Functional effects of Epilepsy associated KCNT1 mutations suggest pathogenesis via aberrant inhibitory neuronal activity

Autor: Grigori Y. Rychkov, Zeeshan Shaukat, Chiao Xin Lim, Rashid Hussain, Ben J. Roberts, Claudia M. Bonardi, Guido Rubboli, Brandon F. Meaney, Robyn Whitney, Rikke S. Møller, Michael G. Ricos, Leanne M. Dibbens

Publikováno v: International Journal of Molecular Sciences; Volume 23; Issue 23; Pages: 15133
Rychkov, G Y, Shaukat, Z, Lim, C X, Hussain, R, Roberts, B J, Bonardi, C M, Rubboli, G, Meaney, B F, Whitney, R, Møller, R S, Ricos, M G & Dibbens, L M 2022, ' Functional Effects of Epilepsy Associated KCNT1 Mutations Suggest Pathogenesis via Aberrant Inhibitory Neuronal Activity ', International Journal of Molecular Sciences, vol. 23, no. 23, 15133 . https://doi.org/10.3390/ijms232315133

Refereed/Peer-reviewed KCNT1 (K+ channel subfamily T member 1) is a sodium-activated potassium channel highly expressed in the nervous system which regulates neuronal excitability by contributing to the resting membrane potential and hyperpolarisatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::457184502f6a85b277ecd10eb5f5c133
https://hdl.handle.net/11541.2/32306

HIF-1α and EPAS ubiquitination mediated by the VHL tumour suppressor involves flexibility in the ubiquitination mechanism, similar to other RING E3 ligases

Autor: Ben J Roberts, S Paltoglou

Publikováno v: Oncogene. 26:604-609

Hypoxia-inducible factor 1alpha (HIF-1alpha) degradation under normoxia is critical to modulating vascular growth. This degradation is mediated during normoxia by the von Hippel-Lindau tumour suppressor protein (VHL)-E3 ubiquitin ligase in partnershi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::671e38b346d481a2c560fda432b0daaa
https://doi.org/10.1038/sj.onc.1209818

Role of the C-terminal α-helical domain of the von Hippel–Lindau protein in its E3 ubiquitin ligase activity

Autor: Martin Lewis, Ben J Roberts

Publikováno v: Oncogene. 23:2315-2323

In the present study, the role of the C-terminal alpha-helical domain (amino acid (aa) 195-208) of the von Hippel-Lindau (VHL) tumour suppressor was investigated. Deletions of the VHL C-terminus up to the naturally occurring 195-Gln-Term resulted in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa3b01642c3517ab0ce5613d84fdea2e
https://doi.org/10.1038/sj.onc.1207384

Evidence of Proteasome-mediated Cytochrome P-450 Degradation

Autor: Ben J. Roberts

Publikováno v: Journal of Biological Chemistry. 272:9771-9778

The cytochrome P-450 family of enzymes performs an incredibly diverse range of detoxification and oxidation reactions within the cell and constitutes between 5 and 10% of protein in hepatic endoplasmic reticulum. In this report it is demonstrated tha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daa0cebc6029c9c185a3a849b671c7fd
https://doi.org/10.1074/jbc.272.15.9771

Role of the von Hippel-Lindau tumour suppressor protein in the regulation of HIF-1alpha and its oxygen-regulated transactivation domains at high cell density

Autor: Ben J Roberts, Steve M Paltoglou

Publikováno v: Oncogene. 24(23)

Hypoxia-inducible factor-1alpha (HIF-1alpha) induction and associated transcription were investigated during high cell density, focusing on the negative regulator of HIF-1alpha expression, the von Hippel-Lindau (VHL) protein. In 293T and HeLa cells,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2f4c1e411865a1b7a92ade2a8d9bdf6
https://pubmed.ncbi.nlm.nih.gov/15750626