Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Hannah K. D'Ambrosio"'
Publikováno v:
iScience, Vol 25, Iss 7, Pp 104608- (2022)
Externí odkaz:
https://doaj.org/article/73337981ad9d401b9ca76a975627f563
Publikováno v:
ACS Chemical Biology. 18:785-793
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e8914234bd2d10999e58a4dc8080b49
https://doi.org/10.1021/acschembio.2c00783
https://doi.org/10.1021/acschembio.2c00783
Autor:
Aaron M. Keeler, Porter E. Petruzziello, Elizabeth G. Boger, Hannah K. D’Ambrosio, Emily R. Derbyshire
Polyketide synthases (PKSs) are megaenzymes that form chemically diverse polyketides and are found within the genomes of nearly all classes of life. We recently discovered the type I PKS from the apicomplexan parasiteToxoplasma gondii, TgPKS2, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::98353adc521507e6c0a254461b98c15a
https://doi.org/10.1101/2023.05.23.541938
https://doi.org/10.1101/2023.05.23.541938
Publikováno v:
ChemBioChem. 21:1279-1284
Anopheles mosquito microbiomes are intriguing ecological niches. Within the gut, microbes adapt to oxidative stress due to heme and iron after blood meals. Although metagenomic sequencing has illuminated spatial and temporal fluxes of microbiome popu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdfee8741fa66d3a511681fc92fe4b76
https://doi.org/10.1002/cbic.201900675
https://doi.org/10.1002/cbic.201900675
Publikováno v:
iScience. 25(6)
Type I polyketide synthases (PKSs) are multidomain, multimodule enzymes capable of producing complex polyketide metabolites. These modules contain an acyltransferase (AT) domain, which selects acyl-CoA substrates to be incorporated into the metabolit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::92733f79f094cd2c43bd512388985604
https://pubmed.ncbi.nlm.nih.gov/35772031
https://pubmed.ncbi.nlm.nih.gov/35772031
Autor:
Rachel Leicher, Albert S Agustinus, Qingfei Zheng, Bo Liu, Yael David, Adewola Osunsade, Efrat Finkin-Groner, Hannah K. D'Ambrosio, Shixin Liu, Nathaniel D. Omans, Sarat Chandarlapaty
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Nature Communications
Nature Communications
Cellular proteins continuously undergo non-enzymatic covalent modifications (NECMs) that accumulate under normal physiological conditions and are stimulated by changes in the cellular microenvironment. Glycation, the hallmark of diabetes, is a preval
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aeb1ed10f1f1cd0b28b91fa3db2cea98
https://doaj.org/article/d549df8147a043739d0eb71b8d597555
https://doaj.org/article/d549df8147a043739d0eb71b8d597555
Publikováno v:
ACS chemical biology. 15(1)
Adenylate-forming enzymes represent one of the most important enzyme classes in biology, responsible for the activation of carboxylate substrates for biosynthetic modifications. The byproduct of the adenylate-forming enzyme acetyl-CoA synthetase, ace
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1ad42b75338c877f5ecac2dc5b94b8b
https://pubmed.ncbi.nlm.nih.gov/31815417
https://pubmed.ncbi.nlm.nih.gov/31815417
Publikováno v:
ChemBioChem. 21:1234-1234
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b066f8f9695462532f2230ffd24c8ed5
https://doi.org/10.1002/cbic.202000216
https://doi.org/10.1002/cbic.202000216
Autor:
Andrew J. Rouff, Jack T. Bragg, Brittany J. Bisnett, Margot G. Paulick, Terence S. Fu, Sudhir Khetan, Hannah K. D'Ambrosio, Caroline A. Gorka, Michael Boyce, Faraz A. Khan, Joshua T. Rose, Timothy J. Smith
Publikováno v:
Chembiochem : a European journal of chemical biology. 18(18)
Trehalose is a disaccharide produced by many organisms to better enable them to survive environmental stresses, including heat, cold, desiccation, and reactive oxygen species. Mammalian cells do not naturally biosynthesize trehalose; however, when in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2339da919fcb90dbd4b65d2c34b0c29f
https://pubmed.ncbi.nlm.nih.gov/28722776
https://pubmed.ncbi.nlm.nih.gov/28722776