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Combined computational and biochemical study reveals the importance of electrostatic interactions between the “pH sensor” and the cation binding site of the sodium/proton antiporter NhaA of Escherichia coli
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/jcc.540040211openalex-snapshot
CHARMM : A program for macromolecular energy, minimization, and dynamics calculations
inferredcites →https://doi.org/10.1002/jcc.540120405openalex-snapshot
A rapid finite difference algorithm, utilizing successive over‐relaxation to solve the Poisson–Boltzmann equation
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A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1007/978-1-4615-0427-6_3openalex-snapshot
Two Fundamental Regulatory Factors of the Na+/H+ Exchangers
inferredcites →https://doi.org/10.1007/springerreference_3675openalex-snapshot
Bacterial Stress Response
inferredcites →https://doi.org/10.1016/0005-2728(94)90204-6openalex-snapshot
Molecular physiology of Na+/H+ antiporters, key transporters in circulation of Na+ and H+ in cells
inferredcites →https://doi.org/10.1016/0014-5793(95)00331-3openalex-snapshot
Essential aspartic acid residues, Asp‐133, Asp‐163 and Asp‐164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli
inferredcites →https://doi.org/10.1016/j.bbabio.2004.04.018openalex-snapshot
NhaA of Escherichia coli, as a model of a pH-regulated Na+/H+antiporter
inferredcites →https://doi.org/10.1016/j.bbamem.2005.09.010openalex-snapshot
Alkaline pH homeostasis in bacteria: New insights
inferredcites →https://doi.org/10.1016/j.jmb.2005.03.051openalex-snapshot
Are Acidic and Basic Groups in Buried Proteins Predicted to be Ionized?
inferredcites →https://doi.org/10.1016/j.tibs.2008.06.007openalex-snapshot
The enlightening encounter between structure and function in the NhaA Na+–H+ antiporter
inferredcites →https://doi.org/10.1016/s0005-2728(00)00060-8openalex-snapshot
A pragmatic approach to structure based calculation of coupled proton and electron transfer in proteins
inferredcites →https://doi.org/10.1016/s0006-3495(04)74254-xopenalex-snapshot
Dynamic Water Networks in Cytochrome c Oxidase from Paracoccus denitrificans Investigated by Molecular Dynamics Simulations
inferredcites →https://doi.org/10.1016/s0006-3495(94)80709-xopenalex-snapshot
Calculation of electrostatic effects at the amino terminus of an alpha helix
inferredcites →https://doi.org/10.1016/s0006-3495(95)80406-6openalex-snapshot
Electrostatic calculations of amino acid titration and electron transfer, Q-AQB-->QAQ-B, in the reaction center
inferredcites →https://doi.org/10.1016/s0006-3495(96)79267-6openalex-snapshot
Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: a molecular dynamics free energy perturbation study
inferredcites →https://doi.org/10.1016/s0006-3495(97)78851-9openalex-snapshot
Incorporating protein conformational flexibility into the calculation of pH-dependent protein properties
inferredcites →https://doi.org/10.1016/s0021-9258(18)53333-0openalex-snapshot
Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli.
inferredcites →https://doi.org/10.1016/s0076-6879(86)25028-4openalex-snapshot
[26] Ion extrusion systems in Escherichia coli
inferredcites →https://doi.org/10.1021/bi00597a023openalex-snapshot
Sodium-proton antiport in isolated membrane vesicles of Escherichia coli
inferredcites →https://doi.org/10.1021/bi011655vopenalex-snapshot
Trans Membrane Domain IV Is Involved in Ion Transport Activity and pH Regulation of the NhaA-Na+/H+ Antiporter of Escherichia coli
inferredcites →https://doi.org/10.1021/bi061048dopenalex-snapshot
Structure−Function Relationship of the Fifth Transmembrane Domain in the Na+/H+ Antiporter of Helicobacter pylori: Topology and Function of the Residues, Including Two Consecutive Essential Aspartate Residues
inferredcites →https://doi.org/10.1021/bi602393sopenalex-snapshot
Functional and Structural Interactions of the Transmembrane Domain X of NhaA, Na+/H+ Antiporter of Escherichia coli, at Physiological pH
inferredcites →https://doi.org/10.1021/bi982700aopenalex-snapshot
Calculated Protein and Proton Motions Coupled to Electron Transfer: Electron Transfer from QA- to QB in Bacterial Photosynthetic Reaction Centers
inferredcites →https://doi.org/10.1021/ci800263copenalex-snapshot
Open Science Grid Study of the Coupling between Conformation and Water Content in the Interior of a Protein
inferredcites →https://doi.org/10.1021/jm00145a002openalex-snapshot
A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
inferredcites →https://doi.org/10.1038/nature03692openalex-snapshot
Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH
inferredcites →https://doi.org/10.1046/j.1432-1327.2001.02391.xopenalex-snapshot
Functional analysis of polar amino‐acid residues in membrane associated regions of the NHE1 isoform of the mammalian Na+/H+ exchanger
inferredcites →https://doi.org/10.1073/pnas.0510914103openalex-snapshot
Multiconformation continuum electrostatics analysis of the NhaA Na + /H + antiporter of Escherichia coli with functional implications
inferredcites →https://doi.org/10.1073/pnas.0707120104openalex-snapshot
A human Na + /H + antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension
inferredcites →https://doi.org/10.1073/pnas.84.9.2615openalex-snapshot
Characterization of a Na+/H+ antiporter gene of Escherichia coli.
inferredcites →https://doi.org/10.1074/jbc.272.3.1761openalex-snapshot
Histidine 225, a Residue of the NhaA-Na+/H+ Antiporter of Escherichia coli Is Exposed and Faces the Cell Exterior
inferredcites →https://doi.org/10.1074/jbc.274.35.24617openalex-snapshot
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
inferredcites →https://doi.org/10.1074/jbc.275.7.4734openalex-snapshot
The Monoclonal Antibody 1F6 Identifies a pH-dependent Conformational Change in the Hydrophilic NH2 Terminus of NhaA Na+/H+ Antiporter ofEscherichia coli
inferredcites →https://doi.org/10.1074/jbc.m301932200openalex-snapshot
Identification of Membrane Domains of the Na+/H+ Antiporter (NhaA) Protein from Helicobacter pylori Required for Ion Transport and pH Sensing
inferredcites →https://doi.org/10.1074/jbc.m309021200openalex-snapshot
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
inferredcites →https://doi.org/10.1074/jbc.m400288200openalex-snapshot
Unraveling Functional and Structural Interactions between Transmembrane Domains IV and XI of NhaA Na+/H+ Antiporter of Escherichia coli
inferredcites →https://doi.org/10.1074/jbc.m409608200openalex-snapshot
Structural and Functional Characterization of Transmembrane Segment IV of the NHE1 Isoform of the Na+/H+ Exchanger
inferredcites →https://doi.org/10.1074/jbc.m705460200openalex-snapshot
Model Structure of the Na+/H+ Exchanger 1 (NHE1)
inferredcites →https://doi.org/10.1074/jbc.m800482200openalex-snapshot
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
inferredcites →https://doi.org/10.1074/jbc.m803447200openalex-snapshot
Structural and Functional Characterization of Transmembrane Segment IX of the NHE1 Isoform of the Na+/H+ Exchanger
inferredcites →https://doi.org/10.1126/science.1142824openalex-snapshot
Mechanism of Na + /H + Antiporting
inferredcites →https://doi.org/10.1139/y06-081openalex-snapshot
Functional characterization of the transmembrane segment VII of the NHE1 isoform of the Na+/H+ exchangerThis paper is one of a selection of papers published in this Special Issue, entitled The Cellular and Molecular Basis of Cardiovascular Dysfunction, Dhalla 70th Birthday Tribute.
inferredcites →https://doi.org/10.1146/annurev.pharmtox.42.092001.143801openalex-snapshot
The Changing Face of the Na+/H+ Exchanger, NHE1: Structure, Regulation, and Cellular Actions
inferredcites →https://doi.org/10.1152/ajpcell.00360.2004openalex-snapshot
Evolutionary origins of eukaryotic sodium/proton exchangers
inferredcites →https://doi.org/10.1529/biophysj.106.098269openalex-snapshot
The Influence of Protonation States on the Dynamics of the NhaA Antiporter from Escherichia coli
inferredcites →https://doi.org/10.1529/biophysj.107.104182openalex-snapshot
Role of Flexibility and Polarity as Determinants of the Hydration of Internal Cavities and Pockets in Proteins
inferredcites →https://doi.org/10.2144/97234bm01openalex-snapshot
Modification of a PCR-Based Site-Directed Mutagenesis Method
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4706745openalex-extracted
A Novel Ph-Sensitive Hemi-Cyanine Containing Tetrahydropyridine Ring Near-Infrared Fluorescence Probe with Lysosome-Targeting Ability
inferred← citeshttps://doi.org/10.1002/j.2040-4603.2011.tb00383.xopenalex-snapshot
Regulation of Nha A by Protons
inferred← citeshttps://doi.org/10.1007/s00894-010-0883-5openalex-snapshot
Computational study of the Na+/H+ antiporter from Vibrio parahaemolyticus
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.12.007openalex-snapshot
Functional and structural dynamics of NhaA, a prototype for Na+ and H+ antiporters, which are responsible for Na+ and H+ homeostasis in cells
inferred← citeshttps://doi.org/10.1016/j.biochi.2020.10.017openalex-snapshot
Site-directed mutations reflecting functional and structural properties of Ec-NhaA
inferred← citeshttps://doi.org/10.1016/j.jmb.2009.12.055openalex-snapshot
Model-Guided Mutagenesis Drives Functional Studies of Human NHA2, Implicated in Hypertension
inferred← citeshttps://doi.org/10.1016/j.saa.2024.124162openalex-snapshot
A novel pH-sensitive hemi-cyanine containing tetrahydropyridine ring near-infrared fluorescence probe with lysosome-targeting ability
inferred← citeshttps://doi.org/10.1038/ncomms12940openalex-snapshot
Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA
inferred← citeshttps://doi.org/10.1038/nrm2820openalex-snapshot
Sensors and regulators of intracellular pH
inferred← citeshttps://doi.org/10.1038/s41467-018-06770-5openalex-snapshot
Broad phylogenetic analysis of cation/proton antiporters reveals transport determinants
inferred← citeshttps://doi.org/10.1038/s41467-022-34120-zopenalex-snapshot
Crystal structure of the Na+/H+ antiporter NhaA at active pH reveals the mechanistic basis for pH sensing
inferred← citeshttps://doi.org/10.1038/s41598-019-51887-2openalex-snapshot
Mutation of two key aspartate residues alters stoichiometry of the NhaB Na+/H+ exchanger from Klebsiella pneumoniae
inferred← citeshttps://doi.org/10.1038/s41598-021-86318-8openalex-snapshot
Insight into the direct interaction of Na+ with NhaA and mechanistic implications
inferred← citeshttps://doi.org/10.1038/srep23339openalex-snapshot
The Ec-NhaA antiporter switches from antagonistic to synergistic antiport upon a single point mutation
inferred← citeshttps://doi.org/10.1073/pnas.1109256108openalex-snapshot
Site-directed tryptophan fluorescence reveals two essential conformational changes in the Na + /H + antiporter NhaA
inferred← citeshttps://doi.org/10.1073/pnas.1703422114openalex-snapshot
Ligand-induced conformational dynamics of the Escherichia coli Na + /H + antiporter NhaA revealed by hydrogen/deuterium exchange mass spectrometry
inferred← citeshttps://doi.org/10.1074/jbc.ra118.004903openalex-snapshot
Replacement of Lys-300 with a glutamine in the NhaA Na+/H+ antiporter of Escherichia coli yields a functional electrogenic transporter
inferred← citeshttps://doi.org/10.1085/jgp.201411219openalex-snapshot
Crystal structure of the sodium–proton antiporter NhaA dimer and new mechanistic insights
inferred← citeshttps://doi.org/10.1096/fj.202201280ropenalex-snapshot
Structural basis for the arsenite binding and translocation of Acr3 antiporter with NhaA folding pattern
inferred← citeshttps://doi.org/10.1242/jeb.026708openalex-snapshot
NhaA crystal structure: functional–structural insights
inferred← citeshttps://doi.org/10.1371/journal.pone.0026115openalex-snapshot
Characterization of the Na+/H+ Antiporter from Yersinia pestis
inferred← citeshttps://doi.org/10.3109/09687688.2012.693209openalex-snapshot
Conformational changes in NhaA Na+/H+antiporter
inferred← citeshttps://doi.org/10.3390/ijms23169156openalex-snapshot
Prokaryotic Na+/H+ Exchangers—Transport Mechanism and Essential Residues
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