Zobrazeno 1 - 9
of 9
pro vyhledávání: '"John S. Scotti"'
Autor:
Rebecca S. Dickinson, Fiona Murphy, Catherine Doherty, Sam Williams, Ananda Mirchandani, Joseph Willson, John S. Scotti, Gail Preston, Christopher J. Schofield, Moira K.B. Whyte, Sarah R. Walmsley
Publikováno v:
Wellcome Open Research, Vol 2 (2017)
Background: Pseudomonas species are adapted to evade innate immune responses and can persist at sites of relative tissue hypoxia, including the mucus-plugged airways of patients with cystic fibrosis and bronchiectasis. The ability of these bacteria t
Externí odkaz:
https://doaj.org/article/fac93a15831840aaafb87d14139b467b
Autor:
Wei Ge, Christopher J. Schofield, Michael A. McDonough, John S. Scotti, Yu Nakashima, Hwangseo Park, Marios S. Markoulides, Hwanho Choi, Rasheduzzaman Chowdhury, Helen Thorbjornsrud, Joongoo Lee, Dahye Kang, Sungwoo Hong, Thomas M. Leissing, Philip A. Gerken, Adam P. Hardy
Publikováno v:
Communications Chemistry, Vol 3, Iss 1, Pp 1-10 (2020)
Factor inhibiting hypoxia-inducible factor (FIH) is a 2-oxoglutarate-dependent protein hydroxylase that catalyses C3 hydroxylations of protein residues. We report FIH can accept (D)- and (L)-residues for hydroxylation. The substrate selectivity of FI
Autor:
Joseph A Willson, Sarah R. Walmsley, Samuel P Williams, John S. Scotti, Ananda S. Mirchandani, Catherine J. Doherty, Rebecca S. Dickinson, Gail M. Preston, Moira K. B. Whyte, Fiona Murphy, Christopher J. Schofield
Publikováno v:
Dickinson, R S, Murphy, F, Doherty, C, Williams, S, Mirchandani, A, Willson, J A, Scotti, J S, Preston, G, Schofield, C J, Whyte, M K B & Walmsley, S R 2017, ' Pseudomonas expression of an oxygen sensing prolyl hydroxylase homologue regulates neutrophil host responses in vitro and in vivo ', Wellcome Open Research, vol. 2, pp. 104 . https://doi.org/10.12688/wellcomeopenres.12871.1
Wellcome Open Research
Wellcome Open Research
Background: Pseudomonas species are adapted to evade innate immune responses and can persist at sites of relative tissue hypoxia, including the mucus-plugged airways of patients with cystic fibrosis and bronchiectasis. The ability of these bacteria t
Autor:
Lesley A.H. Bowman, Michael A. Bentley, Shoichiro Horita, Nadia J. Kershaw, Steinar M. Paulsen, Joongoo Lee, Gail M. Preston, Christoph M. Tang, Christopher J. Schofield, Nikita D. Loik, Wei Ge, Ivanhoe K. H. Leung, Chia Hua Ho, Hwanho Choi, John S. Scotti, Jordi Paps, Michael A. McDonough, Holger B. Kramer, Timothy D. W. Claridge, Wei Shen Aik
Publikováno v:
Proceedings of the National Academy of Sciences. 111:13331-13336
The roles of 2-oxoglutarate (2OG)-dependent prolyl-hydroxylases in eukaryotes include collagen stabilization, hypoxia sensing, and translational regulation. The hypoxia-inducible factor (HIF) sensing system is conserved in animals, but not in other o
Autor:
Marina Demetriades, John S. Scotti, Wei Shen Aik, Michael A. McDonough, Hwanho Choi, Christopher J. Schofield, Lingzhi Gong
Publikováno v:
Nucleic Acids Research
ALKBH5 is a 2-oxoglutarate (2OG) and ferrous iron-dependent nucleic acid oxygenase (NAOX) that catalyzes the demethylation of N6-methyladenine in RNA. ALKBH5 is upregulated under hypoxia and plays a role in spermatogenesis. We describe a crystal stru
Autor:
Emily Flashman, Christopher J. Schofield, Sarah E. Wilkins, John S. Scotti, Rasheduzzaman Chowdhury, Richard J. Hopkinson
Animals respond to chronic limiting oxygen availability by activation of the hypoxia inducible factor (HIF) system. As shown by pioneering work on erythropoietin regulation, HIF is an α,β-heterodimeric transcription factor which contains basic-heli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f06f2c73cb95c2977781b9fe6aa4fe9
https://doi.org/10.1039/9781782621959-00169
https://doi.org/10.1039/9781782621959-00169
Autor:
Shoichiro, Horita, John S, Scotti, Cyrille, Thinnes, Yousef S, Mottaghi-Taromsari, Armin, Thalhammer, Wei, Ge, WeiShen, Aik, Christoph, Loenarz, Christopher J, Schofield, Michael A, McDonough
Publikováno v:
Structure(London, England:1993)
Summary Post-translational ribosomal protein hydroxylation is catalyzed by 2-oxoglutarate (2OG) and ferrous iron dependent oxygenases, and occurs in prokaryotes and eukaryotes. OGFOD1 catalyzes trans-3 prolyl hydroxylation at Pro62 of the small ribos
We have developed a synthetic strategy that mimics the diversity-generating power of monoterpenoid indole alkaloid biosynthesis. Our general approach goes beyond diversification of a single natural product-like substructure and enables production of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::059c122915de5b42f178db334546df9a
https://europepmc.org/articles/PMC3842850/
https://europepmc.org/articles/PMC3842850/
Autor:
Michael A. McDonough, Timothy D. W. Claridge, Christopher J. Schofield, Wei Ge, Rasheduzzaman Chowdhury, John S. Scotti, Ming Yang, Nikita D. Loik, James S. O. McCullagh, Adam P. Hardy
Publikováno v:
Angewandte Chemie International Edition
Substrate specificity: Biochemical and crystallographic analyses reveal the hypoxia-inducible factor hydroxylase (FIH) as being promiscuous with respect to the residues that it can hydroxylate in β-position, which in addition to Asn, Asp, and His in