Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Sascha Tayefeh"'
Autor:
Sascha Tayefeh, Leonhard M. Henkes, Brigitte Hertel, Christian Cosentino, Gerhard Thiel, Dirk Baumeister, James L. Van Etten, Stefan M. Kast, Timo Greiner, Manuela Gebhardt, Anna Moroni
Publikováno v:
Biochemistry (Easton) 51 (2012): 5571–5579. doi:10.1021/bi3006016
info:cnr-pdr/source/autori:Gebhardt M; Henkes LM; Tayefeh S; Hertel B; Greiner T; Van Etten JL; Baumeister D; Cosentino C; Moroni A; Kast SM; Thiel G/titolo:Relevance of Lysine Snorkeling in the Outer Transmembrane Domain of Small Viral Potassium Ion Channels/doi:10.1021%2Fbi3006016/rivista:Biochemistry (Easton)/anno:2012/pagina_da:5571/pagina_a:5579/intervallo_pagine:5571–5579/volume:51
info:cnr-pdr/source/autori:Gebhardt M; Henkes LM; Tayefeh S; Hertel B; Greiner T; Van Etten JL; Baumeister D; Cosentino C; Moroni A; Kast SM; Thiel G/titolo:Relevance of Lysine Snorkeling in the Outer Transmembrane Domain of Small Viral Potassium Ion Channels/doi:10.1021%2Fbi3006016/rivista:Biochemistry (Easton)/anno:2012/pagina_da:5571/pagina_a:5579/intervallo_pagine:5571–5579/volume:51
Transmembrane domains (TMDs) are often flanked by Lys or Arg because they keep their aliphatic parts in the bilayer and their charged groups in the polar interface. Here we examine the relevance of this so-called "snorkeling" of a cationic amino acid
Autor:
Sascha Tayefeh, Manuela Gebhardt, Anna Moroni, Gerhard Thiel, Dirk Baumeister, Harald Schwalbe, Christian Richter, Stefan M. Kast, Michael Kreim, Brigitte Hertel, Thomas Kloss
Publikováno v:
Biophysical Journal; Vol 96
Biophysical journal
96 (2009): 485–498. doi:10.1016/j.bpj.2008.09.050
info:cnr-pdr/source/autori:Tayefeh S; Kloss T; Kreim M; Gebhardt M; Baumeister D; Hertel B; Richter C; Schwalbe H; Moroni A; Thiel G;Kast SM./titolo:Model development for the viral Kcv potassium channel./doi:10.1016%2Fj.bpj.2008.09.050/rivista:Biophysical journal (Print)/anno:2009/pagina_da:485/pagina_a:498/intervallo_pagine:485–498/volume:96
Biophysical journal
96 (2009): 485–498. doi:10.1016/j.bpj.2008.09.050
info:cnr-pdr/source/autori:Tayefeh S; Kloss T; Kreim M; Gebhardt M; Baumeister D; Hertel B; Richter C; Schwalbe H; Moroni A; Thiel G;Kast SM./titolo:Model development for the viral Kcv potassium channel./doi:10.1016%2Fj.bpj.2008.09.050/rivista:Biophysical journal (Print)/anno:2009/pagina_da:485/pagina_a:498/intervallo_pagine:485–498/volume:96
A computational model for the open state of the short viral Kcv potassium channel was created and tested based on homology modeling and extensive molecular-dynamics simulation in a membrane environment. Particular attention was paid to the structure
Autor:
Sascha Tayefeh, Brigitte Hertel, Stefan M. Kast, Gerhard Thiel, and Anna Moroni, Thomas Kloss
Publikováno v:
Biochemistry. 46:4826-4839
The functional effect of mutations near the intracellular mouth of the short viral Kcv potassium channel was studied by molecular dynamics simulations. As a model system we used the analogously mutated and truncated KirBac1.1, a channel with known cr
Autor:
Mario Mehmel, Stefan M. Kast, James L. Van Etten, Anna Moroni, Brigitte Hertel, Gerhard Thiel, Sascha Tayefeh
Publikováno v:
The Journal of Membrane Biology. 210:21-29
The virus-coded channel Kcv has the typical structure of a two-transmembrane domain K(+) channel. Exceptional are its cytoplasmic domains: the C terminus basically ends inside the membrane and, hence, precludes the formation of a cytoplasmic gate by
Autor:
Ming Kang, Anna Moroni, Gerhard Thiel, Stefan M. Kast, Sascha Tayefeh, James L. Van Etten, Sabrina Gazzarrini, Dario DiFrancesco
Publikováno v:
The Journal of biological chemistry
279 (2004): 28443–28449. doi:10.1074/jbc.M401184200
info:cnr-pdr/source/autori:Gazzarrini S.; Kang M.; Van Etten J.L.; Tayefeh S.; Kast S.M.; DiFrancesco D.; Thiel G.; Moroni A./titolo:Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins./doi:10.1074%2Fjbc.M401184200/rivista:The Journal of biological chemistry (Print)/anno:2004/pagina_da:28443/pagina_a:28449/intervallo_pagine:28443–28449/volume:279
279 (2004): 28443–28449. doi:10.1074/jbc.M401184200
info:cnr-pdr/source/autori:Gazzarrini S.; Kang M.; Van Etten J.L.; Tayefeh S.; Kast S.M.; DiFrancesco D.; Thiel G.; Moroni A./titolo:Long distance interactions within the potassium channel pore are revealed by molecular diversity of viral proteins./doi:10.1074%2Fjbc.M401184200/rivista:The Journal of biological chemistry (Print)/anno:2004/pagina_da:28443/pagina_a:28449/intervallo_pagine:28443–28449/volume:279
Kcv is a 94-amino acid protein encoded by chlorella virus PBCV-1 that corresponds to the pore module of K(+) channels. Therefore, Kcv can be a model for studying the protein design of K(+) channel pores. We analyzed the molecular diversity generated
Publikováno v:
The Plant Journal. 37:391-397
Trafficking of K + Inward (K in +) rectifying channels was analyzed in guard cells of Vicia faba transfected with the K in + rectifier from Arabidopals thaliana KAT1 fused to the green fluorescent protein (GFP). Confocal images and whole-cell patch-c
Publikováno v:
The Journal of General Physiology
In the recent collection of articles in Perspectives on: Ion selectivity, several authors summarized the current state of knowledge on ion channel selectivity, predominated by experimental and theoretical approaches to understanding K+/Na+ discrimina
Autor:
Gerhard Thiel, Dirk Baumeister, Stefan M. Kast, Thomas Kloss, Brigitte Hertel, Jennifer Hewing, Sascha Tayefeh, Manuela Gebhardt, Anna Moroni
Publikováno v:
European biophysics journal : EBJ. 39(7)
The viral potassium channel Kcv comprises only 94 amino acids, which represent the pore module of more complex K(+) channels. As for Kir-type channels, Kcv also has a short N-terminal helix exposed to the cytoplasm, upstream of the first transmembran