Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Inga, Pfeffer"'
Autor:
Lennart Brewitz, Anthony Tumber, Inga Pfeffer, Michael A. McDonough, Christopher J. Schofield
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-14 (2020)
Abstract 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 cell
Externí odkaz:
https://doaj.org/article/86f4a7c44ed5487c8df924d7752ecc2e
Autor:
Inga Pfeffer, Lennart Brewitz, Tobias Krojer, Sacha A. Jensen, Grazyna T. Kochan, Nadia J. Kershaw, Kirsty S. Hewitson, Luke A. McNeill, Holger Kramer, Martin Münzel, Richard J. Hopkinson, Udo Oppermann, Penny A. Handford, Michael A. McDonough, Christopher J. Schofield
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
AspH catalyses hydroxylation of asparagine and aspartate residues in epidermal growth factor-like domains (EGFDs). Here, the authors present crystal structures of AspH with and without substrates and show that AspH uses EFGD substrates with a non-can
Externí odkaz:
https://doaj.org/article/f7e2f575ff5740a38a278f59a178aaca
Autor:
Lennart Brewitz, Anthony Tumber, Inga Pfeffer, Michael A. McDonough, Christopher J. Schofield
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-1 (2020)
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
Externí odkaz:
https://doaj.org/article/0088fcf3a3dd4508a97c17907863ada2
Autor:
Inga Pfeffer, Lennart Brewitz, Yu Nakashima, Michael A. McDonough, Amelia Brasnett, Anthony Tumber, Rasheduzzaman Chowdhury, Christopher J. Schofield
Aspartate/asparagine-β-hydroxylase (AspH) is a human 2-oxoglutarate (2OG) and FeIIoxygenase that catalyses C3 hydroxylations of aspartate/asparagine residues of epidermal growth factor-like domains (EGFDs). Unusually, AspH employs two histidine resi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c4362c38da53d372fa160eb387284f2
https://doi.org/10.1002/anie.202103711
https://doi.org/10.1002/anie.202103711
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
Autor:
Inga Pfeffer, Lennart Brewitz, Anthony Tumber, Christopher J. Schofield, Michael A. McDonough
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-1 (2020)
An amendment to this paper has been published and can be accessed via a link at the top of the paper.
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
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
Autor:
Jürgen Brem, Michael A. McDonough, Sander S. van Berkel, Justin L. P. Benesch, Timothy D. W. Claridge, Christopher J. Schofield, Emily Flashman, Hanna Tarhonskaya, Inga Pfeffer, Anna M. Rydzik, Weston B. Struwe, James Spencer
Publikováno v:
Chemical Science. 6:956-963
Metallo-β-lactamases (MBLs) catalyse the hydrolysis of almost all β-lactam antibiotics. We report biophysical and kinetic studies on the Sao Paulo MBL (SPM-1), which reveal its Zn(II) ion usage and mechanism as characteristic of the clinically impo
Autor:
Martine I. Abboud, Philip Hinchliffe, Jürgen Brem, Robert Macsics, Inga Pfeffer, Anne Makena, Klaus-Daniel Umland, Anna M. Rydzik, Guo-Bo Li, James Spencer, Timothy D. W. Claridge, Christopher J. Schofield
Publikováno v:
Abboud, M I, Hinchliffe, P, Brem, J, Macsics, R, Pfeffer, I, Makena, A, Umland, K-D, Rydzik, A M, Li, G-B, Spencer, J, Claridge, T D W & Schofield, C J 2017, ' 19 F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the São Paulo Metallo-β-Lactamase ', Angewandte Chemie-International Edition, vol. 56, no. 14, pp. 3862–3866 . https://doi.org/10.1002/anie.201612185
Resistance to beta-lactam antibiotics mediated by metallo-beta-lactamases (MBLs) is a growing problem. We describe the use of protein-observe 19F-NMR (PrOF NMR) to study the dynamics of the São Paulo MBL (SPM-1) from beta-lactam- resistant Pseudomon