Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Christopher J. Schofield"'
Publikováno v:
Scientific reports. 12(1)
JmjC (Jumonji-C) domain-containing 5 (JMJD5) plays important roles in circadian regulation in plants and humans and is involved in embryonic development and cell proliferation. JMJD5 is a 2-oxoglutarate (2OG) and Fe(II) dependent oxygenase of the Jmj
Pseudohypoxic HIF pathway activation dysregulates collagen structure-function in human lung fibrosis
Autor:
Liudi Yao, Christopher J Brereton, Elizabeth R Davies, Yilu Zhou, Milica Vukmirovic, Joseph A Bell, Siyuan Wang, Robert A Ridley, Lareb SN Dean, Orestis G Andriotis, Franco Conforti, Lennart Brewitz, Soran Mohammed, Timothy Wallis, Ali Tavassoli, Rob M Ewing, Aiman Alzetani, Benjamin G Marshall, Sophie V Fletcher, Philipp J Thurner, Aurelie Fabre, Naftali Kaminski, Luca Richeldi, Atul Bhaskar, Christopher J Schofield, Matthew Loxham, Donna E Davies, Yihua Wang, Mark G Jones
Publikováno v:
eLife. 11
Extracellular matrix (ECM) stiffening with downstream activation of mechanosensitive pathways is strongly implicated in fibrosis. We previously reported that altered collagen nanoarchitecture is a key determinant of pathogenetic ECM structure-functio
Autor:
Afaf H. El-Sagheer, Ivanhoe K. H. Leung, Tom Brown, Michael A. McDonough, Anthony Tumber, Nok Yin Tam, Caitlin Clunie-O'Connor, Dong Zhang, Marina Demetriades, Shifali Shishodia, Wei Shen Aik, Thomas M. Leissing, Eidarus Salah, Pratheesh Maheswaran, Yi Min Ng, Christopher J. Schofield
Publikováno v:
Journal of Medicinal Chemistry
FTO catalyzes the Fe(II) and 2-oxoglutarate (2OG)-dependent modification of nucleic acids, including the demethylation of N6-methyladenosine (m6A) in mRNA. FTO is a proposed target for anti-cancer therapy. Using information from crystal structures of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::639c2be01f207a01903964a703615f30
https://ora.ox.ac.uk/objects/uuid:839b007e-dd4b-4bc0-ac22-ed37a4bd5169
https://ora.ox.ac.uk/objects/uuid:839b007e-dd4b-4bc0-ac22-ed37a4bd5169
Autor:
Christopher J. Schofield, Eidarus Salah, Lennart Brewitz, Armin Thalhammer, Anthony Tumber, Kirsten E. Christensen
Publikováno v:
Chemmedchem
The human 2‐oxoglutarate (2OG)‐dependent oxygenase aspartate/asparagine‐β‐hydroxylase (AspH) is a potential medicinal chemistry target for anticancer therapy. AspH is present on the cell surface of invasive cancer cells and accepts epidermal
Publikováno v:
Journal of medicinal chemistry. 64(11)
Factor inhibiting hypoxia-inducible factor (FIH) is a JmjC domain 2-oxogluarate and Fe(II)-dependent oxygenase that catalyzes hydroxylation of specific asparagines in the C-terminal transcriptional activation domain of hypoxia-inducible factor alpha
Autor:
Amelia, Brasnett, Inga, Pfeffer, Lennart, Brewitz, Rasheduzzaman, Chowdhury, Yu, Nakashima, Anthony, Tumber, Michael A, McDonough, Christopher J, Schofield
Publikováno v:
Angewandte Chemie (International Ed. in English)
Aspartate/asparagine‐β‐hydroxylase (AspH) is a human 2‐oxoglutarate (2OG) and FeII oxygenase that catalyses C3 hydroxylations of aspartate/asparagine residues of epidermal growth factor‐like domains (EGFDs). Unusually, AspH employs two histi
Publikováno v:
Bioorganic & Medicinal Chemistry
Graphical abstract
Human aspartate/asparagine-β-hydroxylase (AspH) is a 2-oxoglutarate (2OG) dependent oxygenase that catalyses the hydroxylation of Asp/Asn-residues of epidermal growth factor-like domains (EGFDs). AspH is reported to be upregu
Human aspartate/asparagine-β-hydroxylase (AspH) is a 2-oxoglutarate (2OG) dependent oxygenase that catalyses the hydroxylation of Asp/Asn-residues of epidermal growth factor-like domains (EGFDs). AspH is reported to be upregu
Autor:
Christopher J. Schofield, Inga Pfeffer, Anthony Tumber, Michael A. McDonough, Lennart Brewitz
Publikováno v:
Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
The human 2-oxoglutarate dependent oxygenase aspartate/asparagine-β-hydroxylase (AspH) catalyses the hydroxylation of Asp/Asn-residues in epidermal growth factor-like domains (EGFDs). AspH is upregulated on the surface of malign cancer cells; increa
Publikováno v:
The Journal of Biological Chemistry
Human aspartate/asparagine-β-hydroxylase (AspH) is a 2-oxoglutarate (2OG) dependent oxygenase that catalyzes the post-translational hydroxylation of Asp- and Asn-residues in epidermal growth factor-like domains (EGFDs). Despite its biomedical signif
Autor:
Penny A. Handford, Sacha A. Jensen, Martin Münzel, Kirsty S. Hewitson, Christopher J. Schofield, Udo Oppermann, Nadia J. Kershaw, Grazyna Kochan, T. Krojer, Lennart Brewitz, Inga Pfeffer, Richard J. Hopkinson, Michael A. McDonough, Luke A. McNeill, Holger B. Kramer
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
Nature Communications
Nature Communications
AspH is an endoplasmic reticulum (ER) membrane-anchored 2-oxoglutarate oxygenase whose C-terminal oxygenase and tetratricopeptide repeat (TPR) domains present in the ER lumen. AspH catalyses hydroxylation of asparaginyl- and aspartyl-residues in epid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc5f448ad1aa45d823fa2af6baae91d5
https://ora.ox.ac.uk/objects/uuid:0a1194dd-a9fc-4cd5-9390-46c2c68e9f33
https://ora.ox.ac.uk/objects/uuid:0a1194dd-a9fc-4cd5-9390-46c2c68e9f33