Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Michal Cagalinec"'
Autor:
Mailis Liiv, Annika Vaarmann, Dzhamilja Safiulina, Vinay Choubey, Ruby Gupta, Malle Kuum, Lucia Janickova, Zuzana Hodurova, Michal Cagalinec, Akbar Zeb, Miriam A. Hickey, Yi-Long Huang, Nana Gogichaishvili, Merle Mandel, Mario Plaas, Eero Vasar, Jens Loncke, Tim Vervliet, Ting-Fen Tsai, Geert Bultynck, Vladimir Veksler, Allen Kaasik
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract Wolfram syndrome is a rare genetic disease caused by mutations in the WFS1 or CISD2 gene. A primary defect in Wolfram syndrome involves poor ER Ca2+ handling, but how this disturbance leads to the disease is not known. The current study, per
Externí odkaz:
https://doaj.org/article/7119060b6c6844ed9cd995417943a2ed
Autor:
Michal Cagalinec, Alexandra Zahradníková, Dominika Kováčová, Ludovit Paulis, Simona Kureková, Matej Hot’ka, Jana Pavelková, Mario Plaas, Marta Novotová, Ivan Zahradník
Publikováno v:
Frontiers in Physiology, Vol 10 (2019)
Wolframin (Wfs1) is a membrane protein of the sarco/endoplasmic reticulum. Wfs1 mutations are responsible for the Wolfram syndrome, characterized by diabetic and neurological symptoms. Although Wfs1 is expressed in cardiac muscle, its role in this ti
Externí odkaz:
https://doaj.org/article/45199483757148e68b928411f9acc7f1
Autor:
Michal Cagalinec, Mailis Liiv, Zuzana Hodurova, Miriam Ann Hickey, Annika Vaarmann, Merle Mandel, Akbar Zeb, Vinay Choubey, Malle Kuum, Dzhamilja Safiulina, Eero Vasar, Vladimir Veksler, Allen Kaasik
Publikováno v:
PLoS Biology, Vol 14, Iss 7, p e1002511 (2016)
Deficiency of the protein Wolfram syndrome 1 (WFS1) is associated with multiple neurological and psychiatric abnormalities similar to those observed in pathologies showing alterations in mitochondrial dynamics. The aim of this study was to examine th
Externí odkaz:
https://doaj.org/article/cc6c71332b70484f82f9d2c57bdc9e10
Publikováno v:
General physiology and biophysics. 39(5)
In previously introduced rat model of Wolfram syndrome, we have shown that in cardiac myocytes lacking functional wolframin protein the calcium transients and contractile response are significantly changed. Therefore, in this model, we evaluated prot
Publikováno v:
Sci Signal
L-type voltage-gated Ca(2+) channels (LTCCs) are implicated in neurodegenerative processes and cell death. Accordingly, LTCC antagonists have been proposed to be neuroprotective although this view is disputed, because intentional LTCC activation can
Autor:
Janine Ebner, Helmut Kubista, Petra L. Szabo, Bruno K. Podesser, Livia C. Hool, Karlheinz Hilber, Hannes Todt, Attila Kiss, Xaver Koenig, Michal Cagalinec, Henrietta Cserne Szappano
Publikováno v:
Biophysical Journal. 118:105a-106a
Autor:
Janine, Ebner, Michal, Cagalinec, Helmut, Kubista, Hannes, Todt, Petra L, Szabo, Attila, Kiss, Bruno K, Podesser, Henrietta, Cserne Szappanos, Livia C, Hool, Karlheinz, Hilber, Xaver, Koenig
Publikováno v:
Pflugers Archiv
Neuronal nitric oxide synthase (nNOS) is considered a regulator of Cav1.2 L-type Ca2+ channels and downstream Ca2+ cycling in the heart. The commonest view is that nitric oxide (NO), generated by nNOS activity in cardiomyocytes, reduces the currents
Publikováno v:
Cytometry Part A
Cytometry
Cytometry
Naturally occurring endogenous fluorescence of flavins, arising in response to excitation by visible light, offers broad opportunity to investigate mitochondrial metabolic state directly in living cells and tissues, including in clinical settings. Ho
Publikováno v:
Multiphoton Microscopy in the Biomedical Sciences XVIII
Multimodal optical imaging of suspected tissues is showing to be a promising method for distinguishing suspected cancerous tissues from healthy ones. In particular, the combination of steady-state spectroscopic methods with timeresolved fluorescence
Autor:
Michal Cagalinec, Eeva-Liisa Eskelinen, Tahira Anwar, Miriam A Hickey, Vinay Choubey, Dzhamilja Safiulina, Malle Kuum, Joanna Liiv, Mailis Liiv, Allen Kaasik
Publikováno v:
Autophagy
The autophagy protein BECN1/Beclin 1 is known to play a central role in autophagosome formation and maturation. The results presented here demonstrate that BECN1 interacts with the Parkinson disease-related protein PARK2. This interaction does not re