Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Dominik A Herbst"'
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e48427 (2012)
Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto aromatic substrates in biosynthetic pathways of microbial secondary metabolites. Therefore, these enzymes contribute to the chemical diversity of natural products.
Externí odkaz:
https://doaj.org/article/aa60e15bc3684e499f11873e42399555
Autor:
Meagan N. Esbin, Robert Tjian, Dominik A Herbst, Gina M. Dailey, Eva Nogales, Qianglin Fang, Xavier Darzacq, Robert K. Louder, Claire Dugast-Darzacq
Publikováno v:
Nature Structural & Molecular Biology
Nature structural & molecular biology, vol 28, iss 12
Nature structural & molecular biology, vol 28, iss 12
The SAGA complex is a regulatory hub involved in gene regulation, chromatin modification, DNA damage repair and signaling. While structures of yeast SAGA (ySAGA) have been reported, there are noteworthy functional and compositional differences for th
Autor:
Jillian F. Banfield, Dominik A Herbst, Eva Nogales, Connor A. Tsuchida, Katarzyna M. Soczek, Jennifer A. Doudna, Patrick Pausch, Basem Al-Shayeb
Publikováno v:
Nat Struct Mol Biol
CRISPR-CasΦ, a small RNA-guided enzyme found uniquely in bacteriophages, achieves programmable DNA cutting as well as genome editing. To investigate how the hypercompact enzyme recognizes and cleaves double-stranded DNA, we determined cryo-EM struct
Autor:
Eva Nogales, Q. Fang, Robert Tjian, Meagan N. Esbin, Claire Dugast-Darzacq, Robert K. Louder, Dominik A Herbst, Gina M. Dailey, Xavier Darzacq
Human SAGA is an essential co-activator complex that regulates gene expression by interacting with enhancer-bound activators, recruiting transcriptional machinery, and modifying chromatin near promoters. Subunit variations and the metazoan-specific r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8f6d4d5343916a6fb1d3f0a742334406
https://doi.org/10.1101/2021.02.08.430339
https://doi.org/10.1101/2021.02.08.430339
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 77:a2-a2
Publikováno v:
Nature. 531:533-537
Polyketide synthases (PKSs) are biosynthetic factories that produce natural products with important biological and pharmacological activities1, 2, 3. Their exceptional product diversity is encoded in a modular architecture. Modular PKSs (modPKSs) cat
Publikováno v:
Natural product reports. 35(10)
Covering: up to mid of 2018 Type I fatty acid synthases (FASs) are giant multienzymes catalyzing all steps of the biosynthesis of fatty acids from acetyl- and malonyl-CoA by iterative precursor extension. Two strikingly different architectures of FAS
Autor:
Hilkka I. Kenttämaa, Thomas Klose, Michael G. Rossmann, Hanyu Zhu, Joann P. Max, Dominik A. Herbst
Publikováno v:
Structure. 23:1058-1065
Mimivirus was initially identified as a bacterium because its dense, 125-nm-long fibers stained Gram-positively. These fibers probably play a role during the infection of some host cells. The normal hosts of Mimivirus are unknown, but in the laborato
Publikováno v:
Journal of Biological Chemistry. 288:1991-2003
The biosynthesis of nonribosomally formed peptides (NRPs), which include important antibiotics such as vancomycin, requires the activation of amino acids through adenylate formation. The biosynthetic gene clusters of NRPs frequently contain genes for
Publikováno v:
Cell chemical biology. 24(3)
Fungal polyketide synthases (PKSs) are large, multi-domain enzymes that biosynthesize a wide range of natural products. A hallmark of these megasynthases is the iterative use of catalytic domains to extend and modify a series of enzyme-bound intermed