S ‐glutathiolation impairs phosphoregulation and function of cardiac myosin‐binding protein C in human heart failure

Autor: Angelika Piasecki, Florian Richter, Sonia Donzelli, Friederike Cuello, Dobromir Dobrev, Sakthivel Sadayappan, Juliana Heidler, Niels Voigt, Lucie Carrier, Paul J.M. Wijnker, Jolanda van der Velden, Thomas Eschenhagen, Konstantina Stathopoulou, Ilka Wittig, Simon Diering, Friedrich Buck, Philip Eaton, Ewald Schröder

Publikováno v: Stathopoulou, K, Wittig, I, Heidler, J, Piasecki, A, Richter, F, Diering, S, van der Velden, J, Buck, F, Donzelli, S, Schroder, E, Wijnker, P J M, Voigt, N, Dobrev, D, Sadayappan, S, Eschenhagen, T, Carrier, L, Eaton, P & Cuello, F 2016, ' S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure ', FASEB Journal, vol. 30, no. 5, pp. 1849-1864 . https://doi.org/10.1096/fj.201500048
FASEB Journal, 30(5), 1849-1864. FASEB

Cardiac myosin-binding protein C (cMyBP-C) regulates actin-myosin interaction and thereby cardiac myocyte contraction and relaxation. This physiologic function is regulated by cMyBP-C phosphorylation. In our study, reduced site-specific cMyBP-C phosp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::598da15ac9489b51ac8b9213e6494ed5
https://doi.org/10.1096/fj.201500048

Glyceraldehyde 3-Phosphate Dehydrogenase is Unlikely to Mediate Hydrogen Peroxide Signaling: Studies with a Novel Anti-Dimedone Sulfenic Acid Antibody

Autor: Philip Eaton, Ewald Schröder, Claire Maller

Publikováno v: Antioxidants & Redox Signaling. 14:49-60

Protein sulfenic acids (SOHs) are the principal oxidation products formed when redox active proteins interact with peroxide molecules. We have developed a new antibody reagent that detects protein SOHs derivatized with dimedone. Using this new antibo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30193c0c7a1e4f7daa39c203af66b4d2
https://doi.org/10.1089/ars.2010.3149

The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid ofPseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase. Corrigendum

Autor: Michail N. Isupov, Ewald Schröder, Robert P. Gibson, Jean Beecher, Giuliana Donadio, Vahid Saneei, Stephlina A. Dcunha, Emma J. McGhie, Christopher Sayer, Colin F. Davenport, Peter C. K. Lau, Yoshie Hasegawa, Hiroaki Iwaki, Maria Kadow, Kathleen Balke, Uwe T. Bornscheuer, Gleb Bourenkov, Jennifer A. Littlechild

Publikováno v: Acta Crystallographica Section D: Biological Crystallography

The first crystal structure of a type II Baeyer–Villiger monooxygenase reveals a different ring orientation of its FMN cofactor compared with other related bacterial luciferase-family enzymes.
The three-dimensional structures of the native enz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6aa843ea99d761ede5c50e0c6b6954c
https://doi.org/10.1107/s205979831800150x

Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: issues and considerations

Autor: Philip Eaton, Ewald Schröder

Publikováno v: Current Opinion in Pharmacology. 8:153-159

Exogenous H(2)O(2) is widely applied to cardiovascular tissues in order to elicit oxidant-dependent responses relevant to signalling and disease. Lower levels of endogenous H(2)O(2) are essential for normal physiological functioning and signalling, w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89f84076d196173f6364aa6e71581f3b
https://doi.org/10.1016/j.coph.2007.12.012

The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: The first crystal structure of a type II Baeyer-Villiger monooxygenase

Autor: Peter C. K. Lau, Maria Kadow, Ewald Schröder, Yoshie Hasegawa, Colin F. Davenport, Robert P. Gibson, Michail N. Isupov, Uwe T. Bornscheuer, Hiroaki Iwaki, Gleb Bourenkov, Emma J. McGhie, C. Sayer, Jennifer A. Littlechild, Vahid Saneei, Stephlina A. Dcunha, Kathleen Balke, Jean Beecher, Giuliana Donadio

The three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer–Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 Å resolution. The structur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6aa144fa1c8813760ab2ed1108cd1cf0
https://doi.org/10.1107/s1399004715017939