Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Evy Mayeur"'
Autor:
Ewa Sieliwonczyk, Bert Vandendriessche, Charlotte Claes, Evy Mayeur, Maaike Alaerts, Philip Holmgren, Tycho Canter Cremers, Dirk Snyders, Bart Loeys, Dorien Schepers
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-13 (2023)
Abstract Despite numerous prior attempts to improve knock-in (KI) efficiency, the introduction of precise base pair substitutions by the CRISPR-Cas9 technique in zebrafish remains challenging. In our efforts to generate KI zebrafish models of human C
Externí odkaz:
https://doaj.org/article/a80db3a6daa9481ea82d1423965402c5
Autor:
Elke Bocksteins, Evy Mayeur, Abbi Van Tilborg, Glenn Regnier, Jean-Pierre Timmermans, Dirk J Snyders
Publikováno v:
PLoS ONE, Vol 9, Iss 6, p e98960 (2014)
The "silent" voltage-gated potassium (KvS) channel subunit Kv6.4 does not form electrically functional homotetramers at the plasma membrane but assembles with Kv2.1 subunits, generating functional Kv2.1/Kv6.4 heterotetramers. The N-terminal T1 domain
Externí odkaz:
https://doaj.org/article/0de902eff1da494a98fce8b9ce8f4bfe
Autor:
Nicolas De Neuter, Luis G. Cuello, Evy Mayeur, Laura C. Coonen, Dirk J. Snyders, Alain J. Labro
Publikováno v:
Biophysical Journal
Biophysical journal
BIOPHYSICAL JOURNAL
Biophysical journal
BIOPHYSICAL JOURNAL
Voltage-gated potassium (Kv) channels display several types of inactivation processes, including N-, C-, and U-types. C-type inactivation is attributed to a nonconductive conformation of the selectivity filter (SF). It has been proposed that the acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::600c0756952c6e32628770b29718eec9
https://doi.org/10.1016/j.bpj.2020.03.032
https://doi.org/10.1016/j.bpj.2020.03.032
Publikováno v:
Molecular and Cellular Neuroscience. 24:357-366
The beta-subunits of the KChIP family modulate properties and expression level of Kv4 channels. We report the cloning of the first splice variant of KChIP1 (KChIP1b) which contains an extra exon, rich in aromatic residues, in the amino terminus. Both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae3080922769c3eabefea3782bd5807c
https://doi.org/10.1016/s1044-7431(03)00174-x
https://doi.org/10.1016/s1044-7431(03)00174-x
Autor:
Dirk J. Snyders, Alain J. Labro, Gildas Loussouarn, Adam Raes, Inge R. Boulet, Tine Bruyns, Frank S. Choveau, Evy Mayeur
Publikováno v:
Journal of biological chemistry
In vivo, KCNQ1 α-subunits associate with the β-subunit KCNE1 to generate the slowly activating cardiac potassium current (I(Ks)). Structurally, they share their topology with other Kv channels and consist out of six transmembrane helices (S1-S6) wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76d712c0041f5085527d8a2f54787aaf
https://hdl.handle.net/10067/880450151162165141
https://hdl.handle.net/10067/880450151162165141
Autor:
Evy Mayeur, Tine Bruyns, Dirk Adriaensen, Elke Bocksteins, Jean-Pierre Timmermans, Alain J. Labro, Dirk J. Snyders
Publikováno v:
Journal of biological chemistry
Voltage-gated potassium (Kv) channels are transmembrane tetramers of individual α-subunits. Eight different Shaker-related Kv subfamilies have been identified in which the tetramerization domain T1, located on the intracellular N terminus, facilitat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cd676d5a9b0a4761039a60d16568b9a
https://hdl.handle.net/10067/799460151162165141
https://hdl.handle.net/10067/799460151162165141
Publikováno v:
Biophysical Journal. 100:348a
Silent Kv (KvS) subunits (Kv6-9) do not form functional channels in homotetrameric configuration but assemble with members of the Kv2 subfamily generating functional heterotetrameric Kv2/KvS channel complexes. In case of the functional subfamilies (K
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1883438968bccf8a0aa856eed23726a9
https://doi.org/10.1016/j.bpj.2010.12.2098
https://doi.org/10.1016/j.bpj.2010.12.2098
Publikováno v:
Biophysical Journal. 98:338a
The long QT syndrome is a cardiac disorder caused by a delayed ventricular repolarization. LQT1 is linked to mutations in the KCNQ1 gene that codes for the six transmembrane spanning α-subunit of the channel complex that underlies IKsin vivo. The LQ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0a0f5004976b05a4ba69242ca76d3c1
https://doi.org/10.1016/j.bpj.2009.12.1833
https://doi.org/10.1016/j.bpj.2009.12.1833
Publikováno v:
Biophysical Journal. 96:174a
Voltage-gated potassium (Kv) channels are tetramers of four α-subunits. Formation of homo- or heterotetramers is determined by their subfamily specific N-terminal T1 domain. This domain contains two regions designated A and B box, which display a pa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1a5bf14da79f0137e21e5c85421c53e
https://doi.org/10.1016/j.bpj.2008.12.805
https://doi.org/10.1016/j.bpj.2008.12.805
Publikováno v:
Biophysical Journal. (2):465a-466a
Fully assembled voltage-gated potassium (Kv) channel are tetramers of α-subunits. The silent (KvS) channel subunits (Kv5-9) do not form functional homotetramers due to retention in the endoplasmic reticulum (ER). This ER retention is relieved by ass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::814e9b32909da2ef2ad5c6dc85398715