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Showing results for amino clinker
Your search for Amina Clinker retrieved no results
Three amino acids in the C-linker are major determinants of gating in cyclic nucleotide-gated channels.
Zong X, Zucker H, Hofmann F, Biel M. Zong X, et al. EMBO J. 1998 Jan 15;17(2):353-62. doi: 10.1093/emboj/17.2.353. EMBO J. 1998. PMID: 9430627 Free PMC article.
In each channel, the cyclic nucleotide-binding site is connected to the last transmembrane segment of the channel by a linker peptide (C-linker) of approximately 90 amino acids. Here we report that replacement of three amino acids in the cone C-linker by the corresp …
In each channel, the cyclic nucleotide-binding site is connected to the last transmembrane segment of the channel by a linker peptide (C-lin …
Structures of the Human HCN1 Hyperpolarization-Activated Channel.
Lee CH, MacKinnon R. Lee CH, et al. Cell. 2017 Jan 12;168(1-2):111-120.e11. doi: 10.1016/j.cell.2016.12.023. Epub 2017 Jan 12. Cell. 2017. PMID: 28086084 Free PMC article.
HCN channels contain a K(+) channel selectivity filter-forming sequence from which the amino acids create a unique structure that explains Na(+) and K(+) permeability. ...
HCN channels contain a K(+) channel selectivity filter-forming sequence from which the amino acids create a unique structure that exp …
The gating mechanism in cyclic nucleotide-gated ion channels.
Mazzolini M, Arcangeletti M, Marchesi A, Napolitano LMR, Grosa D, Maity S, Anselmi C, Torre V. Mazzolini M, et al. Sci Rep. 2018 Jan 8;8(1):45. doi: 10.1038/s41598-017-18499-0. Sci Rep. 2018. PMID: 29311674 Free PMC article.
Distinct amino acids in the C-linker domain of the Arabidopsis K+ channel KAT2 determine its subcellular localization and activity at the plasma membrane.
Nieves-Cordones M, Chavanieu A, Jeanguenin L, Alcon C, Szponarski W, Estaran S, Chérel I, Zimmermann S, Sentenac H, Gaillard I. Nieves-Cordones M, et al. Plant Physiol. 2014 Mar;164(3):1415-29. doi: 10.1104/pp.113.229757. Epub 2014 Jan 9. Plant Physiol. 2014. PMID: 24406792 Free PMC article.
The resulting chimeric/mutated constructs were analyzed for subcellular localization and functionally characterized. We identified two contiguous amino acids, valine-381 and serine-382, located in the C-linker carboxy-terminal end, which prevent KAT2 surface expression whe …
The resulting chimeric/mutated constructs were analyzed for subcellular localization and functionally characterized. We identified two conti …
Structural basis of gating of CNG channels.
Giorgetti A, Nair AV, Codega P, Torre V, Carloni P. Giorgetti A, et al. FEBS Lett. 2005 Mar 28;579(9):1968-72. doi: 10.1016/j.febslet.2005.01.086. FEBS Lett. 2005. PMID: 15792804 Free article.
Tetrandrine, a novel inhibitor of ether-à-go-go-1 (Eag1), targeted to cervical cancer development.
Wang X, Chen Y, Li J, Guo S, Lin X, Zhang H, Zhan Y, An H. Wang X, et al. J Cell Physiol. 2019 May;234(5):7161-7173. doi: 10.1002/jcp.27470. Epub 2018 Oct 26. J Cell Physiol. 2019. PMID: 30362536
Tetrandrine directly interacted with Eag1 and inhibited the currents in a concentration-dependent manner (IC(50) of 69.97 5.2 muM), and the amino acids Ile (550) , Thr (552) , and Gln (557) in the Eag1 C-linker domain were critical for tetrandrine's inhibitory effect. ...
Tetrandrine directly interacted with Eag1 and inhibited the currents in a concentration-dependent manner (IC(50) of 69.97 5.2 muM), and the …
39 results