scholarly article | Q13442814 |
P356 | DOI | 10.1016/J.JMB.2006.07.019 |
P698 | PubMed publication ID | 16919297 |
P50 | author | Hartmut Michel | Q77086 |
Carola Hunte | Q42406419 | ||
P2093 | author name string | Etana Padan | |
Abraham Rimon | |||
Emanuela Screpanti | |||
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Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exterior | Q71985034 | ||
Inhibition of Na(+)-H(+) exchange prevents hypertrophy, fibrosis, and heart failure in beta(1)-adrenergic receptor transgenic mice | Q77975263 | ||
A pH-dependent conformational change of NhaA Na(+)/H(+) antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltoside | Q78151377 | ||
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Three-dimensional structure of the ion-coupled transport protein NhaA. | Q33886837 | ||
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Proton/sodium ion antiport in Escherichia coli | Q42147886 | ||
Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequences. | Q43547737 | ||
Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli | Q43847621 | ||
Mutation E252C Increases Drastically the K Value for Na+ and Causes an Alkaline Shift of the pH Dependence of NhaA Na+/H+ Antiporter of Escherichia coli | Q44646965 | ||
Functional analysis of amino acids of the Na+/H+ exchanger that are important for proton translocation | Q44692637 | ||
Unraveling functional and structural interactions between transmembrane domains IV and XI of NhaA Na+/H+ antiporter of Escherichia coli | Q44811170 | ||
P433 | issue | 2 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 192-202 | |
P577 | publication date | 2006-07-15 | |
P1433 | published in | Journal of Molecular Biology | Q925779 |
P1476 | title | Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformation | |
P478 | volume | 362 |
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Q50467116 | Monomers of the NhaA Na+/H+ antiporter of Escherichia coli are fully functional yet dimers are beneficial under extreme stress conditions at alkaline pH in the presence of Na+ or Li+. |
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Q40447278 | Structure-based functional study reveals multiple roles of transmembrane segment IX and loop VIII-IX in NhaA Na+/H+ antiporter of Escherichia coli at physiological pH |
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