GO:0140831 L-asparagine, sodium:proton antiporter activity: Mechanism, Genes and Research Methods
Research-grade guide for scientists and biopharma professionals
Key Takeaways
• GO:0140831 describes a secondary-active antiporter that couples the inward movement of L-asparagine and Na+ to the outward movement of H+ across a membrane.
• L-asparagine uptake via this antiporter is experimentally linked to stimulation of Na+/H+ exchange and to induction of ornithine decarboxylase (ODC) activity in intestinal epithelial cells.
• The transport reaction is electroneutral in the QuickGO definition: H+(in) + L-asparagine(out) + Na+(out) = H+(out) + L-asparagine(in) + Na+(in).
• Na+/H+ exchanger (NHE/SLC9) proteins are the best-characterized molecular context for this activity; transmembrane histidines and acidic residues in extracellular loop 3 are critical for cation transport.
• Bacterial and plant Na+/H+ antiporters such as Vibrio alginolyticus NhaA and Arabidopsis AtCHX17 provide structural and mutational frameworks for understanding antiporter core residues.
• CRISPR knockout, point-mutation, knock-in and overexpression models enable causal testing of candidate antiporter genes in asparagine-dependent proliferation and stress-response pathways.
Description
GO:0140831, L-asparagine, sodium:proton antiporter activity, is a molecular function that enables the coupled transfer of L-asparagine and sodium ions in one direction and protons in the opposite direction across a membrane. The QuickGO definition specifies the reaction H+(in) + L-asparagine(out) + Na+(out) = H+(out) + L-asparagine(in) + Na+(in), placing this activity within the broader family of solute:cation antiporters. This function is of direct interest to researchers studying nutrient transport, intestinal epithelial physiology and the metabolic regulation of cell proliferation, because L-asparagine is a non-essential amino acid that can act as a growth signal in specific tissues. Experimental work in porcine jejunal enterocytes showed that L-asparagine and L-glutamine stimulate Na+/H+ exchange, providing functional evidence that asparagine handling is coupled to sodium-proton antiport. A related study demonstrated that L-asparagine can induce ornithine decarboxylase (ODC) activity, a key step in polyamine biosynthesis and cell proliferation, and proposed a role for membrane Na+/H+ antiport in this induction. Together with ODC stimulation and enterocyte proliferation data, these findings position GO:0140831 as a transport activity that connects amino acid availability to growth-related signaling. Understanding this activity is therefore relevant to cancer metabolism, intestinal biology and the design of transport-targeted experimental models.
L-asparagine, sodium:proton antiporter activity At A Glance
| GO ID | GO:0140831 |
|---|---|
| GO term | L-asparagine, sodium:proton antiporter activity |
| Ontology | molecular_function |
| Synonym | None listed in QuickGO |
| Major function | Coupled antiport of L-asparagine and Na+ inward with H+ outward across a membrane |
| Reaction | H+(in) + L-asparagine(out) + Na+(out) = H+(out) + L-asparagine(in) + Na+(in) |
| Transport class | Secondary active solute:cation antiporter |
| Representative protein context | Na+/H+ exchanger (NHE/SLC9) family and related antiporters |
| Physiological link | L-asparagine-stimulated Na+/H+ exchange and ODC induction in intestinal epithelial cells |
What Is GO:0140831?
In practical terms, GO:0140831 describes a membrane-embedded antiporter that moves one molecule of L-asparagine and one sodium ion into the cell while moving one proton out of the cell. The process is a form of secondary active transport: the antiporter does not hydrolyze ATP directly but instead uses the electrochemical gradients of Na+ and H+ to drive asparagine translocation. The QuickGO reaction is H+(in) + L-asparagine(out) + Na+(out) = H+(out) + L-asparagine(in) + Na+(in), which is electroneutral because one positive charge enters with Na+ and one positive charge leaves with H+. This distinguishes the activity from electrogenic amino acid transporters and from pure Na+/H+ exchangers that do not carry an amino acid substrate. The term is annotated as a molecular_function, and its experimental support comes from studies of Na+/H+ exchange stimulated by L-asparagine in intestinal cells and from ODC induction by L-asparagine that is sensitive to Na+/H+ antiport.
Why Is L-asparagine, sodium:proton antiporter activity Important in Cell Biology?
GO:0140831 matters because it links the availability of a specific amino acid, L-asparagine, to ion gradients and to downstream growth-related processes. In intestinal epithelial cells, L-asparagine and L-glutamine stimulate Na+/H+ exchange, and L-asparagine can induce ODC activity, a rate-limiting enzyme in polyamine biosynthesis. Because polyamines are required for cell proliferation, an antiporter that controls asparagine influx could influence epithelial renewal and tissue repair. The activity also sits at the intersection of amino acid transport and pH regulation, since H+ movement is intrinsic to the reaction. Mutational studies of Na+/H+ exchangers have identified transmembrane histidines and extracellular loop acidic residues as important for cation transport, providing a mechanistic template for how antiporters achieve coupled substrate movement. Bacterial and plant antiporters such as NhaA and AtCHX17 further show that core residues in unwound alpha-helices and membrane-spanning aspartic residues are functionally critical. For biomedical researchers, this term is therefore a useful entry point for studying nutrient sensing, epithelial physiology and antiporter structure-function relationships.
• Provides a mechanistic explanation for how L-asparagine uptake can be coupled to Na+ and H+ gradients in epithelial cells.
• Connects amino acid transport to ODC induction and polyamine biosynthesis, which are required for cell proliferation.
• Offers a functional context for interpreting Na+/H+ exchanger mutations that abolish or alter cation transport.
• Highlights conserved antiporter residues, including transmembrane histidines and acidic loop residues, that can be tested by mutagenesis.
• Supports comparative studies with bacterial NhaA and plant AtCHX17 to understand antiporter core architecture.
• Relevant to intestinal epithelial biology, where asparagine and glutamine stimulate Na+/H+ exchange and enterocyte proliferation.
• Provides a rationale for CRISPR-based dissection of candidate antiporter genes in metabolic and transport studies.
• Useful for cancer metabolism research because asparagine availability can influence proliferation in some cell contexts.
• Guides design of transport assays that monitor pH, sodium flux and amino acid uptake simultaneously.
• Helps annotate uncharacterized transporters that carry both amino acid and cation flux activities.
What Happens During L-asparagine, sodium:proton antiporter activity?
Substrate recognition at the membrane
In simple terms: The transporter first recognizes L-asparagine and sodium on the outside of the cell.
The antiporter must bind L-asparagine and Na+ from the extracellular or luminal side before translocation. In intestinal enterocytes, L-asparagine and L-glutamine stimulate Na+/H+ exchange, indicating that asparagine availability is sensed at the membrane and coupled to cation flux. The QuickGO reaction specifies L-asparagine(out) and Na+(out) as co-substrates entering the transport cycle, while H+(in) is the counter-substrate. This step is analogous to substrate recognition in other Na+/H+ exchangers, where transmembrane histidines contribute to cation binding and transport.
Coupled translocation of L-asparagine and Na+ inward
In simple terms: The transporter moves asparagine and sodium into the cell at the same time.
During the transport cycle, L-asparagine and Na+ are translocated from the outer side to the inner side of the membrane. The reaction H+(in) + L-asparagine(out) + Na+(out) = H+(out) + L-asparagine(in) + Na+(in) describes this coupled inward movement. Functional evidence for coupling comes from the observation that L-asparagine stimulates Na+/H+ exchange in porcine jejunal enterocytes, linking asparagine handling to sodium-proton antiport activity. Mutational analysis of Na+/H+ exchangers has shown that specific transmembrane histidines are required for normal cation transport, suggesting that similar residues may participate in the coupled translocation step of asparagine-dependent antiport.
Proton counter-transport and pH coupling
In simple terms: While asparagine and sodium go in, a proton goes out, so the cell's pH balance is part of the process.
The antiporter exports H+ as L-asparagine and Na+ enter, making the reaction electroneutral according to the QuickGO definition. This proton counter-transport ties the activity to cellular pH regulation. Acidic residues in extracellular loop 3 of Na+/H+ exchanger type 1 are important in cation transport, indicating that proton and cation pathways are structurally linked. A human SLC9A1 mutation that abolishes Na+/H+ exchanger activity further demonstrates how single residue changes can disrupt the coupled transport mechanism. In plant AtCHX17, core residues in unwound alpha-helices provide insights into transport function, supporting the idea that helix architecture is critical for antiporter activity.
Downstream metabolic signaling
In simple terms: After asparagine enters, it can trigger growth-related signals inside the cell.
L-asparagine influx via this activity has been linked to downstream metabolic effects. L-glutamine and L-asparagine stimulate ODC activity and proliferation in a porcine jejunal enterocyte line, connecting transport to polyamine biosynthesis. A separate study proposed a role for membrane Na+/H+ antiport in ODC induction by L-asparagine, suggesting that the antiporter is part of a signaling axis that responds to asparagine availability. These findings indicate that GO:0140831 is not merely a passive transport event but can be coupled to growth-regulatory pathways in epithelial cells.
Conserved antiporter core residues
In simple terms: Certain amino acids in the transporter protein are essential for it to work, and these are conserved across species.
Mutational studies have identified critical residues in antiporter proteins. Three aspartic residues in membrane-spanning regions of the Vibrio alginolyticus Na+/H+ antiporter play a role in carrier activity, showing that acidic residues are functionally important. In plant AtCHX17, protein architecture and core residues in unwound alpha-helices provide insights into transport function. Transmembrane histidines in the amiloride-sensitive Na+/H+ exchanger are also required for normal transport, reinforcing the idea that a conserved set of polar and charged residues forms the translocation core. These findings provide a structural framework for hypothesizing which residues mediate L-asparagine, sodium:proton antiporter activity.
Key Genes Involved in GO:0140831 L-asparagine, sodium:proton antiporter activity
The following genes and proteins are experimentally or mechanistically linked to Na+/H+ exchange, antiporter function or L-asparagine-stimulated transport processes relevant to GO:0140831.
| Gene | Major Role | Research Relevance |
|---|---|---|
| SLC9A1 (NHE1) | Na+/H+ exchanger type 1; cation transport and pH regulation | Human mutation abolishes Na+/H+ exchanger activity; extracellular loop 3 acidic residues affect cation transport |
| SLC9A family (NHE isoforms) | Sodium-proton antiport across membranes | Model system for studying coupled cation transport and antiporter pharmacology |
| NHA1 / NhaA (Vibrio alginolyticus) | Bacterial Na+/H+ antiporter | Membrane-spanning aspartic residues are required for carrier activity |
| AtCHX17 (Arabidopsis) | Plant cation/H+ exchanger | Core residues in unwound alpha-helices inform antiporter transport function |
| ODC1 | Ornithine decarboxylase; polyamine biosynthesis | L-asparagine stimulates ODC activity and proliferation in enterocytes |
| SLC1A5 (ASCT2) | Glutamine and asparagine transport context | Amino acid availability influences Na+-coupled transport and proliferation |
| SLC38A family | Sodium-coupled amino acid transporters | Comparative framework for Na+-dependent amino acid uptake |
| SLC7A family | Amino acid transporters | Context for asparagine handling in epithelial and cancer cells |
| ATP1A1 (Na+/K+-ATPase) | Maintains sodium gradient | Indirectly supports secondary active antiport by providing Na+ gradient |
| SLC4A family | Bicarbonate and pH regulation | Functional context for pH-coupled transport processes |
| SLC9A3 (NHE3) | Apical Na+/H+ exchange in epithelia | Intestinal Na+/H+ exchange is stimulated by L-asparagine and L-glutamine |
| SLC9A2 (NHE2) | Epithelial Na+/H+ exchange | Potential contributor to asparagine-stimulated cation flux in gut |
| GLS | Glutaminase; glutamine metabolism | Glutamine and asparagine jointly stimulate ODC and proliferation |
| MYC | Proliferation-associated transcription factor | Downstream context for ODC induction and polyamine-driven growth |
| SLC25A family | Mitochondrial carriers | Comparative context for solute transport mechanisms |
| H+/amino acid antiporters (general) | Coupled amino acid and proton transport | Mechanistic comparison for GO:0140831 reaction stoichiometry |
How Is L-asparagine, sodium:proton antiporter activity Regulated?
Regulation of L-asparagine, sodium:proton antiporter activity is not fully defined in the verified literature, but several regulatory themes emerge. The activity is stimulated by extracellular L-asparagine and L-glutamine in intestinal enterocytes, indicating substrate-dependent activation of Na+/H+ exchange. ODC induction by L-asparagine appears to involve membrane Na+/H+ antiport, suggesting that the antiporter can be functionally coupled to polyamine biosynthetic signaling. Na+/H+ exchanger activity itself is sensitive to mutations in transmembrane histidines and extracellular loop acidic residues, which alter cation transport and can abolish activity. In bacteria and plants, antiporter function depends on conserved acidic and polar residues within membrane-spanning regions and unwound helices, providing a structural basis for activity regulation. These observations support a model in which substrate availability, ion gradients and specific protein residues jointly regulate the antiport reaction.
L-asparagine, sodium:proton antiporter activity and Human Disease
| Gene | Disease / Biology | Potential Experimental Model |
|---|---|---|
| SLC9A1 | Loss of Na+/H+ exchanger activity due to human mutation | Point-mutation knock-in of the patient variant in cell lines |
| SLC9A1 | Altered cation transport from extracellular loop 3 changes | Site-directed mutagenesis and transport assays |
| ODC1 | Polyamine biosynthesis and proliferation in intestinal epithelium | Overexpression and knockout in enterocyte lines |
| NhaA (V. alginolyticus) | Bacterial antiporter activity dependent on aspartic residues | Bacterial mutagenesis and complementation |
| AtCHX17 | Plant antiporter transport function and core helix residues | Plant mutant and heterologous expression models |
Na+/H+ exchanger dysfunction and human disease
A novel human mutation in SLC9A1 results in abolition of Na+/H+ exchanger activity, demonstrating that loss-of-function changes in antiporter proteins can have direct physiological consequences. Because GO:0140831 involves coupled Na+ and H+ movement, mutations that disrupt cation transport in NHE proteins provide a disease-relevant template for understanding how antiporter dysfunction may affect cellular pH and ion homeostasis. Acidic residues in extracellular loop 3 of Na+/H+ exchanger type 1 are important in cation transport, further highlighting residues that could be altered in pathological states.
Intestinal epithelial proliferation and polyamine metabolism
L-glutamine and L-asparagine stimulate ODC activity and proliferation in a porcine jejunal enterocyte line, linking asparagine handling to epithelial growth. A related study proposed a role for membrane Na+/H+ antiport in ODC induction by L-asparagine, connecting the transport activity to polyamine biosynthesis. Dysregulation of these pathways could contribute to altered epithelial renewal or proliferative disorders, making GO:0140831 relevant to intestinal biology and cancer metabolism research.
Cancer metabolism and asparagine dependence
Asparagine availability can influence proliferation in some cell contexts, and ODC induction is a growth-associated response. Because GO:0140831 describes a route for L-asparagine entry coupled to Na+ and H+ gradients, it may contribute to asparagine-dependent metabolic programs in proliferating cells. Experimental models that manipulate antiporter genes could help determine whether this activity is required for asparagine-driven proliferation.
Bacterial and plant antiporter models for transport disease
The Vibrio alginolyticus Na+/H+ antiporter requires three membrane-spanning aspartic residues for activity, and plant AtCHX17 core residues inform transport function. These non-human models provide conserved structural insights that can be translated to human antiporter biology relevant to GO:0140831. They also offer experimental systems for testing residue-level mechanisms that may parallel human transport disorders.
From L-asparagine, sodium:proton antiporter activity-Related Genes to Experimental Models
| Research Question | Suitable Model |
|---|---|
| Is a candidate gene required for L-asparagine-stimulated Na+/H+ exchange? | CRISPR knockout in intestinal epithelial cells followed by pH and sodium flux assays |
| Does a specific residue mediate cation transport? | Point-mutation knock-in of histidine or acidic residues in SLC9A1 |
| Can a disease-associated antiporter mutation abolish activity? | Knock-in of the human SLC9A1 mutation and transport measurement |
| Does overexpression of an antiporter increase asparagine uptake? | Overexpression cell model with labeled asparagine uptake |
| Is ODC induction dependent on antiporter activity? | Knockout or pharmacological inhibition combined with ODC activity assay |
| Are conserved acidic residues required in a bacterial antiporter? | Site-directed mutagenesis of NhaA aspartic residues |
How to Study the L-asparagine, sodium:proton antiporter activity Process
| Method | What It Measures | Typical Application |
|---|---|---|
| Intracellular pH imaging | Changes in H+ flux | Detecting Na+/H+ exchange stimulated by L-asparagine |
| Sodium flux assay | Na+ movement across membranes | Testing coupled Na+ transport in antiporter models |
| Site-directed mutagenesis | Effect of specific residues on transport | Testing histidine and acidic residues in SLC9A1 |
| ODC activity assay | Ornithine decarboxylase enzyme activity | Measuring downstream response to L-asparagine |
| Cell proliferation assay | Growth rate of enterocyte or cancer cells | Linking transport to proliferation |
| Heterologous expression | Function of antiporter in a new host | Studying bacterial and plant antiporters |
| Transport complementation | Restoration of transport in mutant strains | Testing NhaA aspartic residue mutants |
| Mutation screening | Identification of loss-of-function variants | Characterizing human SLC9A1 mutations |
Transport and pH flux assays
Measuring Na+/H+ exchange and asparagine-coupled transport requires assays that detect changes in intracellular pH and sodium flux. Studies in porcine jejunal enterocytes used L-asparagine and L-glutamine to stimulate Na+/H+ exchange, providing a functional readout for this activity. Similar approaches can be applied to cells expressing wild-type or mutant antiporters to determine whether specific residues are required for transport.
Mutagenesis and residue-level analysis
Mutational analysis of transmembrane histidines in the amiloride-sensitive Na+/H+ exchanger identified residues important for cation transport. Acidic residues in extracellular loop 3 of Na+/H+ exchanger type 1 are also important in cation transport, and a human SLC9A1 mutation abolishes exchanger activity. These strategies can be adapted to test candidate residues in proteins hypothesized to carry L-asparagine, sodium:proton antiporter activity.
ODC activity and proliferation assays
Because L-asparagine stimulates ODC activity and proliferation in enterocytes, ODC enzyme assays and proliferation measurements can serve as downstream readouts of antiporter function. A proposed role for membrane Na+/H+ antiport in ODC induction by L-asparagine further supports combining transport measurements with ODC activity assays. These methods help connect GO:0140831 to polyamine biosynthesis and growth responses.
Comparative antiporter studies
Bacterial and plant antiporters provide tractable systems for structure-function analysis. Three aspartic residues in membrane-spanning regions of the Vibrio alginolyticus Na+/H+ antiporter play a role in carrier activity, and AtCHX17 core residues in unwound alpha-helices provide insights into transport function. Comparative studies can identify conserved mechanisms relevant to L-asparagine, sodium:proton antiporter activity.
How CRISPR Can Be Used to Study GO:0140831 L-asparagine, sodium:proton antiporter activity
Knockout
CRISPR knockout of candidate antiporter genes can test whether they are required for L-asparagine-stimulated Na+/H+ exchange. Because L-asparagine and L-glutamine stimulate Na+/H+ exchange in enterocytes, knockout lines can be challenged with these amino acids and assayed for pH and sodium flux. Knockout of ODC1 or related genes can also test downstream polyamine responses to asparagine.
Point Mutation
Point-mutation models are valuable for testing residues implicated in cation transport. Transmembrane histidines and extracellular loop 3 acidic residues are important for Na+/H+ exchanger activity, and a human SLC9A1 mutation abolishes exchanger function. CRISPR point-mutation knock-in can recreate these variants to study their effect on L-asparagine, sodium:proton antiporter activity.
Knock-in
Knock-in of tagged or disease-associated alleles allows precise tracking of antiporter expression and function. A human SLC9A1 mutation that abolishes Na+/H+ exchanger activity can be introduced into cell lines to model loss of transport. Tagged knock-in of antiporter genes can also support localization studies in epithelial cells where asparagine stimulates Na+/H+ exchange.
Overexpression
Overexpression of candidate antiporters can test whether increased protein levels enhance L-asparagine uptake or Na+/H+ exchange. Since L-asparagine and L-glutamine stimulate Na+/H+ exchange and ODC activity, overexpression models can be used to amplify transport signals and measure downstream proliferation. Comparative overexpression of wild-type and mutant antiporters can reveal residue-specific effects.
How EDITGENE Supports L-asparagine, sodium:proton antiporter activity Research
Researchers studying L-asparagine, sodium:proton antiporter activity-related genes often need to determine whether a candidate gene is causally involved in coupled amino acid and cation transport, or whether it merely correlates with the phenotype. Establishing causality typically requires loss-of-function, gain-of-function and precise residue-level perturbations in relevant cell models. EDITGENE provides CRISPR-based tools and bioinformatics support to build these models and interpret the resulting transport, metabolic and proliferation data.
Contact EDITGENE today to design your custom CRISPR model for L-asparagine, sodium:proton antiporter activity research.
Frequently Asked Questions About L-asparagine, sodium:proton antiporter activity
What is GO:0140831 L-asparagine, sodium:proton antiporter activity?
GO:0140831 is a molecular function describing an antiporter that couples inward movement of L-asparagine and Na+ to outward movement of H+, according to the reaction H+(in) + L-asparagine(out) + Na+(out) = H+(out) + L-asparagine(in) + Na+(in).
What genes are involved in L-asparagine, sodium:proton antiporter activity?
Genes and proteins experimentally linked to this activity include SLC9A1/NHE1 and related Na+/H+ exchangers, ODC1 in the downstream polyamine pathway, and conserved antiporters such as NhaA and AtCHX17.
How is L-asparagine, sodium:proton antiporter activity measured?
It can be measured using intracellular pH imaging, sodium flux assays and amino acid uptake assays, often combined with ODC activity or proliferation readouts in enterocyte models.
Why is L-asparagine important for Na+/H+ exchange?
L-asparagine and L-glutamine stimulate Na+/H+ exchange in porcine jejunal enterocytes, and L-asparagine can induce ODC activity through a mechanism proposed to involve membrane Na+/H+ antiport.
Which residues are important for Na+/H+ exchanger activity?
Transmembrane histidines and acidic residues in extracellular loop 3 of Na+/H+ exchanger type 1 are important for cation transport, and a human SLC9A1 mutation abolishes exchanger activity.
What is the difference between GO:0140831 and a general Na+/H+ exchanger?
GO:0140831 specifically includes L-asparagine as a co-substrate along with Na+ and H+, whereas a general Na+/H+ exchanger only couples Na+ and H+ movement.
Can CRISPR knockout help study L-asparagine, sodium:proton antiporter activity?
Yes, CRISPR knockout of candidate antiporter genes can test whether they are required for L-asparagine-stimulated Na+/H+ exchange and downstream ODC induction.
What diseases are linked to Na+/H+ exchanger dysfunction?
A human SLC9A1 mutation abolishes Na+/H+ exchanger activity, and altered cation transport residues have been characterized, providing disease-relevant context for antiporter dysfunction.
What model systems are used to study antiporter core residues?
Bacterial NhaA and plant AtCHX17 are used to study conserved antiporter residues, including membrane-spanning aspartic residues and core residues in unwound alpha-helices.
How does L-asparagine, sodium:proton antiporter activity relate to cell proliferation?
L-asparagine stimulates ODC activity and proliferation in enterocytes, linking this transport activity to polyamine biosynthesis and growth-related signaling.
Conclusion
GO:0140831, L-asparagine, sodium:proton antiporter activity, defines a coupled transport function in which L-asparagine and Na+ enter a cell while H+ exits, as specified by the QuickGO reaction. Experimental evidence links L-asparagine to Na+/H+ exchange stimulation and ODC induction in intestinal epithelial cells, connecting this activity to polyamine biosynthesis and proliferation. Mutational studies of Na+/H+ exchangers and conserved antiporters have identified critical histidine, acidic and membrane-spanning residues that inform the mechanism of coupled transport. Researchers can use CRISPR knockout, point-mutation, knock-in and overexpression models to test causality and refine our understanding of this activity in health and disease.
References
- 1. Kandil HM et al.. 1995. L-glutamine and L-asparagine stimulate ODC activity and proliferation in a porcine jejunal enterocyte line.. Am J Physiol 269(4 Pt 1):G591-9 PMID: 7485512
- 2. Rhoads JM et al.. 1994. L-glutamine and L-asparagine stimulate Na+ -H+ exchange in porcine jejunal enterocytes.. Am J Physiol 266(5 Pt 1):G828-38 PMID: 8203529
- 3. Wang D et al.. 1995. Mutational analysis of transmembrane histidines in the amiloride-sensitive Na+/H+ exchanger.. Am J Physiol 269(2 Pt 1):C392-402 PMID: 7653521
- 4. Czerny DD et al.. 2016. Protein architecture and core residues in unwound α-helices provide insights to the transport function of plant AtCHX17.. Biochim Biophys Acta 1858(9):1983-1998 PMID: 27179641
- 5. Li X et al.. 2020. Acidic residues of extracellular loop 3 of the Na(+)/H(+) exchanger type 1 are important in cation transport.. Mol Cell Biochem 468(1-2):13-20 PMID: 32130622
- 6. Li X et al.. 2015. A novel human mutation in the SLC9A1 gene results in abolition of Na+/H+ exchanger activity.. PLoS One 10(3):e0119453 PMID: 25760855
- 7. Fong WF et al.. 1988. Possible role of the membrane Na+/H+ antiport in ornithine decarboxylase induction by L-asparagine.. Biochem Biophys Res Commun 155(2):937-42 PMID: 2844182
- 8. Nakamura T et al.. 1995. Three aspartic residues in membrane-spanning regions of Na+/H+ antiporter from Vibrio alginolyticus play a role in the activity of the carrier.. Biochim Biophys Acta 1230(3):170-6 PMID: 7619834
