lin Zhang, Anja Greule, Julien Tailhades, Edward Marschall, Panward Prasongpholchai, Daniel J. Leng, Jingfan Zhang, Jing Zhu, Joe A. Kaczmarski, Ralf B. Schittenhelm, Oliver Einsle, Colin J. Jackson, Fabrizio Alberti, Andreas Bechthold, Youming Zhang, Manuela Tosin, Tong Si, Max J. Cryle
Publikováno v:
Acta Pharmaceutica Sinica B, Vol 13, Iss 8, Pp 3561-3574 (2023)
WS9326A is a peptide antibiotic containing a highly unusual N-methyl-E-2-3-dehydrotyrosine (NMet-Dht) residue that is incorporated during peptide assembly on a non-ribosomal peptide synthetase (NRPS). The cytochrome P450 encoded by sas16 (P450Sas) ha
Externí odkaz:
https://doaj.org/article/7d63ec27ecab4b6da2493ecc0f966b70
Autor:
Anja Greule, Thierry Izoré, Daniel Machell, Mathias H. Hansen, Melanie Schoppet, James J. De Voss, Louise K. Charkoudian, Ralf B. Schittenhelm, Jeffrey R. Harmer, Max J. Cryle
Publikováno v:
Frontiers in Chemistry, Vol 10 (2022)
Cytochrome P450 enzymes (P450s) are a superfamily of monooxygenases that utilize a cysteine thiolate–ligated heme moiety to perform a wide range of demanding oxidative transformations. Given the oxidative power of the active intermediate formed wit
Externí odkaz:
https://doaj.org/article/6f12f2286b3c4e31af9588c7cec2df9b
Autor:
Anja Greule, Thierry Izoré, Dumitrita Iftime, Julien Tailhades, Melanie Schoppet, Yongwei Zhao, Madeleine Peschke, Iftekhar Ahmed, Andreas Kulik, Martina Adamek, Robert J. A. Goode, Ralf B. Schittenhelm, Joe A. Kaczmarski, Colin J. Jackson, Nadine Ziemert, Elizabeth H. Krenske, James J. De Voss, Evi Stegmann, Max J. Cryle
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Kistamicin is a structurally divergent glycopeptide antibiotic (GPA) that contains a unique 15-membered A-O-B ring. Here, the authors obtained a crystal structure of the kistamicin OxyA/X-domain complex and analysed the cyclisation cascade leading to
Externí odkaz:
https://doaj.org/article/09b465696c784ff3b63bbdc04e4fd0ff
Publikováno v:
Chemical communications (Cambridge, England). 57(18)
Glycopeptides such as vancomycin are antibiotics of last resort whose biosynthetic pathways still hold undefined details. Chemical probes were used to capture biosynthetic intermediates generated in the nonribosomal peptide formation of vancomycin in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf4d56fb4f326665da12ef7e9b26d888
https://pubmed.ncbi.nlm.nih.gov/33533358
https://pubmed.ncbi.nlm.nih.gov/33533358
Autor:
Anja Greule, Saranjah Indumathy, Paul Bowness, Stephanie Gras, Max J. Cryle, Hanim Halim, Ralf B. Schittenhelm, Jamie Rossjohn, Terry C.C. Lim Kam Sian, Anthony W. Purcell
Publikováno v:
J Biol Chem
Expression of human leukocyte antigen (HLA)-B27 is strongly associated with predisposition toward ankylosing spondylitis (AS) and other spondyloarthropathies. However, the exact involvement of HLA-B27 in disease initiation and progression remains unc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c4b17fe31c2fbf883719000c67ace8d
https://doi.org/10.1074/jbc.ra119.010257
https://doi.org/10.1074/jbc.ra119.010257
Autor:
Anja Greule, Max J. Cryle
Glycopeptide antibiotics (GPAs) are an important class of secondary metabolites produced by various actinobacteria, with the most prominent members being vancomycin and teicoplanin. The heptapeptide backbone of GPAs is assembled by a nonribosomal pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::759c2b58ea4b765ec7ca0d17c92b82f4
https://doi.org/10.1016/b978-0-12-409547-2.14691-8
https://doi.org/10.1016/b978-0-12-409547-2.14691-8
Publikováno v:
Natural Product Reports. 35:757-791
Covering: 2000 up to 2018 The cytochromes P450 (P450s) are a superfamily of heme-containing monooxygenases that perform diverse catalytic roles in many species, including bacteria. The P450 superfamily is widely known for the hydroxylation of unactiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ad39276cb1ace3e66e423ac719cc5fc
https://doi.org/10.1039/c7np00063d
https://doi.org/10.1039/c7np00063d
Autor:
Julien Tailhades, Anja Greule, Max J. Cryle, Ralf B. Schittenhelm, Robert J. A. Goode, Melanie Schoppet, James J. De Voss, Yongwei Zhao
Publikováno v:
Organic letters. 21(21)
Natural products are the greatest source of antimicrobial agents, although their structural complexity often renders synthetic production and diversification of key classes impractical. One pertinent example is the glycopeptide antibiotics (GPAs), wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93a190f8392e01c4df64f9896afdc271
https://pubmed.ncbi.nlm.nih.gov/31603691
https://pubmed.ncbi.nlm.nih.gov/31603691
Autor:
Julien Tailhades, Joe A. Kaczmarski, Robert J. A. Goode, Dumitrita Iftime, Anja Greule, Thierry Izoré, Evi Stegmann, Iftekhar Ahmed, Andreas Kulik, Madeleine Peschke, Elizabeth H. Krenske, James J. De Voss, Melanie Schoppet, Nadine Ziemert, Colin J. Jackson, Martina Adamek, Yongwei Zhao, Ralf B. Schittenhelm, Max J. Cryle
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
Nature Communications
Nature Communications
Kistamicin is a divergent member of the glycopeptide antibiotics, a structurally complex class of important, clinically relevant antibiotics often used as the last resort against resistant bacteria. The extensively crosslinked structure of these anti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5853e99bc6b1c8c7a1f1f7e067329b86
https://doi.org/10.1038/s41467-019-10384-w
https://doi.org/10.1038/s41467-019-10384-w
Publikováno v:
Methods in enzymology. 617
Nonribosomal peptide biosynthesis is a complex enzymatic assembly responsible for producing a great diversity of bioactive peptide natural products. Due to the recurring arrangement of catalytic domains within these machineries, great interest has be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::62a3ef28910fea794df34717f9b328eb
https://pubmed.ncbi.nlm.nih.gov/30784400
https://pubmed.ncbi.nlm.nih.gov/30784400