Zobrazeno 1 - 10
of 364
pro vyhledávání: '"T. Stubbs"'
Autor:
Lisa Schmidt, Christian Tüting, Fotis L. Kyrilis, Farzad Hamdi, Dmitry A. Semchonok, Gerd Hause, Annette Meister, Christian Ihling, Milton T. Stubbs, Andrea Sinz, Panagiotis L. Kastritis
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-12 (2024)
Abstract The high abundance of most viruses in infected host cells benefits their structural characterization. However, endogenous viruses are present in low copy numbers and are therefore challenging to investigate. Here, we retrieve cell extracts e
Externí odkaz:
https://doaj.org/article/b2213ea566234e8b8a773838896395a9
Autor:
Kristyna Kupkova, Jose Verdezoto Mosquera, Jason P. Smith, Michał Stolarczyk, Tessa L. Danehy, John T. Lawson, Bingjie Xue, John T. Stubbs, Nathan LeRoy, Nathan C. Sheffield
Publikováno v:
BMC Genomics, Vol 23, Iss 1, Pp 1-6 (2022)
Abstract Background Epigenome analysis relies on defined sets of genomic regions output by widely used assays such as ChIP-seq and ATAC-seq. Statistical analysis and visualization of genomic region sets is essential to answer biological questions in
Externí odkaz:
https://doaj.org/article/950b81e1220f40159c7dd5c9d6968d0e
Autor:
Farzad Hamdi, Christian Tüting, Dmitry A Semchonok, Koen M Visscher, Fotis L Kyrilis, Annette Meister, Ioannis Skalidis, Lisa Schmidt, Christoph Parthier, Milton T Stubbs, Panagiotis L Kastritis
Publikováno v:
PLoS ONE, Vol 15, Iss 5, p e0232540 (2020)
Here we present the structure of mouse H-chain apoferritin at 2.7 Å (FSC = 0.143) solved by single particle cryogenic electron microscopy (cryo-EM) using a 200 kV device, the Thermo Fisher Glacios®. This is a compact, two-lens illumination system w
Externí odkaz:
https://doaj.org/article/ce381ff2427445a7947ff822af7eb63e
Autor:
Kumar Nagarathinam, Yoshiko Nakada-Nakura, Christoph Parthier, Tohru Terada, Narinobu Juge, Frank Jaenecke, Kehong Liu, Yunhon Hotta, Takaaki Miyaji, Hiroshi Omote, So Iwata, Norimichi Nomura, Milton T. Stubbs, Mikio Tanabe
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
The multidrug resistance transporter mediated efflux of antibiotics from the bacterial cytoplasm represents a major challenge to medicine. Here authors solve the X-ray crystallographic structure of the drug/H+ antiporter MdfA from Escherichia coli an
Externí odkaz:
https://doaj.org/article/9c31b685bee4442382a7b84e7402aa22
Akademický článek
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Autor:
Lisa Schmidt, Christian Tüting, Fotis L. Kyrilis, Farzad Hamdi, Dmitry A. Semchonok, Gerd Hause, Annette Meister, Christian Ihling, Pranav N. M. Shah, Milton T. Stubbs, Andrea Sinz, David I. Stuart, Panagiotis L. Kastritis
The high abundance of most viruses in infected host cells benefits their structural characterization; endogenous viruses are present in low copy numbers, however, and are therefore challenging to investigate. Here, we retrieve cell extracts enriched
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::743ec44aa3e5350e31c1f7b4d54fc2c3
https://doi.org/10.1101/2022.07.15.498668
https://doi.org/10.1101/2022.07.15.498668
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
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Autor:
Archna Archna, Constanze Breithaupt, Duc-Anh Nguyen, Hauke Lilie, Jorg Ziegler, Milton T. Stubbs
MqnA, the only chorismate dehydratase known so far, catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. Here we present crystal structures of Streptomyces coelicolor MqnA and its active site variants in complex w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::201970f4ddae44a7c6887a77e30fb793
https://doi.org/10.26434/chemrxiv-2022-dhhzn
https://doi.org/10.26434/chemrxiv-2022-dhhzn
Autor:
Archna Prasad, Constanze Breithaupt, Duc-Anh Nguyen, Hauke Lilie, Jörg Ziegler, Milton T. Stubbs
Publikováno v:
Journal of Biological Chemistry. 298:102601
MqnA, the only chorismate dehydratase known so far, catalyzes the initial step in the biosynthesis of menaquinone via the futalosine pathway. Details of the MqnA reaction mechanism remain unclear. Here, we present crystal structures of Streptomyces c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::007f54404029de81e2ecbb269c9cab35
https://doi.org/10.1016/j.jbc.2022.102601
https://doi.org/10.1016/j.jbc.2022.102601
Akademický článek
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K zobrazení výsledku je třeba se přihlásit.