| scholarly article | Q13442814 |
| P50 | author | Daniel Hilger | Q61820576 |
| Heinz-Jürgen Steinhoff | Q64084811 | ||
| P2093 | author name string | Gunnar Jeschke | |
| Klaus-Peter Vogel | |||
| Etana Padan | |||
| Heinrich Jung | |||
| Christoph Wegener | |||
| P2860 | cites work | Molecular Characterization of Helix-Loop-Helix Peptides | Q67486610 |
| Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli | Q68238305 | ||
| Histidine 225, a residue of the NhaA-Na+/H+ antiporter of Escherichia coli is exposed and faces the cell exterior | Q71985034 | ||
| Topology of the Na+/proline transporter of Escherichia coli | Q77359726 | ||
| A point mutation (G338S) and its suppressor mutations affect both the pH response of the NhaA-Na+/H+ antiporter as well as the growth phenotype of Escherichia coli | Q77359753 | ||
| 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 | ||
| Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli | Q28609363 | ||
| Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme. | Q30330285 | ||
| Transmembrane protein structure: spin labeling of bacteriorhodopsin mutants | Q30403092 | ||
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| Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure. | Q32163219 | ||
| Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 A resolution | Q33866894 | ||
| Three-dimensional structure of the ion-coupled transport protein NhaA. | Q33886837 | ||
| Na(+)/H(+) antiporters. | Q33937928 | ||
| Identifying conformational changes with site-directed spin labeling | Q34019511 | ||
| Histidine-226 is part of the pH sensor of NhaA, a Na+/H+ antiporter in Escherichia coli. | Q34355324 | ||
| Quaternary structure and function of transport proteins | Q34699373 | ||
| Distance measurements in the nanometer range by pulse EPR. | Q35034788 | ||
| NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporter | Q35849739 | ||
| Sensitivity enhancement in pulse EPR distance measurements. | Q39686750 | ||
| Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin | Q40184717 | ||
| Interresidual distance determination by four-pulse double electron-electron resonance in an integral membrane protein: the Na+/proline transporter PutP of Escherichia coli | Q40278902 | ||
| Molecular analysis of the role of Na+/H+ antiporters in bacterial cell physiology. | Q40853638 | ||
| Oligomerization of NhaA, the Na+/H+ antiporter of Escherichia coli in the membrane and its functional and structural consequences. | Q43547737 | ||
| Molecular model of the Escherichia coli Na1/H1 antiporter NhaA. | Q43791228 | ||
| Trans membrane domain IV is involved in ion transport activity and pH regulation of the NhaA-Na(+)/H(+) antiporter of Escherichia coli | Q43847621 | ||
| Methods for study of protein dynamics and protein-protein interaction in protein-ubiquitination by electron paramagnetic resonance spectroscopy | Q44088815 | ||
| Proximity of cytoplasmic and periplasmic loops in NhaA Na+/H+ antiporter of Escherichia coli as determined by site-directed thiol cross-linking | Q44244214 | ||
| Unraveling functional and structural interactions between transmembrane domains IV and XI of NhaA Na+/H+ antiporter of Escherichia coli | Q44811170 | ||
| Localization of the N-terminal domain in light-harvesting chlorophyll a/b protein by EPR measurements | Q45310575 | ||
| Topological analysis of NhaA, a Na+/H+ antiporter from Escherichia coli. | Q54575384 | ||
| EPR Probes with Well-Defined, Long Distances between Two or Three Unpaired Electrons | Q58878329 | ||
| Dead-Time Free Measurement of Dipole–Dipole Interactions between Electron Spins | Q58878339 | ||
| P433 | issue | 2 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | Escherichia coli | Q25419 |
| membrane protein | Q423042 | ||
| P304 | page(s) | 1328-1338 | |
| P577 | publication date | 2005-05-13 | |
| P1433 | published in | Biophysical Journal | Q2032955 |
| P1476 | title | Assessing oligomerization of membrane proteins by four-pulse DEER: pH-dependent dimerization of NhaA Na+/H+ antiporter of E. coli | |
| P478 | volume | 89 |
| Q38424508 | A comparative study of structures and structural transitions of secondary transporters with the LeuT fold |
| Q30413946 | Allosteric control of syntaxin 1a by Munc18-1: characterization of the open and closed conformations of syntaxin |
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| Q43094603 | Backbone structure of transmembrane domain IX of the Na+/proline transporter PutP of Escherichia coli. |
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| Q91497036 | Cardiolipin is an Optimal Phospholipid for the Assembly, Stability, and Proper Functionality of the Dimeric Form of NhaA Na+/H+ Antiporter |
| Q90031505 | Characterization of the Human KCNQ1 Voltage Sensing Domain (VSD) in Lipodisq Nanoparticles for Electron Paramagnetic Resonance (EPR) Spectroscopic Studies of Membrane Proteins |
| Q56378891 | Choice of reconstitution protocol modulates the aggregation state of full-length membrane-reconstituted synaptotagmin-1 |
| Q46789671 | Computational study of the Na+/H + antiporter from Vibrio parahaemolyticus |
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| Q54334524 | Conformational changes in NhaA Na+/H+ antiporter. |
| Q34558712 | Crucial steps in the structure determination of the Na+/H+ antiporter NhaA in its native conformation |
| Q30268449 | Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights |
| Q42067529 | Differential effects of mutations on the transport properties of the Na+/H+ antiporter NhaA from Escherichia coli |
| Q52315526 | Disruption of the E. coli LptC dimerization interface and characterization of lipopolysaccharide and LptA binding to monomeric LptC. |
| Q41140577 | EPR and NMR spectroscopies provide input on the coordination of Cu(I) and Ag(I) to a disordered methionine segment |
| Q27682210 | High Resolution Structure and Double Electron-Electron Resonance of the Zebrafish Voltage-dependent Anion Channel 2 Reveal an Oligomeric Population |
| Q35037255 | High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase |
| Q39939476 | High-resolution structure of a Na+/H+ antiporter dimer obtained by pulsed electron paramagnetic resonance distance measurements |
| Q50449385 | Intermolecular cross-linking of monomers in Helicobacter pylori Na+/H+ antiporter NhaA at the dimer interface inhibits antiporter activity. |
| Q36848309 | Long-range distance determinations in biomacromolecules by EPR spectroscopy |
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| Q30413811 | Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex. |
| 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+. |
| Q30380407 | Navigating Membrane Protein Structure, Dynamics, and Energy Landscapes Using Spin Labeling and EPR Spectroscopy. |
| Q37226855 | Peptide-Membrane Interactions by Spin-Labeling EPR |
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| Q92995166 | Probing the solution structure of the E. coli multidrug transporter MdfA using DEER distance measurements with nitroxide and Gd(III) spin labels |
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| Q41156794 | Refined distances between paramagnetic centers of a multi-copper nitrite reductase determined by pulsed EPR (iDEER) spectroscopy |
| Q38111722 | Regulation of NhaA by protons |
| Q36785003 | Secondary transport of amino acids in prokaryotes. |
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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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| Q52671619 | Studying structure and function of membrane proteins with PELDOR/DEER spectroscopy - A crystallographers' perspective. |
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