Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nina Larisch"'
Autor:
Margherita Festa, Velia Minicozzi, Anna Boccaccio, Laura Lagostena, Antonella Gradogna, Tianwen Qi, Alex Costa, Nina Larisch, Shin Hamamoto, Emanuela Pedrazzini, Stefan Milenkovic, Joachim Scholz-Starke, Matteo Ceccarelli, Alessandro Vitale, Petra Dietrich, Nobuyuki Uozumi, Franco Gambale, Armando Carpaneto
Publikováno v:
Cells, Vol 11, Iss 6, p 921 (2022)
A distinct set of channels and transporters regulates the ion fluxes across the lysosomal membrane. Malfunctioning of these transport proteins and the resulting ionic imbalance is involved in various human diseases, such as lysosomal storage disorder
Externí odkaz:
https://doaj.org/article/fdbe2428eb234230ab4b6c8065d1a986
Autor:
Petra Dietrich, Nina Larisch, Tanja Studtrucker, Sonja A. Kirsch, Rainer A. Böckmann, Alexandra Schambony
Publikováno v:
Cellular and Molecular Life Sciences
Two-pore channels (TPCs) constitute a family of intracellular cation channels with diverse permeation properties and functions in animals and plants. In the model plant Arabidopsis, the vacuolar cation channel TPC1 is involved in propagation of calci
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::076c3b2e7527904dfcede183afda4753
https://doi.org/10.1007/s00018-016-2131-3
https://doi.org/10.1007/s00018-016-2131-3
Publikováno v:
Traffic. 13:1012-1022
Two-pore channels (TPCs) constitute a family of endolysosomal cation channels with functions in Ca²⁺ signaling. We used a mutational analysis to investigate the role of channel domains for the trafficking of the Arabidopsis TPC1 to the tonoplast,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abe1bacef113f0f169278c785ae66ed1
https://doi.org/10.1111/j.1600-0854.2012.01366.x
https://doi.org/10.1111/j.1600-0854.2012.01366.x
Autor:
Nina Larisch, Nobuyuki Uozumi, Shin Hamamoto, Petra Dietrich, Paul Vijay Kanth Gutla, Armando Carpaneto, Anna Boccaccio, Margherita Festa, Alex Costa, Joachim Scholz-Starke
Publikováno v:
Cellular and molecular life sciences (Print. ed.) 71 (2014): 4275–4283. doi:10.1007/s00018-014-1623-2
info:cnr-pdr/source/autori:Boccaccio, Anna; Scholz-Starke, Joachim; Hamamoto, Shin; Larisch, Nina; Festa, Margherita; Gutla, Paul Vijay Kanth; Costa, Alex; Dietrich, Petra; Uozumi, Nobuyuki; Carpaneto, Armando/titolo:The phosphoinositide PI(3,5)P-2 mediates activation of mammalian but not plant TPC proteins: functional expression of endolysosomal channels in yeast and plant cells./doi:10.1007%2Fs00018-014-1623-2/rivista:Cellular and molecular life sciences (Print. ed.)/anno:2014/pagina_da:4275/pagina_a:4283/intervallo_pagine:4275–4283/volume:71
info:cnr-pdr/source/autori:Boccaccio, Anna; Scholz-Starke, Joachim; Hamamoto, Shin; Larisch, Nina; Festa, Margherita; Gutla, Paul Vijay Kanth; Costa, Alex; Dietrich, Petra; Uozumi, Nobuyuki; Carpaneto, Armando/titolo:The phosphoinositide PI(3,5)P-2 mediates activation of mammalian but not plant TPC proteins: functional expression of endolysosomal channels in yeast and plant cells./doi:10.1007%2Fs00018-014-1623-2/rivista:Cellular and molecular life sciences (Print. ed.)/anno:2014/pagina_da:4275/pagina_a:4283/intervallo_pagine:4275–4283/volume:71
Two-pore channel proteins (TPC) encode intracellular ion channels in both animals and plants. In mammalian cells, the two isoforms (TPC1 and TPC2) localize to the endo-lysosomal compartment, whereas the plant TPC1 protein is targeted to the membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17a6d4886bbe67af00c939c84fb3f0e2
http://www.cnr.it/prodotto/i/288975
http://www.cnr.it/prodotto/i/288975
Autor:
Anna, Boccaccio, Joachim, Scholz-Starke, Shin, Hamamoto, Nina, Larisch, Margherita, Festa, Paul Vijay Kanth, Gutla, Alex, Costa, Petra, Dietrich, Nobuyuki, Uozumi, Armando, Carpaneto
Publikováno v:
Cellular and molecular life sciences : CMLS. 71(21)
Two-pore channel proteins (TPC) encode intracellular ion channels in both animals and plants. In mammalian cells, the two isoforms (TPC1 and TPC2) localize to the endo-lysosomal compartment, whereas the plant TPC1 protein is targeted to the membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9e6c372ba4cb13e2795010e60b661aba
https://pubmed.ncbi.nlm.nih.gov/24770793
https://pubmed.ncbi.nlm.nih.gov/24770793
Publikováno v:
Traffic (Copenhagen, Denmark). 13(7)
Two-pore channels (TPCs) constitute a family of endolysosomal cation channels with functions in Ca²⁺ signaling. We used a mutational analysis to investigate the role of channel domains for the trafficking of the Arabidopsis TPC1 to the tonoplast,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6e693a78671d620c1bc53e910e7bb4f7
https://pubmed.ncbi.nlm.nih.gov/22490017
https://pubmed.ncbi.nlm.nih.gov/22490017