Zobrazeno 1 - 10
of 102
pro vyhledávání: '"Peter C E Moody"'
Autor:
Neil Bate, Christos G Savva, Peter C E Moody, Edward A Brown, Sian E Evans, Jonathan K Ball, John W R Schwabe, Julian E Sale, Nicholas P J Brindle
Publikováno v:
PLoS Pathogens, Vol 18, Iss 7, p e1010733 (2022)
Emerging SARS-CoV-2 variants are creating major challenges in the ongoing COVID-19 pandemic. Being able to predict mutations that could arise in SARS-CoV-2 leading to increased transmissibility or immune evasion would be extremely valuable in develop
Externí odkaz:
https://doaj.org/article/1c450b5c20754a42910056edeab3abf1
Autor:
Sofia M. Kapetanaki, Mark J. Burton, Jaswir Basran, Chiasa Uragami, Peter C. E. Moody, John S. Mitcheson, Ralf Schmid, Noel W. Davies, Pierre Dorlet, Marten H. Vos, Nina M. Storey, Emma Raven
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Despite being highly toxic, carbon monoxide (CO) is also essential as an intracellular signalling molecule, but CO-dependent signalling is poorly understood. Here, authors employ spectroscopic and electrophysiology methods and find that CO activates
Externí odkaz:
https://doaj.org/article/443ba616a4bf488fa3708f48abac1594
Autor:
Hanna Kwon, Jaswir Basran, Cecilia M. Casadei, Alistair J. Fielding, Tobias E. Schrader, Andreas Ostermann, Juliette M. Devos, Pierre Aller, Matthew P. Blakeley, Peter C. E. Moody, Emma L. Raven
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-6 (2016)
The nature of the ferryl intermediate generated in reactions catalysed by heme-containing enzymes is uncertain, due to the ambiguity of X-ray crystallography data. Here, the authors apply neutron diffraction, kinetics and other spectroscopy to direct
Externí odkaz:
https://doaj.org/article/ba0cf1877308498b991c38c8062c0431
Autor:
Prof.Dr. Peter C. E. Moody, Adnan Ayna
Publikováno v:
Biochemistry and Cell Biology. 98:518-524
The glycolytic pathway of the enteric pathogen Campylobacter jejuni is incomplete; the absence of phosphofructokinase means that the suppression of futile cycling at this point in the glycolytic–gluconeogenic pathway might not be required, and ther
Autor:
Sofia M. Kapetanaki, Mark J. Burton, Jaswir Basran, Chiasa Uragami, Peter C. E. Moody, John S. Mitcheson, Ralf Schmid, Noel W. Davies, Pierre Dorlet, Marten H. Vos, Nina M. Storey, Emma Raven
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-1 (2018)
The originally published version of this article contained an error in the subheading ‘Heme is required for CO-dependent channel activation’, which was incorrectly given as ‘Hame is required for CO-dependent channel activation’. This has now
Externí odkaz:
https://doaj.org/article/112dfef6f2674e25b9fc4f30441b3d46
Autor:
Mehul H. Jesani, Jonathan Clayden, Laura P. Campbell, Sarah J. Thackray, Jaswir Basran, Peter C. E. Moody, Emma Lloyd Raven, Elizabeth S. Booth, Christopher G. Mowat, Hanna Kwon
Publikováno v:
Basran, J, Booth, E S, Campbell, L P, Thackray, S J, Jesani, M H, Clayden, J, Moody, P C E, Mowat, C G, Kwon, H & Raven, E L 2021, ' Binding of L-kynurenine to X. campestris tryptophan 2,3-dioxygenase ', Journal of Inorganic Biochemistry, vol. 225, 111604 . https://doi.org/10.1016/j.jinorgbio.2021.111604
The kynurenine pathway is the major route of tryptophan metabolism. The first step of this pathway is catalysed by one of two heme-dependent dioxygenase enzymes – tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) – leading in
Autor:
Umakhanth Venkatraman Girija, Emma Lloyd Raven, Alistair J. Fielding, Louise Fairall, Dimitri A. Svistunenko, Samuel L. Freeman, Charalambos P. Kyriacou, Gary Parkin, Nicola Portolano, Peter C. E. Moody, Hanna Kwon, Jaswir Basran, John W.R. Schwabe
Publikováno v:
Freeman, S L, Kwon, H, Portolano, N, Parkin, G, Girija, U V, Basran, J, Fielding, A J, Fairall, L, Svistuneko, D A, Moody, P C E, Schwabe, J W R, Kyriacou, C P & Raven, E 2019, ' Heme binding to human CLOCK affects interactions with the E-box ', Proceedings of the National Academy of Sciences of the United States of America, vol. 116, no. 40, pp. 19911-19916 . https://doi.org/10.1073/pnas.1905216116
The file attached to this record is the author's final peer reviewed version. The Publisher's final version can be found by following the DOI link. The circadian clock is an endogenous time-keeping system that is ubiquitous in animals and plants as w
Autor:
Chinar Pathak, Takehiko Tosha, Hitomi Sawai, Mahdi Hussain, Hiroshi Sugimoto, Yoshitsugu Shiro, Natalia Stefanou, Hironori Murakami, Anna J Bailey, Go Ueno, Keitaro Yamashita, Kunio Hirata, Alistair J. Fielding, Jaswir Basran, Masaki Yamamoto, Samuel L. Freeman, Hazel A. Sparkes, Kensuke Tono, Peter C. E. Moody, Hanna Kwon, Hideo Ago, Emma Lloyd Raven
Publikováno v:
Angewandte Chemie (International Ed. in English)
Kwon, H, Basran, J, Pathak, C, Hussain, M, Freeman, S L, Fielding, A, Bailey, A, Stefanou, N, Sparkes, H A, Tosha, T, Yamashita, K, Hirata, K, Murakami, H, Ueno, G, Ago, H, Tono, K, Yamamoto, M, Sawai, H, Shiro, Y, Sugimoto, H, Raven, E & Moody, P 2021, ' XFEL Crystal Structures of Peroxidase Compound II ', Angewandte Chemie-International Edition, vol. 60, no. 26, pp. 14578-14585 . https://doi.org/10.1002/anie.202103010
Kwon, H, Basran, J, Pathak, C, Hussain, M, Freeman, S L, Fielding, A, Bailey, A, Stefanou, N, Sparkes, H A, Tosha, T, Yamashita, K, Hirata, K, Murakami, H, Ueno, G, Ago, H, Tono, K, Yamamoto, M, Sawai, H, Shiro, Y, Sugimoto, H, Raven, E & Moody, P 2021, ' XFEL Crystal Structures of Peroxidase Compound II ', Angewandte Chemie-International Edition, vol. 60, no. 26, pp. 14578-14585 . https://doi.org/10.1002/anie.202103010
Oxygen activation in all heme enzymes requires the formation of high oxidation states of iron, usually referred to as ferryl heme. There are two known intermediates: Compound I and Compound II. The nature of the ferryl heme—and whether it is an FeI
Autor:
Tobias E. Schrader, Reynier Suardíaz, Marc W. van der Kamp, Matthew P. Blakeley, Andreas Ostermann, Jaswir Basran, Hanna Kwon, Adrian J. Mulholland, Juliette M. Devos, Emma Lloyd Raven, Peter C. E. Moody
Publikováno v:
Kwon, H, Basran, J, Devos, J M, Suardiaz Del Rio, R, Van Der Kamp, M W, Mulholland, A J, Schrader, T E, Ostermann, A, Blakeley, M P, Moody, P C E & Raven, E 2020, ' Visualizing the protons in a metalloenzyme electron proton transfer pathway ', Proceedings of the National Academy of Sciences of the United States of America . https://doi.org/10.1073/pnas.1918936117
Proceedings of the National Academy of Sciences of the United States of America 117(12), 6484-6490 (2020). doi:10.1073/pnas.1918936117
Proc Natl Acad Sci U S A
Proceedings of the National Academy of Sciences of the United States of America 117(12), 6484-6490 (2020). doi:10.1073/pnas.1918936117
Proc Natl Acad Sci U S A
In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including resp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d5d0c60b8dad118e90a1a4953bb4391
https://research-information.bris.ac.uk/en/publications/1fb08f30-b3f4-4c9c-8b9c-70b658dc8784
https://research-information.bris.ac.uk/en/publications/1fb08f30-b3f4-4c9c-8b9c-70b658dc8784
Autor:
Adnan, Ayna, Peter C E, Moody
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 98(4)
The glycolytic pathway of the enteric pathogen