Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Clara Brieke"'
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Toxin–antitoxin (TA) systems are important modulators of bacterial physiology. Here, the authors structurally characterize the epsilon/zeta TA system from the Gram-negative pathogen Neisseria gonorrhoeae and show that the toxin interferes with pept
Externí odkaz:
https://doaj.org/article/699eb30358954fe0b388e73c4a1fe340
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 12, Iss 1, Pp 2849-2864 (2016)
The chemical complexity and biological activity of the glycopeptide antibiotics (GPAs) stems from their unique crosslinked structure, which is generated by the actions of cytochrome P450 (Oxy) enzymes that affect the crosslinking of aromatic side cha
Externí odkaz:
https://doaj.org/article/f5cc71bf50ca4f659373762a46ab8ebd
Publikováno v:
Drug Discovery Today. 26:2786-2793
Delivering transformative therapies to patients while maintaining growth in the pharmaceutical industry requires an efficient use of research and development (R&D) resources and technologies to develop high-impact new molecular entities (NMEs). Howev
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Nature Communications
Bacterial toxin–antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 12, Iss 1, Pp 2849-2864 (2016)
Beilstein Journal of Organic Chemistry
Beilstein Journal of Organic Chemistry
The chemical complexity and biological activity of the glycopeptide antibiotics (GPAs) stems from their unique crosslinked structure, which is generated by the actions of cytochrome P450 (Oxy) enzymes that affect the crosslinking of aromatic side cha
Autor:
Felix Schuebel, Julia Schessner, Clara Brieke, Andrea Rocker, Anton Meinhart, Daniel Edelmann
Publikováno v:
The Journal of Biological Chemistry
An arsenal of effector proteins is injected by bacterial pathogens into the host cell or its vicinity to increase virulence. The commonly used top-down approaches inferring the toxic mechanism of individual effector proteins from the host's phenotype
Publikováno v:
Journal of the American Chemical Society
Glycopeptide antibiotics (GPAs) are nonribosomal peptides rich in modifications introduced by external enzymes. These enzymes act on the free peptide aglycone or intermediates bound to the nonribosomal peptide synthetase (NRPS) assembly line. In this
Publikováno v:
Chemical Communications
We show that two α-N-methyltransferases involved in the biosynthesis of glycopeptide antibiotics (GPAs) already recognise partly crosslinked precursor peptides of teicoplanin aglycone indicating that in vivo N-methylation can occur as an early tailo
Publikováno v:
MedChemComm
The glycopeptide antibiotics are important clinical antibiotics that are currently employed against serious Gram-positive bacterial infections. Their chemical complexity means that their production is reliant upon the natural biosynthesis pathway, of
Publikováno v:
Journal of Inorganic Biochemistry
Cytochrome P450 enzymes perform an impressive range of oxidation reactions against diverse substrate scaffolds whilst generally maintaining a conserved tertiary structure and active site chemistry. Within secondary metabolism, P450 enzymes play wides