Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Katrin Czempinski"'
Autor:
Shin Hamamoto, Ingo Dreyer, Judith Lucia Gomez-Porras, Camilla Voelker, Katrin Czempinski, Bernd Mueller-Roeber, Nobuyuki Uozumi, Dirk Becker, Franco Gambale
Publikováno v:
Plant Biology. 12:56-63
The group of voltage-independent K+ channels in Arabidopsis thaliana consists of six members, five tandem-pore channels (TPK1-TPK5) and a single K-ir-like channel (KCO3). All TPK/KCO channels are located at the vacuolar membrane except for TPK4, whic
Publikováno v:
The Plant Journal. 48:296-306
The Arabidopsis thaliana K+ channel family of AtTPK/KCO proteins consists of six members including a 'single-pore' (Kir-type) and five 'tandem-pore' channels. AtTPK4 is currently the only ion channel of this family for which a function has been demon
Autor:
Bernard Attali, Nava Moran, Dirk Becker, Menachem Moshelion, Katrin Czempinski, Rainer Hedrich, Bernd Mueller-Roeber
Publikováno v:
Plant Physiology. 128:634-642
In a search for potassium channels involved in light- and clock-regulated leaf movements, we cloned four putative K channel genes from the leaf-moving organs, pulvini, of the legume Samanea saman. The S. saman SPOCK1 is homologous to KCO1, an Arabido
Publikováno v:
Canadian Journal of Botany. 73:243-250
Parasitella parasitica is a facultative parasite of many Mucorales including Absidia glauca. The infection process includes the formation of a plasmatic continuum between host and parasite, which allows the invasion of the host by nuclei of the paras
Autor:
Alexandra Grippa, Alessandra Rocchetti, Katrin Czempinski, Joachim Scholz-Starke, Alessandro Vitale, Tripti Sharma, Emanuela Pedrazzini, Ingo Dreyer, Armando Carpaneto, Camilla Wulfetange
Publikováno v:
Frontiers in Plant Science
Frontiers in Plant Science, Vol 3 (2012)
Frontiers in plant science 3 (2012): 1–13. doi:10.3389/fpls.2012.00251
info:cnr-pdr/source/autori:Rocchetti A., Sharma T., Wulfetange C., Scholz-Starke J., Grippa A., Carpaneto A., Dreyer I., Vitale A., Czempinski K., Pedrazzini E./titolo:The putative K+ channel subunit AtKCO3 forms stable dimers in Arabidopsis/doi:10.3389%2Ffpls.2012.00251/rivista:Frontiers in plant science/anno:2012/pagina_da:1/pagina_a:13/intervallo_pagine:1–13/volume:3
Frontiers in Plant Science, Vol 3 (2012)
Frontiers in plant science 3 (2012): 1–13. doi:10.3389/fpls.2012.00251
info:cnr-pdr/source/autori:Rocchetti A., Sharma T., Wulfetange C., Scholz-Starke J., Grippa A., Carpaneto A., Dreyer I., Vitale A., Czempinski K., Pedrazzini E./titolo:The putative K+ channel subunit AtKCO3 forms stable dimers in Arabidopsis/doi:10.3389%2Ffpls.2012.00251/rivista:Frontiers in plant science/anno:2012/pagina_da:1/pagina_a:13/intervallo_pagine:1–13/volume:3
The permeation pore of K(+) channels is formed by four copies of the pore domain. AtKCO3 is the only putative voltage-independent K(+) channel subunit of Arabidopsis thaliana with a single pore domain. KCO3-like proteins recently emerged in evolution
Autor:
Katrin Czempinski, Anke Burmester
Publikováno v:
European Journal of Biochemistry. 220:403-408
In this paper we compare the sequences of a segment of the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase gene, isolated from eleven different strains belonging to four species of the fungal order Mucorales, Parasitella parasitica, Absidia
Autor:
Michael M. Wudick, Emanuela Pedrazzini, Bhakti Prinsi, Marie Maîtrejean, Camilla Voelker, Katrin Czempinski, Alessandro Vitale, Bernd Mueller-Roeber
Publikováno v:
Plant Physiology
Plant physiology (Bethesda) 156 (2011): 1783–1796.
info:cnr-pdr/source/autori:Maîtrejean M., Wudick M.M., Voelker C., Prinsi B., Mueller-Roeber B., Czempinski K., Pedrazzini E., Vitale A./titolo:Assembly and sorting of the tonoplast potassium channel AtTPK1 and its turnover by internalization into the vacuole./doi:/rivista:Plant physiology (Bethesda)/anno:2011/pagina_da:1783/pagina_a:1796/intervallo_pagine:1783–1796/volume:156
Plant physiology (Bethesda) 156 (2011): 1783–1796.
info:cnr-pdr/source/autori:Maîtrejean M., Wudick M.M., Voelker C., Prinsi B., Mueller-Roeber B., Czempinski K., Pedrazzini E., Vitale A./titolo:Assembly and sorting of the tonoplast potassium channel AtTPK1 and its turnover by internalization into the vacuole./doi:/rivista:Plant physiology (Bethesda)/anno:2011/pagina_da:1783/pagina_a:1796/intervallo_pagine:1783–1796/volume:156
The assembly, sorting signals, and turnover of the tonoplast potassium channel AtTPK1 of Arabidopsis (Arabidopsis thaliana) were studied. We used transgenic Arabidopsis expressing a TPK1-green fluorescent protein (GFP) fusion or protoplasts transient
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e7ae72bbbd141f0f0b123c531e945aa
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/36717
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/36717
Autor:
Anthony Gobert, Camilla Voelker, Katrin Czempinski, Stanislav Isayenkov, Frans J. M. Maathuis
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 104(25)
The Arabidopsis thaliana genome contains five genes that encode two pore K + (TPK) channels. The most abundantly expressed isoform of this family, TPK1, is expressed at the tonoplast where it mediates K + -selective currents between cytoplasmic and v
TPK1 (formerly KCO1) is the founding member of the family of two-pore domain K+ channels in Arabidopsis (Arabidopsis thaliana), which originally was described following expression in Sf9 insect cells as a Ca2+- and voltage-dependent outwardly rectify
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b872c4d8148afa4173fd69346351b94d
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/13499
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/13499
Autor:
Anja Roller, Marcel Dunkel, Adam Bertl, Camilla Voelker, Bernd Mueller-Roeber, Katrin Czempinski, Armando Carpaneto, Andreas Latz, M. R. G. Roelfsema, Petra Dietrich, Dirk Becker, Dietmar Geiger, Rainer Hedrich, D. Schmidt
The Arabidopsis tandem-pore K + (TPK) channels displaying four transmembrane domains and two pore regions share structural homologies with their animal counterparts of the KCNK family. In contrast to the Shaker -like Arabidopsis channels (six transme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38027eabee560362602cf5d94f81cfce
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/15093
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/15093