Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Alicia Engelbrecht"'
Autor:
Alicia Engelbrecht, Felix Wolf, Annika Esch, Andreas Kulik, Sergei I. Kozhushkov, Armin de Meijere, Chambers C. Hughes, Leonard Kaysser
Publikováno v:
Organic Letters. 24:736-740
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f5a5fa77cbfab401d928bf58d9f0046
https://doi.org/10.1021/acs.orglett.1c04205
https://doi.org/10.1021/acs.orglett.1c04205
Autor:
Ikuro Abe, Richiro Ushimaru, Shotaro Shimo, Andreas Kulik, Masanobu Uchiyama, Mei Harada, Leonard Kaysser, Alicia Engelbrecht, Kazunori Miyamoto
Publikováno v:
Journal of the American Chemical Society. 143:18413-18418
Belactosins and hormaomycins are peptide natural products containing 3-(2-aminocyclopropyl)alanine and 3-(2-nitrocyclopropyl)alanine residues, respectively, with opposite stereoconfigurations of the cyclopropane ring. Herein we demonstrate that the h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d56f4f2d0c6efb771fc8275e493fca8
https://doi.org/10.1021/jacs.1c10201
https://doi.org/10.1021/jacs.1c10201
Publikováno v:
Microbial physiology, 31(3):217-232
Nocardia spp. are filamentous Actinobacteria of the order Corynebacteriales and mostly known for their ability to cause localized and systemic infections in humans. However, the onset and progression of nocardiosis is only poorly understood, in parti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56987c26e3d1d1897d56c16dc0b81501
https://doi.org/10.1159/000516864
https://doi.org/10.1159/000516864
Autor:
Alicia, Engelbrecht, Felix, Wolf, Annika, Esch, Andreas, Kulik, Sergei I, Kozhushkov, Armin, de Meijere, Chambers C, Hughes, Leonard, Kaysser
Publikováno v:
Organic letters. 24(2)
Belactosin A, a β-lactone proteasome inhibitor, contains a unique 3-(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5954676eed7f97736934675a25475680
https://pubmed.ncbi.nlm.nih.gov/34990553
https://pubmed.ncbi.nlm.nih.gov/34990553
Autor:
Maraike Müller, Robert Maria Kluj, Qingping Xu, Alicia Engelbrecht, Marina Borisova, Christoph Mayer, Khaled A. Selim, Alexander Titz, Tim Teufel, Katja Balbuchta, Matthew B. Calvert, Isabel Hottmann
Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that potentially lyse bacterial cells. They catalyze an endo-lytic cleavage of the peptidoglycan, the structural component of the bacterial cell wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f53e0923112be7de28920505f126ab3
https://doi.org/10.1101/2021.01.10.425899
https://doi.org/10.1101/2021.01.10.425899
Autor:
Alexander Titz, Qingping Xu, Marina Borisova, Alicia Engelbrecht, Isabel Hottmann, Christoph Mayer, Maraike Müller, Matthew B. Calvert, Robert Maria Kluj, Khaled A. Selim, Tim Teufel, Katja Balbuchta
Publikováno v:
The Journal of Biological Chemistry
The Journal of biological chemistry
United States
The Journal of biological chemistry
United States
Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that catalyze an endo-lytic cleavage of peptidoglycan; i.e., they hydrolyze the β-1,4-glycosidic bonds connecting N-acetylmuramic acid (MurNAc) an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e70e3e2be80887f413760f79d4b107d3
https://pubmed.ncbi.nlm.nih.gov/33684445
https://pubmed.ncbi.nlm.nih.gov/33684445
Autor:
Björn, Watzer, Alicia, Engelbrecht, Waldemar, Hauf, Mark, Stahl, Iris, Maldener, Karl, Forchhammer
Publikováno v:
Microbial Cell Factories
Background PII signal processor proteins are wide spread in prokaryotes and plants where they control a multitude of anabolic reactions. Efficient overproduction of metabolites requires relaxing the tight cellular control circuits. Here we demonstrat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2926a6a2c081df7a6bae585787734b0f
https://pubmed.ncbi.nlm.nih.gov/26608263
https://pubmed.ncbi.nlm.nih.gov/26608263