Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue

Autor: Charles, RL, Schröder, E, May, G, Free, P, Gaffney, PR, Wait, R, Begum, S, Heads, RJ, Eaton, P

Protein sulfenic acids are reactive intermediates in the catalytic cycles of many enzymes as well as the in formation of other redox states. Sulfenic acid formation is a reversible post-translational modification with potential for protein regulation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::4e6378282a24e0d72bc76f7a1b1b9f3a
https://doi.org/10.1074/mcp.m700065-mcp200

COVID-19 and Toll-Like Receptor 4 (TLR4): SARS-CoV-2 May Bind and Activate TLR4 to Increase ACE2 Expression, Facilitating Entry and Causing Hyperinflammation.

Autor: Aboudounya MM; Department of Cardiology, The Rayne Institute, St Thomas' Hospital, British Heart Foundation Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, UK., Heads RJ; Department of Cardiology, The Rayne Institute, St Thomas' Hospital, British Heart Foundation Centre of Research Excellence, School of Cardiovascular Medicine and Sciences, King's College London, UK.

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Loss of Protein Kinase Novel 1 (PKN1) is associated with mild systolic and diastolic contractile dysfunction, increased phospholamban Thr17 phosphorylation, and exacerbated ischaemia-reperfusion injury.

Autor: Francois AA; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK., Obasanjo-Blackshire K; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK., Clark JE; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK., Boguslavskyi A; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK., Holt MR; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK.; Randall Division of Cell and Molecular Biophysics, King's College London, New Hunt's House, Guy's Hospital Campus, London SE1 1UL, UK., Parker PJ; Division of Cancer Studies, School of Cancer and Pharmaceutical Sciences, Faculty of Life Sciences and Medicine, King's College London, New Hunt's House, Guy's Hospital Campus, London SE1 9RT, UK.; Protein Phosphorylation Laboratory, Francis Crick Institute, Lincoln's Inn Fields, London WC2A 3LY, UK., Marber MS; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK., Heads RJ; Department of Cardiology, School of Cardiovascular Medicine and Sciences, British Heart Foundation Centre for Research Excellence, Faculty of Life Sciences and Medicine, The Rayne Institute, King's College London, St Thomas's Hospital, Lambeth Palace Road, London SE1 7EH, UK.

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Essential but partially redundant roles for POU4F1/Brn-3a and POU4F2/Brn-3b transcription factors in the developing heart.

Autor: Maskell LJ; Medical Molecular Biology Unit, Institute of Cardiovascular Science, University College London, UCL Rayne Building, London, UK., Qamar K; Medical Molecular Biology Unit, Institute of Cardiovascular Science, University College London, UCL Rayne Building, London, UK., Babakr AA; Medical Molecular Biology Unit, Institute of Cardiovascular Science, University College London, UCL Rayne Building, London, UK., Hawkins TA; Division of Biosciences, Cell and Developmental Biology, UCL, London, UK., Heads RJ; Cardiovascular Division, Faculty of Life Sciences and Medicine, King's College London, London, UK., Budhram-Mahadeo VS; Medical Molecular Biology Unit, Institute of Cardiovascular Science, University College London, UCL Rayne Building, London, UK.

Publikováno v: Cell death & disease [Cell Death Dis] 2017 Jun 08; Vol. 8 (6), pp. e2861. Date of Electronic Publication: 2017 Jun 08.

Protein kinase Cε-calcineurin cosignaling downstream of toll-like receptor 4 downregulates fibrosis and induces wound healing gene expression in cardiac myofibroblasts.

Autor: Mesquita RF; Cardiovascular Division, King's College London, Department of Cardiology, The Rayne Institute, St Thomas's Hospital, London, United Kingdom., Paul MA, Valmaseda A, Francois A, Jabr R, Anjum S, Marber MS, Budhram-Mahadeo V, Heads RJ

Publikováno v: Molecular and cellular biology [Mol Cell Biol] 2014 Feb; Vol. 34 (4), pp. 574-94. Date of Electronic Publication: 2013 Dec 02.