Výsledky vyhledávání - "Peter C. E. Moody"

Akademický článek

A mechanism for CO regulation of ion channels

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

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Akademický článek

Direct visualization of a Fe(IV)–OH intermediate in a heme enzyme

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

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Akademický článek

Author Correction: A mechanism for CO regulation of ion channels

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

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Activity of fructose-1,6-bisphosphatase fromCampylobacter jejuni

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7434adbc8f75f9900746ce471ce0154a
https://doi.org/10.1139/bcb-2020-0021

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In vitro evolution predicts emerging SARS-CoV-2 mutations with high affinity for ACE2 and cross-species binding

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. 18(7)

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://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d1da5381f98f865f0fa99a86f842472
https://pubmed.ncbi.nlm.nih.gov/35849637

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Binding of l-kynurenine to X. campestris tryptophan 2,3-dioxygenase

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c9ed062898cb8f82251351b97a81a35
https://pubmed.ncbi.nlm.nih.gov/34571402

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Heme binding to human CLOCK affects interactions with the E-box

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a24f39680f6f48b410fef70ef5d4af8
https://doi.org/10.1073/pnas.1905216116

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XFEL Crystal Structures of Peroxidase Compound II

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

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::274c64c946e8e8a80b583b50ae0c4129
https://pubmed.ncbi.nlm.nih.gov/33826799

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Visualizing the protons in a metalloenzyme electron proton transfer pathway

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

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

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