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Ion selectivity and gating mechanisms of FNT channels.
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Structural and functional characterization of the nitrite channel NirC from Salmonella typhimurium.
Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18395-400. doi: 10.1073/pnas.1210793109. Epub 2012 Oct 22.
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The soluble cytoplasmic N-terminal domain of the FocA channel gates bidirectional formate translocation.
Mol Microbiol. 2021 Apr;115(4):758-773. doi: 10.1111/mmi.14641. Epub 2020 Nov 30.
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The formate channel FocA exports the products of mixed-acid fermentation.
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The formate/nitrite transporter family of anion channels.
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Regulation of Single-Channel Conductance of Voltage-Dependent Anion Channel by Mercuric Chloride in a Planar Lipid Bilayer.
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Emerging issues of connexin channels: biophysics fills the gap.
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The VDAC channel: Molecular basis for selectivity.
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pH-dependent gating in a FocA formate channel.
Science. 2011 Apr 15;332(6027):352-4. doi: 10.1126/science.1199098.

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Comparison of ion selectivities of nitrite channel NirC and water channel aquaporin.
World J Microbiol Biotechnol. 2023 Mar 15;39(5):120. doi: 10.1007/s11274-023-03553-z.
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A single amino acid exchange converts FocA into a unidirectional efflux channel for formate.
Microbiology (Reading). 2022 Jan;168(1). doi: 10.1099/mic.0.001132.
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Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.
Chem Rev. 2020 Sep 23;120(18):10298-10335. doi: 10.1021/acs.chemrev.9b00830. Epub 2020 Aug 25.
6
Is the E. coli Homolog of the Formate/Nitrite Transporter Family an Anion Channel? A Computational Study.
Biophys J. 2020 Feb 25;118(4):846-860. doi: 10.1016/j.bpj.2019.12.024. Epub 2019 Dec 31.
7
The glycyl-radical enzyme 2-ketobutyrate formate-lyase, TdcE, interacts specifically with the formate-translocating FNT-channel protein FocA.
Biochem Biophys Rep. 2016 Apr 16;6:185-189. doi: 10.1016/j.bbrep.2016.04.005. eCollection 2016 Jul.
8
Energetics and mechanism of anion permeation across formate-nitrite transporters.
Sci Rep. 2017 Sep 20;7(1):12027. doi: 10.1038/s41598-017-11437-0.
9
The C-terminal Six Amino Acids of the FNT Channel FocA Are Required for Formate Translocation But Not Homopentamer Integrity.
Front Microbiol. 2017 Aug 22;8:1616. doi: 10.3389/fmicb.2017.01616. eCollection 2017.
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Mechanism of formate-nitrite transporters by dielectric shift of substrate acidity.
EMBO J. 2017 Apr 3;36(7):949-958. doi: 10.15252/embj.201695776. Epub 2017 Mar 1.

本文引用的文献

1
Regulation of reductive dehalogenase gene transcription in Dehalococcoides mccartyi.
Philos Trans R Soc Lond B Biol Sci. 2013 Mar 11;368(1616):20120317. doi: 10.1098/rstb.2012.0317. Print 2013 Apr 19.
2
The formate/nitrite transporter family of anion channels.
Biol Chem. 2013 Jun;394(6):715-27. doi: 10.1515/hsz-2012-0339.
3
Structural and functional characterization of the nitrite channel NirC from Salmonella typhimurium.
Proc Natl Acad Sci U S A. 2012 Nov 6;109(45):18395-400. doi: 10.1073/pnas.1210793109. Epub 2012 Oct 22.
4
The formate channel FocA exports the products of mixed-acid fermentation.
Proc Natl Acad Sci U S A. 2012 Aug 14;109(33):13254-9. doi: 10.1073/pnas.1204201109. Epub 2012 Jul 30.
5
Concerted movement in pH-dependent gating of FocA from molecular dynamics simulations.
J Chem Inf Model. 2012 Aug 27;52(8):2119-31. doi: 10.1021/ci300250q. Epub 2012 Jul 13.
6
Identification and characterization of a bacterial hydrosulphide ion channel.
Nature. 2012 Mar 11;483(7390):494-7. doi: 10.1038/nature10881.
7
The nitrite transport protein NirC from Salmonella typhimurium is a nitrite/proton antiporter.
Biochim Biophys Acta. 2012 May;1818(5):1342-50. doi: 10.1016/j.bbamem.2012.02.004. Epub 2012 Feb 14.
8
Physiological and biochemical characterization of AnNitA, the Aspergillus nidulans high-affinity nitrite transporter.
Eukaryot Cell. 2011 Dec;10(12):1724-32. doi: 10.1128/EC.05199-11. Epub 2011 Oct 21.
9
pH-dependent gating in a FocA formate channel.
Science. 2011 Apr 15;332(6027):352-4. doi: 10.1126/science.1199098.
10
Redox biochemistry of hydrogen sulfide.
J Biol Chem. 2010 Jul 16;285(29):21903-7. doi: 10.1074/jbc.R110.128363. Epub 2010 May 6.

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