The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-terminal domain, altering its interaction with the cardiac ryanodine receptor

Autor: Anders B. Sorensen, C. Holt, Louise Hamborg, Reinhard Wimmer, K.T. Larsen, Michael Toft Overgaard, Filip Van Petegem, Cordula Sommer, Kelvin Lau, Malene Brohus

Publikováno v: J Biol Chem
Holt, C, Hamborg, L, Lau, K, Brohus, M, Sørensen, A B, Larsen, K T, Sommer, C, Van Petegem, F, Overgaard, M T & Wimmer, R 2020, ' The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-terminal domain, altering its interaction with the cardiac ryanodine receptor ', Journal of Biological Chemistry, vol. 295, no. 22, pp. 7620-7634 . https://doi.org/10.1074/jbc.RA120.013430

Mutations in the genes encoding the highly conserved Ca(2+)-sensing protein calmodulin (CaM) cause severe cardiac arrhythmias, including catecholaminergic polymorphic ventricular tachycardia or long QT syndrome and sudden cardiac death. Most of the i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15d740d2e915a5876f44f8917526b378
https://europepmc.org/articles/PMC7261784/

Allostery in Coagulation Factor VIIa Revealed by Ensemble Refinement of Crystallographic Structures

Autor: Thomas M. Frimurer, Michael Toft Overgaard, Prafull S. Gandhi, Ole Hvilsted Olsen, Jesper J. Madsen, Egon Persson, Anders B. Sorensen

Publikováno v: Sorensen, A B, Madsen, J J, Frimurer, T M, Overgaard, M T, Gandhi, P S, Persson, E & Olsen, O H 2019, ' Allostery in Coagulation Factor VIIa Revealed by Ensemble Refinement of Crystallographic Structures ', Biophysical Journal, vol. 116, no. 10, pp. 1823-1835 . https://doi.org/10.1016/j.bpj.2019.03.024
Biophys J

A critical step in injury-induced initiation of blood coagulation is the formation of the complex between the trypsin-like protease coagulation factor VIIa (FVIIa) and its cofactor tissue factor (TF), which converts FVIIa from an intrinsically poor e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f8ce586891e7184709a138ab69bfee5
https://vbn.aau.dk/da/publications/404c1613-91d7-427d-8332-8c6af461eb9d

Calmodulin mutations causing catecholaminergic polymorphic ventricular tachycardia confer opposing functional and biophysical molecular changes

Autor: Claus Oxvig, Sara Linse, Anders B. Sorensen, Michael Toft Overgaard, Kasper Kjaer-Sorensen, Mads Toft Søndergaard, Louise L. Skov, Mette Nyegaard, Mikael C. Bauer

Publikováno v: Søndergaard, M T, Sorensen, A B, Skov, L L, Kjaer-Sorensen, K, Bauer, M C, Nyegaard, M, Linse, S, Oxvig, C & Overgaard, M T 2015, ' Calmodulin mutations causing catecholaminergic polymorphic ventricular tachycardia confer opposing functional and biophysical molecular changes ', F E B S Journal, vol. 282, no. 4, pp. 803-816 . https://doi.org/10.1111/febs.13184

Calmodulin (CaM)(1) is the central mediator of intracellular Ca(2+) signalling in cardiomyocytes, where it conveys the intricate Ca(2+) transients to the proteins controlling cardiac contraction. We recently linked two separate mutations in CaM (N53I

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56140de031d3422902ff32200880914b
https://doi.org/10.1111/febs.13184

Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-Mediated Allosteric Regulation of Factor VIIa Activity

Autor: Michael Toft Overgaard, Ole Hvilsted Olsen, Anette A. Pedersen, Anders B. Sorensen, Jesper J. Madsen, Prafull S. Gandhi, L. Anders Svensson, Henrik Østergaard

Publikováno v: Sorensen, A B, Madsen, J J, Svensson, L A, Pedersen, A A, Østergaard, H, Overgaard, M T, Olsen, O H & Gandhi, P S 2016, ' Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-Mediated Allosteric Regulation of Factor VIIa Activity ', Journal of Biological Chemistry, vol. 291, pp. 4671-4683 . https://doi.org/10.1074/jbc.M115.698613
Sorensen, A B, Madsen, J J, Svensson, L A, Pedersen, A A, Østergaard, H, Overgaard, M T, Olsen, O H & Gandhi, P S 2016, ' Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa Activity ', Journal of Biological Chemistry, vol. 291, no. 9, pp. 4671-4683 . https://doi.org/10.1074/jbc.M115.698613

The complex of coagulation factor VIIa (FVIIa), a trypsin-like serine protease, and membrane-bound tissue factor (TF) initiates blood coagulation upon vascular injury. Binding of TF to FVIIa promotes allosteric conformational changes in the FVIIa pro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bff5a8d6ff4ba5dc6e1519550a623859
https://vbn.aau.dk/da/publications/e409dda5-e539-4497-8252-d6b85807874f

Monitoring the Early Stage Self-Assembly of Enzyme-Assisted Peptide Hydrogels

Autor: Anders B. Sorensen, Richard J. Williams, James Gardiner, Keith M. McLean, Silvia Marchesan, Patrick G. Hartley, Roger J. Mulder

Publikováno v: Australian Journal of Chemistry. 66:572

The early stages of the self-assembly of peptide hydrogels largely determine their final material properties. Here we discuss experimental methodologies for monitoring the self-assembly kinetics which underpin peptide hydrogel formation. The early st

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0362ed416fb6156508263b2c92508360
https://doi.org/10.1071/ch12557