Phenotype Distinctions in Mice Deficient in the Neuron-Specific α3 Subunit of Na,K-ATPase: Atp1a 3 ^tm1Ling/+ and Atp1a3 ^+/D801Y .

Autor: Liu YB; Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts 02114., Arystarkhova E; Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts 02114.; Harvard Medical School, Boston, Massachusetts 02115., Sacino AN; Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts 02114., Szabari MV; Department Anesthesia, Massachusetts General Hospital, Boston, Massachusetts 02114., Lutz CM; The Jackson Laboratory, Bar Harbor, Maine 04609., Terrey M; The Jackson Laboratory, Bar Harbor, Maine 04609., Morsci NS, Jakobs TC; Harvard Medical School, Boston, Massachusetts 02115.; Department of Ophthalmology, Massachusetts Eye and Ear Infirmary/Schepens Eye Research Institute, Harvard Medical School, Boston, Massachusetts 02114., Lykke-Hartmann K; Department of Biomedicine, Aarhus University, Aarhus 8000, Denmark., Brashear A; Department of Neurology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York 14203., Napoli E; Department of Neurology, University of California Davis School of Medicine, Sacramento, California 95817., Sweadner KJ; Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts 02114 ksweadner@mgh.harvard.edu.; Harvard Medical School, Boston, Massachusetts 02115.

Publikováno v: ENeuro [eNeuro] 2024 Aug 28; Vol. 11 (8). Date of Electronic Publication: 2024 Aug 28 (Print Publication: 2024).

The FXYD1 protein plays a protective role against pulmonary hypertension and arterial remodeling via redox and inflammatory mechanisms.

Autor: Hansen TS; Kolling Institute, University of Sydney, Sydney, New South Wales, Australia.; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia., Karimi Galougahi K; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia., Tang O; Kolling Institute, University of Sydney, Sydney, New South Wales, Australia.; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia., Tsang M; Kolling Institute, University of Sydney, Sydney, New South Wales, Australia.; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia., Scherrer-Crosbie M; Perelman School of Medicine, The Hospital of the University of Pennsylvania, Philadelphia, Pennsylvania, United States., Arystarkhova E; Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts, United States., Sweadner K; Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts, United States., Bursill C; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia.; Vascular Research Centre, South Australian Health and Medical Research Institute, Adelaide, South Australia, Australia., Bubb KJ; Kolling Institute, University of Sydney, Sydney, New South Wales, Australia.; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia.; Biomedicine Discovery Institute and Victorian Heart Institute, Monash University Faculty of Medicine, Nursing and Health Sciences, Clayton, Victoria, Australia., Figtree GA; Kolling Institute, University of Sydney, Sydney, New South Wales, Australia.; Faculty of Medicine and Health, University of Sydney, Sydney, New South Wales, Australia.

Publikováno v: American journal of physiology. Heart and circulatory physiology [Am J Physiol Heart Circ Physiol] 2024 Mar 01; Vol. 326 (3), pp. H623-H635. Date of Electronic Publication: 2023 Dec 22.

Misfolding, altered membrane distributions, and the unfolded protein response contribute to pathogenicity differences in Na,K-ATPase ATP1A3 mutations.

Autor: Arystarkhova E; Laboratory of Membrane Biology, Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts, USA; Department of Neurology, Massachusetts General Hospital, Boston, Massachusetts, USA. Electronic address: aristarkhova@helix.mgh.harvard.edu., Ozelius LJ; Department of Neurology, Massachusetts General Hospital, Boston, Massachusetts, USA., Brashear A; Department of Medicine, University of California at Davis Medical School, Sacramento, California, USA., Sweadner KJ; Laboratory of Membrane Biology, Department of Neurosurgery, Massachusetts General Hospital, Boston, Massachusetts, USA; Department of Neurology, Massachusetts General Hospital, Boston, Massachusetts, USA. Electronic address: sweadner@helix.mgh.harvard.edu.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2021 Jan-Jun; Vol. 296, pp. 100019. Date of Electronic Publication: 2020 Nov 22.

Genotype-structure-phenotype relationships diverge in paralogs ATP1A1 , ATP1A2 , and ATP1A3 .

Autor: Sweadner KJ; Department of Neurosurgery (K.J. Sweadner, E.A., J.T.P.), Center for Human Genetics Research (K.J. Swoboda), and Department of Neurology, (K.J. Swoboda, L.J.O.) Massachusetts General Hospital, Boston; and the Department of Neurology (A.B.), Wake Forest School of Medicine, Winston-Salem, NC., Arystarkhova E; Department of Neurosurgery (K.J. Sweadner, E.A., J.T.P.), Center for Human Genetics Research (K.J. Swoboda), and Department of Neurology, (K.J. Swoboda, L.J.O.) Massachusetts General Hospital, Boston; and the Department of Neurology (A.B.), Wake Forest School of Medicine, Winston-Salem, NC., Penniston JT; Department of Neurosurgery (K.J. Sweadner, E.A., J.T.P.), Center for Human Genetics Research (K.J. Swoboda), and Department of Neurology, (K.J. Swoboda, L.J.O.) Massachusetts General Hospital, Boston; and the Department of Neurology (A.B.), Wake Forest School of Medicine, Winston-Salem, NC., Swoboda KJ; Department of Neurosurgery (K.J. Sweadner, E.A., J.T.P.), Center for Human Genetics Research (K.J. Swoboda), and Department of Neurology, (K.J. Swoboda, L.J.O.) Massachusetts General Hospital, Boston; and the Department of Neurology (A.B.), Wake Forest School of Medicine, Winston-Salem, NC., Brashear A; Department of Neurosurgery (K.J. Sweadner, E.A., J.T.P.), Center for Human Genetics Research (K.J. Swoboda), and Department of Neurology, (K.J. Swoboda, L.J.O.) Massachusetts General Hospital, Boston; and the Department of Neurology (A.B.), Wake Forest School of Medicine, Winston-Salem, NC., Ozelius LJ; Department of Neurosurgery (K.J. Sweadner, E.A., J.T.P.), Center for Human Genetics Research (K.J. Swoboda), and Department of Neurology, (K.J. Swoboda, L.J.O.) Massachusetts General Hospital, Boston; and the Department of Neurology (A.B.), Wake Forest School of Medicine, Winston-Salem, NC.

Publikováno v: Neurology. Genetics [Neurol Genet] 2019 Feb 04; Vol. 5 (1), pp. e303. Date of Electronic Publication: 2019 Feb 04 (Print Publication: 2019).

Біотестування промислових токсикантів на основі порушень поведінки білих мишей (Mus musculus L.)

Autor: Arystarkhova, E., Palii, I., Shubovych, L., Mashehova, A.

У статті розглядається можливість застосування лабораторних тварин (Mus musculus L.) для біотестування найбільш небезпечних промислових токс

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3109::803a542b8cb131daae9c8500080be9cd
http://ir.znau.edu.ua/handle/123456789/6970