nhaA Antibody

1. analysis of NhaA pH-dependent activation by molecular dynamics simulation of atomic details of proton-coupled transport across membrane PMID: 27708266
2. Lysine 300 has an essential role in stability but not electrogenic transport of Escherichia coli NhaA PMID: 28330875
3. Data show that the Li(+) binding, H(+) release and antiporter activity were all affected to the same extent by Na(+), Li(+)/H(+) antiporter (NhaA) mutations in the Li(+) binding site (D163E, D163N, D164N, D164E). PMID: 27021484
4. Data show that the two aspartic acid residues of Na+/H+ antiporter NhaA, D163 and D164, act as Na+ trap and energetic barrier for the transport of Na+. PMID: 26392528
5. NhaA antiporter functions using 10 helices, and an additional 2 contribute to assembly/stability. PMID: 26417087
6. As it has been previously suggested that Asp163 is one of the two residues through which proton transport occurs, these results have clear implications to the current mechanistic models of sodium-proton antiport in NhaA. PMID: 25422503
7. Data indicate that binding of Li+ to purified Na(+)/H(+) antiporter NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. PMID: 22915592
8. Data show that a Trp at position 136 specifically monitors a pH-induced conformational change that activates NhaA, whereas a Trp at position 339 senses a ligand-induced conformational change that does not occur until NhaA is activated at alkaline pH. PMID: 21873214
9. functional and structural interactions between transmembrane domains; an active conformation of NhaA PMID: 15039449
10. The molecular interactions established on Na(+) binding may represent an early step in NhaA activation. PMID: 15962009
11. crystal structure of pH-downregulated NhaA, the main antiporter of Escherichia coli PMID: 15988517
12. In the passive downhill uptake mode pH regulation of the carrier affects both apparent Km as well as turnover (Vmax). PMID: 16139785
13. folding rates of structural segments ranged from 0.31 s(-1) to 47 s(-1), providing detailed insight into a distinct folding hierarchy of an unfolded polypeptide into the native membrane protein structure PMID: 16298390
14. The protonation states of residues in the sodium proton exchanger NhaA from Escherichia coli were investigated. PMID: 16477015
15. under extreme stress conditions (0.1 m LiCl or 0.7 m NaCl at pH 8.5), the dimeric native NhaA was much more efficient than the monomeric mutant in conferring extreme stress resistance. PMID: 17635927
16. combinatorial approach based on molecular dynamics simulations led to formulation of a model of NhaA transport mechanism, pH regulation & cation selectivity consistent with experimental data PMID: 17690293
17. Model structure of the Na+/H+ exchanger 1 in human and E. coli PMID: 17981808
18. Na+/H+ antiporter genes may contribute to sodium-lithium countertransport activity and salt homeostasis in humans PMID: 18000046
19. A novel structural fold creates a delicately balanced electrostatic environment in the middle of the membrane, which might be essential for ion binding and translocation. Review. PMID: 18707888
20. NhaA dimers are crucial for the stability of the antiporter under extreme stress conditions. PMID: 19129192
21. N-terminus verified by Edman degradation on complete protein PMID: 8381959

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KEGG: ecj:JW0018

STRING: 316385.ECDH10B_0020