Zobrazeno 31 - 40
of 62
pro vyhledávání: '"Christopher J. Schofield"'
Autor:
Shifali Shishodia, Stephanie M. Luco, Hussein Daoud, Olga Jarinova, James Wickens, Hwanho Choi, David A. Dyment, Andrea C. Yu, Christopher J. Schofield, Michael A. McDonough, Dong Zhang, Jason R. Vanstone, Nancy Carson, Christine M. Armour, Mary-Ellen Harper, Fiona McMurray
Publikováno v:
Journal of Medical Genetics. 53:200-207
Background A homozygous loss-of-function mutation p.(Arg316Gln) in the fat mass and obesity-associated ( FTO ) gene, which encodes for an iron and 2-oxoglutarate-dependent oxygenase, was previously identified in a large family in which nine affected
Autor:
Christoph Loenarz, Martine I. Abboud, Rasheduzzaman Chowdhury, Kerstin Lippl, Ivanhoe K. H. Leung, Christopher J. Schofield, Timothy D. W. Claridge
Publikováno v:
Chembiochem. 19(21)
In animals, the response to chronic hypoxia is mediated by upregulation of the α,β-heterodimeric hypoxia-inducible factors (HIFs). Levels of HIFα isoforms, but not HIFβ, are regulated by their post-translational modification as catalysed by proly
Autor:
Akane Kawamura, Rachel Schiller, Richard J. Hopkinson, Louise J. Walport, Rasheduzzaman Chowdhury, Christopher J. Schofield, Yijia Zhang, Joanna Bonnici
Publikováno v:
FEBS Letters
Febs Letters
Febs Letters
N‐Methylation of lysyl residues is widely observed on histone proteins. Using isolated enzymes, we report mechanistic and structural studies on histone lysine demethylase (KDM)‐catalysed demethylation of N ε‐methylated lysine 26 on histone 1 i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b41479872714cf56da2a7738b8087eb
http://hdl.handle.net/10044/1/65213
http://hdl.handle.net/10044/1/65213
Autor:
Cindy H. Chau, Kirk R. Gustafson, Shaunna L. Beedie, Emily M Harris, Phoebe A. Huang, Christopher J. Schofield, William D. Figg, Melissa M. Cadelis, Brent R. Copp, Jonathan D. Strope, Goey Akl, Kristina M. Cook
Publikováno v:
Marine Drugs
Volume 16
Issue 7
Marine Drugs, Vol 16, Iss 7, p 241 (2018)
Volume 16
Issue 7
Marine Drugs, Vol 16, Iss 7, p 241 (2018)
Elements of the hypoxia inducible factor (HIF) transcriptional system, a key regulator of the cellular hypoxic response, are up-regulated in a range of cancer cells. HIF is fundamentally involved in tumor angiogenesis, invasion, and energy metabolism
Autor:
Pablo Wappner, Helen E McNeil, Robert K. Leśniak, Martine I. Abboud, Wei Ge, Rasheduzzaman Chowdhury, Simon J. Davis, Charlotte A. Hall, Weston B. Struwe, Ming Yang, Rebecca Konietzny, Peter J. Ratcliffe, Christopher J. Schofield, Sarah E. Wilkins, Charlotte D. Eaton, Roman Fischer, Suzana Markolovic, Maximiliano Javier Katz, Qinqin Zhuang, Justin L. P. Benesch, Benedikt M. Kessler, Mathew L. Coleman, Matthew E. Cockman
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Nature chemical biology
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Nature chemical biology
Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely relat
Autor:
Raymond J. Owens, Sander S. van Berkel, Philip Hinchliffe, Timothy R. Walsh, Ramya Salimraj, Magda Kosmopoulou, Michael A. McDonough, James Spencer, Anil Verma, Jürgen Brem, Christopher J. Schofield, Jonathan M. Tyrrell
Publikováno v:
The Febs Journal
Salimraj, R, Hinchliffe, P, Kosmopoulou, M, Tyrrell, J M, Brem, J, van Berkel, S S, Verma, A, Owens, R J, McDonough, M A, Walsh, T R, Schofield, C J & Spencer, J 2019, ' Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases ', FEBS Journal, vol. 286, no. 1, pp. 169-183 . https://doi.org/10.1111/febs.14695
Salimraj, R, Hinchliffe, P, Kosmopoulou, M, Tyrrell, J M, Brem, J, van Berkel, S S, Verma, A, Owens, R J, McDonough, M A, Walsh, T R, Schofield, C J & Spencer, J 2019, ' Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases ', FEBS Journal, vol. 286, no. 1, pp. 169-183 . https://doi.org/10.1111/febs.14695
Metallo-β-Lactamases (MBLs) protect bacteria from almost all β-lactam antibiotics. Verona integron-encoded MBL (VIM) enzymes are among the most clinically important MBLs, with VIM-1 increasing in carbapenem-resistant Enterobacteriaceae (Escherichia
Autor:
Christopher J. Schofield
Antibiotic resistance against β-lactams is of paramount therapeutic importance. Although such resistance is known to involve degradation by hydrolysis, the molecular details of what happens next remain unclear. A new study reveals how soil microbes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f5f4d8a4d14ab5c13f2b5f356dba2ca
https://doi.org/10.1038/s41564-018-0181-z
https://doi.org/10.1038/s41564-018-0181-z
Publikováno v:
Chemical record (New York, N.Y.). 18(12)
The 2‐oxoglutarate (2OG) dependent oxygenases were first identified as having roles in the post‐translational modification of procollagen in animals. Subsequently in plants and microbes, they were shown to have roles in the biosynthesis of many s
Autor:
Richard J. Hopkinson, Christopher J. Schofield, Thomas M. Leissing, Md. Saiful Islam, Rasheduzzaman Chowdhury
2-Oxoglutarate (2OG)-dependent oxygenases (2OGXs) catalyze a remarkably diverse range of oxidative reactions. In animals, these comprise hydroxylations and N-demethylations proceeding via hydroxylation; in plants and microbes, they catalyze a wider r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29daae8e96a9395bf85c34b0b6b1f34c
https://doi.org/10.1146/annurev-biochem-061516-044724
https://doi.org/10.1146/annurev-biochem-061516-044724
Autor:
Christopher T. Lohans, Emma van Groesen, Kiran Kumar, Catherine L. Tooke, James Spencer, Robert S. Paton, Jürgen Brem, Christopher J. Schofield
Publikováno v:
Angewandte Chemie International Edition, 130(5), 1296-1299
Lohans, C T, van Groesen, E, Kumar, K, Tooke, C L, Spencer, J, Paton, R S, Brem, J & Schofield, C J 2018, ' A New Mechanism for β-Lactamases : Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation ', Angewandte Chemie-International Edition, vol. 57, no. 5, pp. 1282-1285 . https://doi.org/10.1002/anie.201711308
Angewandte Chemie (International Ed. in English)
Lohans, C T, van Groesen, E, Kumar, K, Tooke, C L, Spencer, J, Paton, R S, Brem, J & Schofield, C J 2018, ' A New Mechanism for β-Lactamases : Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation ', Angewandte Chemie-International Edition, vol. 57, no. 5, pp. 1282-1285 . https://doi.org/10.1002/anie.201711308
Angewandte Chemie (International Ed. in English)
β‐Lactamases threaten the clinical use of carbapenems, which are considered antibiotics of last resort. The classical mechanism of serine carbapenemase catalysis proceeds through hydrolysis of an acyl‐enzyme intermediate. We show that class D β
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85f78e6ee7c2fb8baf97d038cacbfa05
https://doi.org/10.1002/anie.201711308
https://doi.org/10.1002/anie.201711308