The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index; none of the 15 sources its claims cite is checked for support yet.
Bacterial fluoride resistance, Fluc channels, and the weak acid accumulation effect
Open accessAbstract
Fluoride ion (F−) is a ubiquitous environmental threat to microorganisms, which have evolved a family of highly selective “Fluc” F− channels that export this inhibitory anion from their cytoplasm. It is unclear, however, how a thermodynamically passive mechanism like an ion channel can protect against high concentrations of external F−. We monitored external F− concentrations in Escherichia coli suspensions and showed that, in bacteria lacking Fluc, F− accumulates when the external medium is acidified, as a predicted function of the transmembrane pH gradient. This weak acid accumulation effect, which results from the high pKa (3.4) and membrane permeability of HF, is abolished by Fluc channels. We also found that, although bacterial growth is inhibited by high concentrations of F−, bacteria can withstand cytoplasmic F− at levels a hundred times higher than those that inhibit proliferation, resuming growth when the F− challenge is removed.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
Fluc channels protect *E. coli* from fluoride toxicity by counteracting weak acid accumulation of F− in acidic environments. The paper shows quantitatively that without Fluc, cytoplasmic F− rises according to the transmembrane pH gradient, stalling but not killing cells.
Key findings
- Wild-type *E. coli* withstands F− across pH 7.0–5.0, whereas ΔFluc growth inhibition appears at progressively lower F− concentrations as pH is lowered from 7.0 to 5.0.
- Acidification drives F− uptake into ΔFluc bacteria but not wild-type; uptake increases as extracellular pH is lowered and as extracellular F− concentration increases.
- The cytoplasmic-to-extracellular F− ratio matches the extracellular-to-cytoplasmic proton activity ratio over two orders of magnitude, and at fixed pH gradient internal F− varies linearly with external F−; the fitted slope of 54 corresponds to a pH gradient of 1.7 units, close to the expected 1.8 units assuming cytoplasmic pH 7.0.
- F− exposure stops ΔFluc growth but does not kill: survival was close to 100% for wild-type and ΔFluc at pH 7.0 or 5.5 over 2–26 h; after F− washout, recovery lag was roughly 30 min at pH 5.5 where intracellular F− reached ∼15 mM, versus no lag at pH 7.0 where it was ∼0.5 mM.
Methods
- Growth sensitivity assays used wild-type *E. coli* strain BW25113 and a Fluc-deleted (ΔFluc; kanr) strain; *E. coli* strains do not possess CLCF F−/H+ antiporters.
- For F− uptake, stationary-phase bacteria were pelleted and resuspended in recording medium (150 mM NaCl, 0.1–1.3 mM NaF, 10 mM KPi, 10 mM MES, pH 7.0), and extracellular F− was continuously monitored with an F−-specific electrode in a 2-ml stirred cell after acid pulses.
- Intracellular F− was estimated from loss of extracellular anion, using a cytoplasmic water volume of 0.8–1.0 fl/cell determined from [14C]inulin and [14C]sucrose distributions; survival was assessed by plating on F−-free neutral-pH LB plates and counting colonies.
Limitations
- Not explicitly stated: the paper has no formal limitations section. The quantitative analysis assumes cytoplasmic pH remains constant at 7.0 under the tested conditions; internal pH was not measured in these experiments but taken from prior literature.
- Evident from the text: all experiments are in *E. coli* (WT BW25113 and ΔFluc), so generality to other bacteria, yeasts, and protozoa is inferred from prior work rather than directly tested here.
- Evident from the text: F− uptake is measured indirectly as extracellular F− loss by electrode and converted to cytoplasmic concentration using an estimated cytoplasmic volume, not by direct intracellular F− measurement.
Model-written summary. Check it against the paper before relying on it.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
0 of 15 cited sources checked · 0 supported · 0 flagged
- Findingown data
F− uptake into ΔFluc bacteria increases as extracellular pH is lowered.
“Moreover, F− uptake into ΔFluc bacteria increases as extracellular pH is lowered (Fig. 3 B), again as expected.”
Quote in the paperSubstantial claim - Findingown data
The amount of F− transported in response to acidification increases with extracellular F− concentration.
“A further prediction is that the amount of F− transported in response to acidification should increase with extracellular F− concentration, as is also observed (Fig. 3 C).”
Quote in the paperSubstantial claim - Findingown data
Growth inhibition of ΔFluc E. coli appears at progressively lower F− concentrations as pH is lowered from 7.0 to 5.0.
“Although wild-type E. coli withstands F− in all conditions tested, growth inhibition of ΔFluc bacteria appears at progressively lower F− concentrations as pH is lowered from 7.0 to 5.0.”
Quote in the paperSubstantial claim - Findingown data
Wild-type E. coli withstands F− in all conditions tested.
“Although wild-type E. coli withstands F− in all conditions tested, growth inhibition of ΔFluc bacteria appears at progressively lower F− concentrations as pH is lowered from 7.0 to 5.0.”
Quote in the paperSubstantial claim - Findingown data
Upon acidification to pH 5.5, extracellular F− immediately begins to drop in ΔFluc suspensions, indicating uptake of F− into these bacteria over and above the initial equilibrated concentration.
“Upon acidification to pH 5.5, extracellular F− immediately begins to drop in ΔFluc suspensions, indicating uptake of the halide into these bacteria over and above the initial equilibrated concentration.”
Quote in the paperSubstantial claim
- Findingown data
No such F− uptake is observed with wild-type bacteria.
“No such F− uptake is observed with wild-type bacteria.”
Quote in the paperSubstantial claim - Findingown data
The ratio of cytoplasmic to extracellular F− is numerically equal to the extracellular to cytoplasmic proton activity ratio over two orders of magnitude.
“The ratio of cytoplasmic to extracellular F− is numerically equal to the extracellular to cytoplasmic proton activity ratio over two orders of magnitude (Fig. 4 A), assuming that cytoplasmic pH is regulated near neutrality under these conditions, as has been long known to be the case (Slonczewski et al., 1981; Zilberstein et al., 1984; Wilks and Slonczewski, 2007).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Slonczewski et al., 1981 source
- cites Zilberstein et al., 1984 source
- cites Wilks and Slonczewski, 2007 source
- The authors state this as an assumption: Cytoplasmic pH is regulated near neutrality under the conditions of the F− uptake experiments.
- Findingown data
The weak acid accumulation effect operates quantitatively as expected.
“By measuring F− uptake into Fluc-knockout Escherichia coli under a variety of pH conditions, we now show that these bacteria display pH-dependent hypersensitivity to F−, that the weak acid accumulation effect operates quantitatively as expected, and that Fluc channels completely abolish F− accumulation, permitting growth in the presence of F−.”
Quote in the paperSubstantial claim - Findingown data
Survival of wild-type and ΔFluc E. coli after 2-26 h exposure to 0.5 mM F− at pH 7.0 or 5.5 is close to 100%.
“Survival of all cells, wild-type and ΔFluc, is close to 100% for both pH conditions.”
Quote in the paperSubstantial claim - Findingown data
At a fixed pH gradient, cytoplasmic F− concentration varies linearly with extracellular F−.
“Furthermore, at a fixed pH gradient, cytoplasmic F− concentration varies linearly with extracellular F−, also as predicted (Fig. 4 B).”
Quote in the paperSubstantial claim - Premisecitation
Plasma membranes of many bacteria, yeasts, and protozoa carry F− exporter proteins to maintain cytoplasmic F− below inhibitory concentrations.
“Accordingly, plasma membranes of many bacteria, yeasts, and protozoa carry F− exporter proteins to maintain cytoplasmic F− below inhibitory concentrations (Breaker, 2012; Stockbridge et al., 2012, 2013; Li et al., 2013).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Breaker, 2012 source
- cites Stockbridge et al., 2012, 2013
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites Li et al., 2013
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- Interpretationcitation
In a hypoxic milieu of pH 5.5, a bacterium lacking F− exporters with pH 7.0 cytoplasm would accumulate F− ∼30-fold into the millimolar range, where enzyme inhibition would be severe.
“According to this mechanism, in a hypoxic milieu of pH 5.5, for example, a bacterium lacking F− exporters, when experiencing mild acid stress, with pH 7.0 cytoplasm (Wilks and Slonczewski, 2007), would accumulate the anion ∼30-fold into the millimolar range, where enzyme inhibition would be severe.”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Wilks and Slonczewski, 2007 source
- Rests on an assumption: HF is a weak acid with pKa = 3.4 and is membrane-permeant.
- Interpretationreasoning
Fluc channels protect bacteria from accumulating F− in acidic environments.
“Fluc channels protect bacteria from accumulating F− in acidic environments.”
Quote in the paperSubstantial claim - Interpretationreasoning
An F− channel present in the cell membrane would abolish the weak acid accumulation effect by collapsing the F− gradient, exporting the anion to its low equilibrium level.
“An F− channel present in the cell membrane would abolish this effect by collapsing the F− gradient, exporting the anion to its low equilibrium level.”
Quote in the paperNot a substantial claim - Interpretationown data
Fluc channels are required to counteract cytoplasmic F− accumulation driven by pH gradients across the bacterial inner membrane set up by mild acidification of the growth medium.
“These experiments demonstrate quantitatively that Fluc channels are required to counteract cytoplasmic F− accumulation driven by pH gradients across the bacterial inner membrane set up by mild acidification of the growth medium, a condition which mimics environments that microorganisms sporadically encounter.”
Quote in the paperSubstantial claim - Interpretationreasoning
In such a case, any organism without an F− permeability pathway would necessarily concentrate the halide in its cytoplasm far above the extracellular concentration via the weak acid accumulation effect.
“In such a case, any organism without an F− permeability pathway would necessarily concentrate the halide in its cytoplasm far above the extracellular concentration via the weak acid accumulation effect.”
Quote in the paperNot a substantial claim- Rests on an assumption: HF is a weak acid with pKa = 3.4 and is membrane-permeant.
- Interpretationcitation
For a bacterial cell with a −100-mV potential, the equilibrium level of cytoplasmic F− would be ∼50-fold lower than the extracellular concentration, i.e., <1 μM.
“For a bacterial cell with a −100-mV potential, the equilibrium level of cytoplasmic F− would be ∼50-fold lower than the extracellular concentration, i.e., <1 µM (far below inhibitory levels; Adamek et al., 2005).”
Quote in the paperSubstantial claim0 of 1 sources checked- cites Adamek et al., 2005
- Rests on an assumption: Nearly all cells maintain negative membrane potentials, which can be quite large for bacteria and yeast under energy-using conditions.
- It may state two separate claims as one. 10
It may state two separate claims as one.
Findingown dataThe bacteria are not killed by F− exposure, but merely stalled.
“The experiments of Fig. 5 show that the bacteria are not killed, but merely stalled.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Findingown dataF− exposure stops growth of ΔFluc cells but does not kill them; instead, it puts them into a quiescent condition from which they rapidly recover when F− is subsequently removed.
“We also show that although F− accumulation stops growth of Fluc-knockout cells, it does not kill them; instead, it puts them into a quiescent condition from which they rapidly recover when F− is subsequently removed.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Findingown dataΔFluc E. coli exposed to 0.5 mM F− at pH 5.5 accumulate intracellular F− to ∼15 mM, and after F− removal growth resumes after a lag of roughly 30 min; at pH 7.0 where cytoplasmic F− is low (∼0.5 mM), no lag is observed.
“At pH 7.0, where cytoplasmic F− is low (∼0.5 mM), no lag is observed, but at pH 5.5, where intracellular F− has accumulated to ∼15 mM, a lag of roughly 30 min is necessary for full recovery of growth rate.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Findingown dataFluc channels completely abolish F− accumulation, permitting growth in the presence of F−.
“By measuring F− uptake into Fluc-knockout Escherichia coli under a variety of pH conditions, we now show that these bacteria display pH-dependent hypersensitivity to F−, that the weak acid accumulation effect operates quantitatively as expected, and that Fluc channels completely abolish F− accumulation, permitting growth in the presence of F−.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Findingown dataThe slope of the linear fit is equivalent to a pH gradient of 1.7 units, in good agreement with the value (1.8 units) under the assumption that cytoplasmic pH remains constant at 7.0.
“The slope of the linear fit is equivalent to a pH gradient of 1.7 units, which is in good agreement with the value (1.8 units) under the assumption that cytoplasmic pH remains constant at 7.0 under these conditions.”
Quote in the paperSubstantial claim- The authors state this as an assumption: Internal pH remains constant at 7.0 under the conditions of the F− uptake experiments.
It may state two separate claims as one.
PremisecitationΔFluc E. coli is hypersensitive to F− in pH-neutral media, and this effect is reversed by expressing F− exporters with a rescue plasmid.
“In previous work, a Fluc-knockout (ΔFluc) strain of E. coli was shown to be hypersensitive to F−, as assessed by growth in pH-neutral media, and this effect could be reversed by expressing F− exporters in the bacteria with a rescue plasmid (Breaker, 2012; Stockbridge et al., 2012).”
Quote in the paperSubstantial claim0 of 2 sources checkedIt may state two separate claims as one.
PremisecitationAqueous F− at 10-100 μM inhibits phosphoryl-transfer enzymes essential for energy production and nucleic acid synthesis, making it potentially toxic to cells.
“Aqueous F−, ubiquitous in the environment at 10–100-µM levels, is potentially toxic to cells because at these concentrations it inhibits phosphoryl-transfer enzymes essential for energy production and nucleic acid synthesis (Adamek et al., 2005; Breaker, 2012).”
Quote in the paperSubstantial claim0 of 2 sources checked- cites Adamek et al., 2005
- cites Breaker, 2012 source
It may state two separate claims as one.
PremisecitationIt is now firmly established that Fluc proteins are F−-specific ion channels that protect E. coli and yeasts from F− toxicity.
“It is now firmly established that Fluc proteins are F−-specific ion channels that protect E. coli and yeasts from F− toxicity (Baker et al., 2012; Stockbridge et al., 2012, 2013; Li et al., 2013).”
Quote in the paperSubstantial claim0 of 3 sources checked- cites Baker et al., 2012 source
- cites Stockbridge et al., 2012, 2013
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
- cites Li et al., 2013
Couldn’t be matched to a paper in Crossref, so it can’t be checked.
It may state two separate claims as one.
InterpretationreasoningFluc-type F− channels act to keep cytoplasmic F− below extracellular concentrations and below levels that would otherwise inhibit metabolism.
“Though thermodynamically passive, Fluc-type F− channels act to keep cytoplasmic F− below extracellular concentrations and below levels that would otherwise inhibit metabolism.”
Quote in the paperSubstantial claimIt may state two separate claims as one.
Interpretationown dataThe results verify that HF acts as a membrane-permeant weak acid to deliver F− anion to the bacterial cytoplasm and trap it there at high concentrations, thus preventing growth.
“The aforementioned results verify the idea that HF acts as a membrane-permeant weak acid to deliver F− anion to the bacterial cytoplasm and trap it there at high concentrations, thus preventing growth.”
Quote in the paperSubstantial claim- Rests on an assumption: HF is a weak acid with pKa = 3.4 and is membrane-permeant.
The paper relies on this without support.
The relevance of the weak acid accumulation mechanism to F− toxicity and Fluc function has not been previously examined.
“But the relevance of the weak acid accumulation mechanism to F− toxicity and Fluc function has not been previously examined.”
The authors state this as an assumption.
Cytoplasmic pH is regulated near neutrality under the conditions of the F− uptake experiments.
“assuming that cytoplasmic pH is regulated near neutrality under these conditions, as has been long known to be the case (Slonczewski et al., 1981; Zilberstein et al., 1984; Wilks and Slonczewski, 2007).”
The authors state this as an assumption.
Internal pH remains constant at 7.0 under the conditions of the F− uptake experiments.
“Internal pH was assumed to remain constant at 7.0.”
The paper relies on this without support.
Nearly all cells maintain negative membrane potentials, which can be quite large for bacteria and yeast under energy-using conditions.
“First, nearly all cells maintain negative membrane potentials, and these can be quite large for bacteria and yeast under energy-using conditions.”
The paper relies on this without support.
HF is a weak acid with pKa = 3.4 and is membrane-permeant.
“This effect arises because HF is both a weak acid (pKa = 3.4) and a membrane-permeant molecule (Fig. 1).”
The paper relies on this without support.
In the absence of F− exporter proteins, microorganisms become hypersensitive to F−, an effect exacerbated by low extracellular pH.
“In the absence of such proteins, these microorganisms become hypersensitive to F−, an effect exacerbated by low extracellular pH.”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Expression of F− export proteins in the plasma membrane undermines weak acid accumulation of fluoride.
“By providing a route for accumulating F− to exit the cell, expression of these F− export proteins in the plasma membrane simply undermines weak acid accumulation of fluoride (1, 14, 25, 26).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
Fluoride produced intracellularly and released, or produced in the periplasm, readily re-enters and accumulates in cells via weak acid accumulation.
“Moreover, fluoride produced intracellularly and released, or produced in the periplasm, readily re-enters and accumulates in cells via a process called weak acid accumulation65,71, especially as the medium pH acidifies, which is typical with dense bacterial cultures.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
Environmental fluoride enters cells largely as HF.
“Environmental fluoride enters cells largely as HF71.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
In E. coli, high concentrations of fluoride stall cell division and growth, which is only resumed after fluoride is removed.
“In E. coli, high concentrations of fluoride stall cell division and growth, which is only resumed after fluoride is removed71.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
The ionic form of fluoride becomes trapped in the cell, accumulating to levels dictated by the pH gradient across the membrane.
“The ionic form becomes trapped in the cell, accumulating to levels dictated by the pH gradient across the membrane71.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
E. coli appears to shut down metabolism entirely under fluoride, only resuming growth once the fluoride insult is removed.
“Other bacteria, like E. coli, appear to shut down metabolism entirely, only resuming growth once the fluoride insult is removed71.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
In E. coli, fluoride accumulation is bacteriostatic, halting metabolism while fluoride is present.
“For some bacteria, like E. coli, fluoride accumulation is bacteriostatic, halting metabolism while fluoride is present71.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
Flucs function as passive fluoride channels that exploit the positive-outside membrane potential to drive expulsion of fluoride.
“In contrast to the CLCFs, the Flucs (Fluoride channel) function as passive fluoride channels81 that exploit the positive-outside membrane potential (the electrical component of the proton-motive force) to drive the expulsion of this anionic species71.”
From The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis (2024) · cites this paper as [71]
Microbial fluoride sensitivity is amplified by low pH, as is characteristic of dysbiotic dental biofilms.
“First, microbial fluoride sensitivity is amplified by low pH, as is characteristic of dysbiotic dental biofilms (20).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [20]
In the absence of a fluoride export mechanism, impermeable fluoride ions become trapped and accumulate intracellularly.
“In the absence of a fluoride export mechanism, these impermeable ions become trapped and accumulate intracellularly (20).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [20]
In cells, intracellular fluoride accumulation quantitatively follows the pH gradient.
“In these cells, intracellular fluoride accumulation quantitatively follows the pH gradient (20).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [20]
Fluoride acts as a bacteriostatic agent for many microbes.
“Whereas fluoride acts as a bacteriostatic agent for many microbes (18, 20, 46)”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [20]
The high fluoride accumulation in biofilms with ∆CLCF S. mutans is due to fluoride accumulation in the cytoplasm of species that lack a fluoride exporter.
“We propose that this is due to fluoride accumulation in the cytoplasm of the species that lack a fluoride exporter, as has been shown to occur in other fluoride export-deficient bacteria (17, 20).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [20]
The fluoride retention in biofilms with ∆CLCF S. mutans mirrors intracellular fluoride accumulation measured in other microbes that lack fluoride exporters.
“This effect mirrors the intracellular fluoride accumulation that has been measured in other microbes that lack fluoride exporters (17, 20, 52).”
From Fluoride export is required for the competitive fitness of pathogenic microorganisms in dental biofilm models (2024) · cites this paper as [20]
Fluoride behaves as a weak acid itself, accumulating in cytoplasm without active uptake when extracellular pH is lower than intracellular pH, due to high pKa and membrane permeability of hydrogen fluoride (HF).
“It also behaves as a weak acid itself, accumulating in the cytoplasm without active uptake when the extracellular pH is lower than the intracellular pH, due to the high pKa and membrane permeability of hydrogen fluoride (HF) (169).”
From Toward the development of a molecular toolkit for the microbial remediation of per-and polyfluoroalkyl substances (2024) · cites this paper as [169]
Fluc proteins are F--specific ion channels of the Fluc family.
“microorganisms export this anion through F--specific ion channels of the Fluc family1–4.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [3]
Unicellular organisms counteract F- toxicity through F--exporting membrane transport proteins that keep cytoplasmic F- below inhibitory levels.
“Unicellular organisms directly exposed to environmental F- counteract the anion’s toxicity through the action of F--exporting membrane transport proteins that keep cytoplasmic F- below inhibitory levels1–4,8.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [3]
Fluoride exporters from the CLCF and Fluc families are not necessarily associated with a riboswitch; some, including the E. coli Fluc channel, are instead constitutively expressed.
“Fluoride exporters from the CLCF and Fluc families are not necessarily associated with a riboswitch(1, 25); some, including the E. coli Fluc channel, are instead constitutively expressed (14).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
Inhibitory constants by F− are in the hundreds of micromolar range, well within the range of cytoplasmic F− accumulation that occurs in modestly acidic environmental niches.
“In these various examples, the inhibitory constants by F− are in the hundreds of micromolar range, well within the range of cytoplasmic F− accumulation that occurs in modestly acidic environmental niches(14).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
In microbes that lack any F− export pathway, intracellular F− accumulates according to Eq. 1; for a microbe in a modestly acidic niche of pH 5.5 that maintains a cytoplasmic pH of 7.5, the intracellular fluoride will accumulate 100-fold in the cytoplasm compared to environmental levels, reaching millimolar concentrations.
“In microbes that lack any F− export pathway, intracellular F− accumulates according to this simple scheme: (Eq. 1)F−in F−out =H+out H+in so that for a microbe in a modestly acidic niche of pH 5.5 that maintains a cytoplasmic pH of 7.5, the intracellular fluoride will accumulate 100-fold in the cytoplasm compared to environmental levels, reaching millimolar concentrations (14).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
The weak acid accumulation effect can lead to cytoplasmic fluoride levels that exceed external F−.
“First, the weak acid accumulation effect can lead to cytoplasmic fluoride levels that exceed external F−, and a fluoride-selective efflux pathway simply undermines this process.”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
Knockouts of genomic Fluc/FEX proteins increase fluoride sensitivity of bacteria including E. coli, B. subtilis, and S. sanguinis, and fungi including S. cerevisiae, C. albicans, N. crassa, and A. fumigatus.
“Knockouts of genomic Fluc/FEX proteins increase fluoride sensitivity of bacteria including Escherichia coli(14, 25), Bacillus subtilis(25, 64), and oral bacterium Streptococcus sanguinis(49), and fungi including Saccharomyces cerevisiae(3, 26), Candida albicans(26), Neurospora crassa(26), and Aspergillus fumigatus(65).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
A metabolizing cell maintains a negative-inside membrane potential, so the electrical potential favors anion expulsion.
“Second, a metabolizing cell maintains a negative-inside membrane potential, so that the electrical potential favors anion expulsion(14).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [14]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Different starting pH values for the Figure 3A experiment
MinorThe results text says the bacteria were suspended at pH 7.0 before acidification, but the Figure 3A caption says the pH was lowered from 7.5 to 5.5.
“Bacteria were suspended in pH 7.0 media containing 0.5 mM F−, and extracellular F− concentration was continuously monitored electrochemically. Upon acidification to pH 5.5, extracellular F− immediately begins to drop in ΔFluc suspensions”
“addition of HCl to drop the pH from 7.5 to 5.5 (open triangle)”
Citations
Cites
Periplasmic space in Salmonella typhimurium and Escherichia coli.
Stock, J., Rauch, B., & Roseman, S. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41044-1 · Cited by 575
Widespread genetic switches and toxicity resistance proteins for fluoride
Baker, J. L., Sudarsan, N., Weinberg, Z., Roth, A., Stockbridge, R. B., & Breaker, R. R. (2012) · Science · doi:10.1126/science.1215063 · Cited by 438
Self-citationVolkmer, B., & Heinemann, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023126 · Cited by 375
Wilks, J. C., & Slonczewski, J. L. (2007) · Journal of Bacteriology · doi:10.1128/jb.00615-07 · Cited by 366
Slonczewski, J. L., Rosen, B. P., Alger, J. R., & Macnab, R. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.10.6271 · Cited by 301
Fluoride and organic weak acids as modulators of microbial physiology
Marquis, R. E., Clock, S. A., & Mota-Meira, M. (2003) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2003.tb00627.x · Cited by 299
Escherichia coli intracellular pH, membrane potential, and cell growth
Zilberstein, D., Agmon, V, Schuldiner, S., & Padan, E. (1984) · Journal of Bacteriology · doi:10.1128/jb.158.1.246-252.1984 · Cited by 193
Fluoride resistance and transport by riboswitch-controlled CLC antiporters
Stockbridge, R. B., Lim, H.-H., Otten, R., Williams, C., Shane, T., Weinberg, Z., & Miller, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210896109 · Cited by 150
Self-citationDetermination of bacterial cell volume with the Coulter Counter
KUBITSCHEK, H. E., & Friske, J. A. (1986) · Journal of Bacteriology · doi:10.1128/jb.168.3.1466-1467.1986 · Cited by 144
Li, S., Smith, K. D., Davis, J. H., Gordon, P. B., Breaker, R. R., & Strobel, S. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310439110 · Cited by 122
A family of fluoride-specific ion channels with dual-topology architecture
Stockbridge, R. B., Robertson, J. L., Kolmakova-Partensky, L., & Miller, C. (2013) · eLife · doi:10.7554/elife.01084 · Cited by 120
Self-citationNew insight on the response of bacteria to fluoride
Breaker, R. R. (2012) · Caries Research · doi:10.1159/000336397 · Cited by 56
Gramicidin D enhances the antibacterial activity of fluoride
Nelson, J. W., Zhou, Z., & Breaker, R. R. (2014) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2014.03.061 · Cited by 15
(2005) · PubMed
Flagged first, then by citations
Cited by
Sorted by citations
Dental Enamel Formation and Implications for Oral Health and Disease
Lacruz, R. S., Habelitz, S., Wright, J. T., & Paine, M. L. (2017) · Physiological Reviews · doi:10.1152/physrev.00030.2016 · Cited by 650
Principles of fluoride toxicity and the cellular response: a review
Johnston, N. R., & Strobel, S. A. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02687-5 · Cited by 356
Fast and selective fluoride ion conduction in sub-1-nanometer metal-organic framework channels
Li, X., Zhang, H., Wang, P., Hou, J., Lü, J., Easton, C. D., Zhang, X., Hill, M. R., Thornton, A. W., Liu, J. Z., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10420-9 · Cited by 279
Molecular Mechanisms for Bacterial Potassium Homeostasis
Stautz, J., Hellmich, Y., Fuss, M. F., Silberberg, J. M., Devlin, J. R., Stockbridge, R. B., & Hänelt, I. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166968 · Cited by 189
Self-citationStrapped calix[4]pyrroles: from syntheses to applications
Peng, S., He, Q. G., Vargas‐Zúñiga, G. I., Qin, L., Hwang, I., Kim, S. K., Heo, N. J., Lee, C., Dutta, R., & Sessler, J. L. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00528e · Cited by 180
Wackett, L. P. (2022) · Microbial Biotechnology · doi:10.1111/1751-7915.13928 · Cited by 165
Bacillus subtilis, the model Gram‐positive bacterium: 20 years of annotation refinement
Borriss, R., Danchin, A., Harwood, C. R., Médigue, C., Rocha, E. P. C., Sekowska, A., & Vallenet, D. (2017) · Microbial Biotechnology · doi:10.1111/1751-7915.13043 · Cited by 120
Crystal structures of a double-barrelled fluoride ion channel
Stockbridge, R. B., Kolmakova-Partensky, L., Shane, T., Koide, A., Koide, S., Miller, C., & Newstead, S. (2015) · Nature · doi:10.1038/nature14981 · Cited by 119
Self-citationBilela, L. L., Matijošytė, I., Krutkevičius, J., Alexandrino, D. A. M., Šafařı́k, I., Burlakovs, J., Gaudêncio, S. P., & Carvalho, M. F. (2023) · Marine Pollution Bulletin · doi:10.1016/j.marpolbul.2023.115309 · Cited by 107
Zirconium Metal–Organic Framework Materials for Efficient Ion Adsorption and Sieving
Hou, J., Wang, H., & Zhang, H. (2020) · Industrial & Engineering Chemistry Research · doi:10.1021/acs.iecr.0c02683 · Cited by 93
Transmembrane Fluoride Transport: Direct Measurement and Selectivity Studies
Clarke, H. J., Howe, E. N. W., Wu, X., Sommer, F., Yano, M., Light, M. E., Kubik, S., & Gale, P. A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b10694 · Cited by 88
Heavy Pnictogenium Cations as Transmembrane Anion Transporters in Vesicles and Erythrocytes
Park, G., Brock, D. J., Pellois, J., & Gabbaı̈, F. P. (2019) · Chem · doi:10.1016/j.chempr.2019.06.013 · Cited by 81
Why Is the Biodegradation of Polyfluorinated Compounds So Rare?
Wackett, L. P. (2021) · mSphere · doi:10.1128/msphere.00721-21 · Cited by 77
Stockbridge, R. B., & Wackett, L. P. (2024) · Nature Communications · doi:10.1038/s41467-024-49018-1 · Cited by 80
Self-citationMembrane exporters of fluoride ion
McIlwain, B. C., Ruprecht, M. T., & Stockbridge, R. B. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071520-112507 · Cited by 69
Self-citationHu, M., & Scott, C. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.00157-24 · Cited by 63
Evolutionary obstacles and not C–F bond strength make PFAS persistent
Wackett, L. P. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.14463 · Cited by 60
Dalby, F. R., Svane, S., Sigurðarson, J. J., Sørensen, M. K., Hansen, M. J., Karring, H., & Feilberg, A. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c01231 · Cited by 57
Calero, P., Gurdo, N., & Nikel, P. I. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16110 · Cited by 56
Triethylene Glycol Up-Regulates Virulence-Associated Genes and Proteins in Streptococcus mutans
Sadeghinejad, L., Cvitkovitch, D. G., Siqueira, W. L., Santerre, J. P., & Finer, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165760 · Cited by 56
Reconstitution and functional characterization of ion channels from nanodiscs in lipid bilayers
Winterstein, L.-M., Kukovetz, K., Rauh, O., Turman, D. L., Braun, C., Moroni, A., Schroeder, I., & Thiel, G. (2018) · The Journal of General Physiology · doi:10.1085/jgp.201711904 · Cited by 43
Confronting PFAS persistence: enzymes catalyzing C–F bond cleavage
Wackett, L. P. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.11.001 · Cited by 37
Smith, K. D., Gordon, P. B., Rivetta, A., Allen, K. E., Berbasova, T., Slayman, C., & Strobel, S. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.651976 · Cited by 41
Mechanistic signs of double-barreled structure in a fluoride ion channel
Last, N. B., Kolmakova-Partensky, L., Shane, T., & Miller, C. (2016) · eLife · doi:10.7554/elife.18767 · Cited by 34
Self-citationFacts and Fallacies of the Fluoride Controversy: A Contemporary Perspective
Samaranayake, L. P., Porntaveetus, T., Tsoi, J. K. H., & Tuygunov, N. (2025) · International Dental Journal · doi:10.1016/j.identj.2025.04.013 · Cited by 33
Павлович, Ч. С., Hkudaigulov, G., Шарипов, Д. А., Starikov, S., & Четверикова, Д. В. (2023) · Toxics · doi:10.3390/toxics11121001 · Cited by 32
Zhu, J., Xing, A., Wu, Z., Tao, J., Ma, Y., Wen, B., Zhu, X., Fang, W., & Wang, Y. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b00509 · Cited by 32
Bygd, M. D., Aukema, K. G., Richman, J. E., & Wackett, L. P. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.00288-22 · Cited by 30
Small Molecule Fluoride Toxicity Agonists
Nelson, J. W., Plummer, M. S., Blount, K. F., Ames, T. D., & Breaker, R. R. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.03.016 · Cited by 30
Selective Fluoride Transport in Subnanometer TiO 2 Pores
Zhou, X., Heiranian, M., Yang, M., Epsztein, R., Gong, K., White, C. E., Hu, S., Kim, J., & Elimelech, M. (2021) · ACS Nano · doi:10.1021/acsnano.1c07210 · Cited by 29
Fluoride: a risk factor for inflammatory bowel disease?
Follin‐Arbelet, B., & Moum, B. A. (2016) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365521.2016.1177855 · Cited by 28
An Engineered E. coli Strain for Direct in Vivo Fluorination
Markakis, K., Lowe, P. T., Davison‐Gates, L., O'Hagan, D., Rosser, S. J., & Elfick, A. (2020) · ChemBioChem · doi:10.1002/cbic.202000051 · Cited by 27
Song, J., Hou, C., Guo, J., Niu, Q., Wang, X., Ren, Z., Zhang, Q., Feng, C., Liu, L., Tian, W., et al. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c03444 · Cited by 27
Pseudomonas : versatile biocatalysts for PFAS
Wackett, L. P. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.15990 · Cited by 27
Atlas of the microbial degradation of fluorinated pesticides
Alexandrino, D. A. M., Mucha, A. P., Almeida, C. M. R., & Carvalho, M. F. (2021) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2021.1977234 · Cited by 24
The fluoride permeation pathway and anion recognition in Fluc family fluoride channels
McIlwain, B. C., Gundepudi, R., Koff, B. B., & Stockbridge, R. B. (2021) · eLife · doi:10.7554/elife.69482 · Cited by 24
Self-citationDodge, A. G., Thoma, C. J., O’Connor, M. R., & Wackett, L. P. (2024) · mBio · doi:10.1128/mbio.02785-23 · Cited by 23
Comparative genomics of the transportome of Ten Treponema species
Buyuktimkin, B., Zafar, H., & Saier, M. H. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.04.034 · Cited by 22
Li, M., Zhao, X. Y., Yan, P., Xie, H., Zhang, J., Wu, S., & Wu, H. (2024) · Environmental Research · doi:10.1016/j.envres.2024.119967 · Cited by 21
Calle-Castañeda, S. M., Godoy, M. A. M., & Hernandez-Ortiz, J. P. (2017) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-017-2390-7 · Cited by 20
Han, S., Washio, J., Abiko, Y., Zhang, L., & Takahashi, N. (2023) · Caries Research · doi:10.1159/000534055 · Cited by 20
A topologically diverse family of fluoride channels
Macdonald, C. B., & Stockbridge, R. B. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.04.003 · Cited by 21
Self-citationAn interfacial sodium ion is an essential structural feature of fluc family fluoride channels
McIlwain, B. C., Martin, K., Hayter, E. A., & Stockbridge, R. B. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.007 · Cited by 24
Self-citationBanerjee, A., Kang, C.-Y., An, M., Koff, B. B., Sunder, S., Kumar, A., Tenuta, L. M. A., & Stockbridge, R. B. (2024) · mBio · doi:10.1128/mbio.00184-24 · Cited by 17
Self-citationIon permeation, selectivity, and electronic polarization in fluoride channels
Yue, Z., Wang, Z., & Voth, G. A. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.02.019 · Cited by 17
Wang, Z., & Wu, Z. (2025) · Bioresource Technology · doi:10.1016/j.biortech.2025.132854 · Cited by 16
Turman, D. L., & Stockbridge, R. B. (2017) · Journal of General Physiology · doi:10.1085/jgp.201611747 · Cited by 15
Self-citationTransmembrane transport of fluoride studied by time-resolved emission spectroscopy
Cataldo, A., Chvojka, M., Park, G., Šindelář, V., Gabbaı̈, F. P., Butler, S. J., & Valkenier, H. (2023) · Chemical Communications · doi:10.1039/d3cc00897e · Cited by 16
Nitrate and Phosphate Transporters Rescue Fluoride Toxicity in Yeast
Johnston, N. R., & Strobel, S. A. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00315 · Cited by 16
Yao, S., Zhang, H., Zhang, J., Luo, Y., Zhou, Y., & Kong, Q. (2024) · Process Safety and Environmental Protection · doi:10.1016/j.psep.2024.04.142 · Cited by 15
Thesai, A. S., Nagarajan, G., Rajakumar, S., Pugazhendhi, A., & Ayyasamy, P. M. (2021) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.124367 · Cited by 15
Shao, X., Hao, W., Konhauser, K. O., Gao, Y., Tang, L., Su, M., & Li, Z. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-15551-5 · Cited by 14
Patra, A. K., Srimayee, S., Halder, D., Roy, A., Mukherjee, S., Kundu, S., Hossain, M., Saha, R., Lee, C., Manna, D., et al. (2023) · Chemical Communications · doi:10.1039/d3cc02032k · Cited by 13
Transmembrane Fluoride Transport by a Cyclic Azapeptide With Two β-Turns
Zhao, Z., Zhang, M., Tang, B., Weng, P., Zhang, Y., Yan, X., Li, Z., & Jiang, Y. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2020.621323 · Cited by 12
Alexandrino, D. A. M., Mucha, A. P., Tomasino, M. P., Almeida, C. M. R., & Carvalho, M. F. (2021) · Microorganisms · doi:10.3390/microorganisms9102109 · Cited by 12
Potassium alleviates fluoride accumulation and enhances fluoride tolerance in Camellia sinensis
Sun, Y., Wu, Z., Xing, A., Zhang, H., Xu, X., Gong, Z., Zhao, Z., Liu, S., Chen, X., Li, X., et al. (2024) · Industrial Crops and Products · doi:10.1016/j.indcrop.2024.119062 · Cited by 11
Cells Adapt to Resist Fluoride through Metabolic Deactivation and Intracellular Acidification
Johnston, N. R., Cline, G., & Strobel, S. A. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00222 · Cited by 9
Molecular Interactions between a Fluoride Ion Channel and Synthetic Protein Blockers
Turman, D. L., Cheloff, A. Z., Corrado, A. D., Nathanson, J. T., & Miller, C. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01272 · Cited by 10
Self-citationFluoride permeation mechanism of the Fluc channel in liposomes revealed by solid-state NMR
Zhang, J., Song, D., Schackert, F. K., Li, J., Xiang, S., Tian, C., Gong, W., Carloni, P., Alfonso‐Prieto, M., & Shi, C. (2023) · Science Advances · doi:10.1126/sciadv.adg9709 · Cited by 10
Yu, Y., Lin, W.-H., Surampalli, R. Y., Chen, S., & Kao, C. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.138628 · Cited by 9
Uncovering the Mechanism of the Proton-Coupled Fluoride Transport in the CLC F Antiporter
Mills, K. R., & Torabifard, H. (2023) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01228 · Cited by 9
Hertz, L. M., White, E. N., Kuznedelov, K. D., Cheng, L., Yu, A. M., Kakkaramadam, R., Severinov, K., Chen, A. A., & Lucks, J. B. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae231 · Cited by 8
Wu, Z., Xing, A., Chu, R., Xu, X., Sun, Y., Zhu, J., Yang, Y., Yin, J., & Wang, Y. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.116407 · Cited by 8
Defluorination of monofluorinated alkane by Rhodococcus sp. NJF-7 isolated from soil
Yan, M., Gao, Z., Xiang, X., Wang, Q., Song, X., Wu, Y., Löffler, F. E., Zeng, J., & Lin, X. (2024) · AMB Express · doi:10.1186/s13568-024-01729-w · Cited by 8
The mechanisms of chromogranin B-regulated Cl− homeostasis
Jiang, Q., & Yadav, G. P. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220435 · Cited by 8
Microwell fluoride assay screening for enzymatic defluorination
Wackett, L. P. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.12.020 · Cited by 5
Wintenberg, M., Vasilyeva, O. B., & Schaffter, S. W. (2025) · BMC Genomics · doi:10.1186/s12864-025-12109-4 · Cited by 4
Toward a molecular understanding of fluoride stress in a model Pseudomonas strain
Wackett, L. P. (2022) · Environmental Microbiology · doi:10.1111/1462-2920.16114 · Cited by 4
Effect of Arsenic on Fluoride Tolerance in Microbacterium paraoxydans Strain IR-1
Mathur, M., Rawat, N., Saxena, T., Khandelwal, R., Jain, N., Sharma, M. K., Medicherla, K. M., Bhatnagar, P., Flora, S. J. S., & Kaushik, P. (2023) · Toxics · doi:10.3390/toxics11110945 · Cited by 3
Banerjee, A., Pickelner, S. M. P., Smith, F., Tenuta, L. M. A., & Stockbridge, R. B. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2511884122 · Cited by 3
Self-citationDong, W., & Setlow, P. (2019) · Journal of Applied Microbiology · doi:10.1111/jam.14155 · Cited by 3
Impairing fluoride export of Aspergillus fumigatus mitigates its voriconazole resistance
Binder, J., Held, J., & Krappmann, S. (2019) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2019.02.003 · Cited by 3
Kang, C.-Y., An, M., & Stockbridge, R. B. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.01.012 · Cited by 3
Self-citationMicrobial Remediation of Groundwater Fluoride Contamination: Prospect for Environmental Clean-up
Buragohain, K., & Nath, R. (2025) · Water Air & Soil Pollution · doi:10.1007/s11270-025-08931-x · Cited by 2
Metabolic Engineering of Escherichia coli for Fumarate Production from Ethanol
Liu, J., Liu, M., Chen, G., Feng, X., Ji, M., Bao, Z., Zhang, R., Xian, M., & Zhao, G. (2026) · ACS Synthetic Biology · doi:10.1021/acssynbio.5c00826 · Cited by 2
Babajko, S., Buzalaf, M. A. R., Fini, J., & Pamela, D. B. (2026) · Calcified Tissue International · doi:10.1007/s00223-026-01525-7 · Cited by 2
Methods for the recycling of fluoropolymers: A review
Chapman, B. R. P., Anderson, P. A., Kentish, S. E., & Leeke, G. A. (2026) · Resources Conservation and Recycling · doi:10.1016/j.resconrec.2026.108970 · Cited by 2
Dafalla, M., EL-SAYED, W. S., Memuduaghan, A., Omar, H., Ismail, W. A., & Hamza, R. (2026) · Applied Sciences · doi:10.3390/app16167945 · Cited by 2
Fluoride Transport and Inhibition Across CLC Transporters
Asgharpour, S., Chi, L. A., Spehr, M., Carloni, P., & Alfonso‐Prieto, M. (2022) · Handbook of experimental pharmacology · doi:10.1007/164_2022_593 · Cited by 2
Measurement and analysis of microbial fluoride resistance in dental biofilm models
Banerjee, A., Stockbridge, R. B., & Tenuta, L. M. A. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2023.12.018 · Cited by 2
Self-citationYadav, P. R., & Basha, S. H. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1951356 · Cited by 2
Biodegradation of fluorinated octanoic acids in an O2-based membrane biofilm reactor
Gao, T.-Y., Luo, Y., Long, M., Zhou, C., Cai, Y., Zhao, H., & Rittmann, B. E. (2025) · Water Research X · doi:10.1016/j.wroa.2025.100462
Protein ligands for studying ion channel proteins
Chavan, T., Maduke, M. C., & Swartz, K. J. (2017) · The Journal of General Physiology · doi:10.1085/jgp.201711776 · Cited by 1
Adaptation Potential of Three Psychrotolerant Aquatic Bacteria in the Pan-Okhotsk Region
Voronina, O. L., Kunda, M. S., Ryzhova, N. N., Aksenova, E. I., Novikova, O. D., & Al, G. (2022) · Water · doi:10.3390/w14071107 · Cited by 1
Electrophysiology of fluoride channels in the yeasts Saccharomyces cerevisiae and Candida albicans
Rivetta, A., & Slayman, C. L. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.01.005 · Cited by 1
A call to expand the dimensions of halide-philicity
Wackett, L. P., & Stockbridge, R. B. (2026) · mBio · doi:10.1128/mbio.01084-26 · Cited by 1
Self-citationOf lipid transfer, resistance to F−, and stimulus-dependent channel conformations
Adler, E. M. (2014) · The Journal of General Physiology · doi:10.1085/jgp.201411265
Passive Passage: Investigation of Pore Lining Residues in Fluc type F- Ion Channels
Pham, M. (2016) · Brandeis Institutional Repository
Characterization of Fluoride Ion Channel interactions with synthetic crystallization chaperones
Cheloff, A. Z. (2018) · Brandeis Institutional Repository · doi:10.48617/etd.847
Mills, K., & Torabifard, H. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.01.006
Global Fluoride Toxicology Landscape: Bibliometric Approaches and Scientific Mapping
Ferreira, M. K. M., Souza‐Monteiro, D., Nascimento, P. C., Eiró‐Quirino, L., Bittencourt, L. O., Zohoori, F. V., Martinez-Mier, E. A., Buzalaf, M. A. R., & Lima, R. R. (2025) · Environmental Toxicology · doi:10.1002/tox.24600
Xing, A., Peng, C., Tang, Y., Cao, R., Ma, S., Xu, X., Wu, Z., Sun, Y., Wang, C., Liu, S., et al. (2026) · Horticulturae · doi:10.3390/horticulturae12010094
CLC F , Not CrcB , Protects Pseudomonas putida ATCC 12633 During Intense Fluoride Stress
Dodge, A. G., O’Connor, M. R., & Wackett, L. P. (2026) · Environmental Microbiology · doi:10.1111/1462-2920.70385
A growth-based screening method to detect defluorinating enzymesPreprint
Idowu, A., Rathbun, C. M., & Schroer, H. W. (2026) · ChemRxiv · doi:10.26434/chemrxiv.15006506/v2
Advances in transmembrane anion transport by discrete molecular carriers
York, E., Quesada, R., & Gale, P. A. (2026) · Australian Journal of Chemistry · doi:10.1071/ch26059
Chen, M., Liu, W., Bu, Y., Song, X., 张二林, & Hu, J. (2026) · Biomaterials · doi:10.1016/j.biomaterials.2026.124687
Zhao, J., Song, K., Hou, X., Jing, H., Li, Y., & Wu, Y. (2026) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2026.119396
Metadata
- Authors
- Ji, C., Stockbridge, R. B., & Miller, C.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Miller, Christopher
- Venue
- Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 2014-08-25
- Volume
- 144
- Issue
- 3
- Pages
- 257-261
- ISSN
- 0022-1295 (ISSN-L)
- 1540-7748
- PMC
- PMC4144673
- OpenAlex
- W2331349292
- Semantic Scholar
- 41705fa505ea1c12e93f2c74e5ea69338c0e6935
- Cited by
- 97
- References
- 14
- Citations by year
- 2026: 11 · 2025: 8 · 2024: 16 · 2023: 9 · 2022: 9 · 2021: 11 · 2020: 8 · 2019: 6 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 3 · 2014: 1
- FWCI
- 1.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of General Physiology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (K99GM111767, R01GM107023)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Keywords
- fluoride resistance, fluoride accumulation, Escherichia coli, transmembrane pH gradient, bacterial growth inhibition, fluoride toxicity, ion channel selectivity
- MeSH terms
- Escherichia coli, Fluorides, Hydrogen-Ion Concentration, Ion Channels, Ion Transport, Escherichia coli Proteins, Cell Proliferation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
A language model drew the claims from the paper on 2026-11-10, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-11-10 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
