| review article | Q7318358 |
| scholarly article | Q13442814 |
| P50 | author | Daniel Jobst Muller | Q54877794 |
| P2093 | author name string | Alexej Kedrov | |
| P2860 | cites work | Force spectroscopy of single biomolecules | Q78721170 |
| Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin | Q81376882 | ||
| Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy | Q81578473 | ||
| Atomic force microscope | Q21563713 | ||
| Principles that govern the folding of protein chains | Q28236872 | ||
| Entropic elasticity of lambda-phage DNA | Q28247727 | ||
| pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme | Q28284778 | ||
| From Levinthal to pathways to funnels | Q28300934 | ||
| Bacterial Na(+)-ATP synthase has an undecameric rotor | Q28361302 | ||
| Fluorescence correlation spectroscopy for the detection and study of single molecules in biology | Q29400560 | ||
| Dominant forces in protein folding | Q29616390 | ||
| Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters | Q29616590 | ||
| Membrane protein folding on the example of outer membrane protein A of Escherichia coli. | Q30164479 | ||
| Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. | Q30351849 | ||
| Biological atomic force microscopy: from microns to nanometers and beyond | Q30468641 | ||
| Molecular force modulation spectroscopy revealing the dynamic response of single bacteriorhodopsins. | Q30502990 | ||
| Observing structure, function and assembly of single proteins by AFM. | Q30847493 | ||
| Observing single biomolecules at work with the atomic force microscope. | Q30913966 | ||
| Stretching single molecules into novel conformations using the atomic force microscope. | Q30913983 | ||
| Fingerprinting polysaccharides with single-molecule atomic force microscopy | Q30982702 | ||
| Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment | Q31019167 | ||
| Mechanical unfolding intermediates in titin modules. | Q31431985 | ||
| Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane | Q31918014 | ||
| Electrostatically balanced subnanometer imaging of biological specimens by atomic force microscope | Q31920509 | ||
| Atomic force bio-analytics | Q33194255 | ||
| Functional and cellular regulation of the myocardial Na+/H+ exchanger | Q33730443 | ||
| Mechanical and chemical unfolding of a single protein: a comparison | Q33856547 | ||
| Three-dimensional structure of the ion-coupled transport protein NhaA. | Q33886837 | ||
| Unfolding pathways of individual bacteriorhodopsins. | Q33897204 | ||
| Na(+)/H(+) antiporters. | Q33937928 | ||
| Helical membrane protein folding, stability, and evolution | Q34019415 | ||
| Covalent binding of biological samples to solid supports for scanning probe microscopy in buffer solution | Q34020182 | ||
| Misfolding of membrane proteins in health and disease: the lady or the tiger? | Q34029178 | ||
| Unravelling the folding of bacteriorhodopsin | Q34030925 | ||
| Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length | Q34043693 | ||
| Conformational changes in surface structures of isolated connexin 26 gap junctions. | Q34089658 | ||
| Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. | Q34092060 | ||
| Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. | Q34129304 | ||
| Tapping-mode atomic force microscopy produces faithful high-resolution images of protein surfaces | Q34171183 | ||
| Probing protein-DNA interactions by unzipping a single DNA double helix | Q34178541 | ||
| Probing the kinetics of single molecule protein folding | Q34187969 | ||
| Structure of a Na+/H+ antiporter and insights into mechanism of action and regulation by pH. | Q34430086 | ||
| High-resolution AFM topographs of Rubrivivax gelatinosus light-harvesting complex LH2. | Q34769872 | ||
| Protein misfolding in Alzheimer's and Parkinson's disease: genetics and molecular mechanisms | Q34977039 | ||
| The molecular basis for the chemical denaturation of proteins by urea | Q34982168 | ||
| The present view of the mechanism of protein folding | Q35141764 | ||
| Games played by rogue proteins in prion disorders and Alzheimer's disease | Q35573421 | ||
| Conformational change of the hexagonally packed intermediate layer of Deinococcus radiodurans monitored by atomic force microscopy | Q35607745 | ||
| Atomic force microscopy and drug discovery | Q35687679 | ||
| The machinery of membrane protein assembly | Q35863877 | ||
| Imaging crystals, polymers, and processes in water with the atomic force microscope | Q36418152 | ||
| Atomic force microscopy of an organic monolayer | Q36449005 | ||
| Force-induced conformational change of bacteriorhodopsin | Q36707834 | ||
| Direct measurement of the forces between complementary strands of DNA. | Q36728149 | ||
| Electron and atomic force microscopy of membrane proteins | Q36877993 | ||
| Helices VII and X in the lactose permease of Escherichia coli: proximity and ligand-induced distance changes | Q38293449 | ||
| Unfolding pathways of native bacteriorhodopsin depend on temperature. | Q39927873 | ||
| Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy | Q40220193 | ||
| Origin of mechanical strength of bovine carbonic anhydrase studied by molecular dynamics simulation | Q40308358 | ||
| Complex stability of single proteins explored by forced unfolding experiments. | Q40330726 | ||
| Observing membrane protein diffusion at subnanometer resolution. | Q40597630 | ||
| A protein sequence that can encode native structure by disfavoring alternate conformations | Q40739635 | ||
| Pressure stability of proteins | Q40788704 | ||
| Molten globule and protein folding | Q40944932 | ||
| Intermediate states in protein folding | Q40990251 | ||
| The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis | Q41649513 | ||
| Designing transmembrane alpha-helices that insert spontaneously | Q41729430 | ||
| Folding of a bacterial outer membrane protein during passage through the periplasm | Q41924765 | ||
| Locating ligand binding and activation of a single antiporter | Q43205543 | ||
| Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin | Q43591541 | ||
| Membrane insertion and dissociation processes of a model transmembrane helix | Q44171726 | ||
| 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 | ||
| Hydrophobic helical hairpins: design and packing interactions in membrane environments | Q45143766 | ||
| Solvent denaturation and stabilization of globular proteins | Q46646846 | ||
| Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy | Q47241032 | ||
| Probing the energy landscape of the membrane protein bacteriorhodopsin | Q47640355 | ||
| Sec-independent insertion of thylakoid membrane proteins. Analysis of insertion forces and identification of a loop intermediate involving the signal peptide. | Q47828318 | ||
| Force-clamp spectroscopy monitors the folding trajectory of a single protein | Q47962025 | ||
| Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure. | Q54757919 | ||
| BIOGENESIS OF INNER MEMBRANE PROTEINS IN ESCHERICHIA COLI | Q57381517 | ||
| Adsorption of Biological Molecules to a Solid Support for Scanning Probe Microscopy | Q57825449 | ||
| The Monoclonal Antibody 1F6 Identifies a pH-dependent Conformational Change in the Hydrophilic NH2Terminus of NhaA Na+/H+Antiporter ofEscherichia coli | Q57828249 | ||
| Slow α Helix Formation during Folding of a Membrane Protein† | Q57905247 | ||
| Rhodopsin dimers in native disc membranes | Q59056014 | ||
| Single-Molecule Measurement of Protein Folding Kinetics | Q59332599 | ||
| Protein interactions with urea and guanidinium chloride. A calorimetric study | Q67493188 | ||
| Intracellular pH regulation in ferret ventricular muscle. The role of Na-H exchange and the influence of metabolic substrates | Q67912051 | ||
| Overproduction and purification of a functional Na+/H+ antiporter coded by nhaA (ant) from Escherichia coli | Q68238305 | ||
| Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy | Q72121312 | ||
| Essential aspartic acid residues, Asp-133, Asp-163 and Asp-164, in the transmembrane helices of a Na+/H+ antiporter (NhaA) from Escherichia coli | Q72210118 | ||
| Covalent anchoring of proteins onto gold-directed NHS-terminated self-assembled monolayers in aqueous buffers: SFM images of clathrin cages and triskelia | Q72370699 | ||
| Single protein misfolding events captured by atomic force microscopy | Q73133459 | ||
| Reversible unfolding of individual titin immunoglobulin domains by AFM | Q73334897 | ||
| Determining molecular forces that stabilize human aquaporin-1 | Q73467442 | ||
| A biophysical study of integral membrane protein folding | Q73940353 | ||
| A mechanical unfolding intermediate in an actin-crosslinking protein | Q75247106 | ||
| Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy | Q77901475 | ||
| 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 | ||
| P433 | issue | 6 | |
| P921 | main subject | molecular interaction | Q33059490 |
| P304 | page(s) | 400-412 | |
| P577 | publication date | 2006-03-17 | |
| P1433 | published in | Naunyn-Schmiedeberg's Archives of Pharmacology | Q1468251 |
| P1476 | title | Characterizing folding, structure, molecular interactions and ligand gated activation of single sodium/proton antiporters | |
| P478 | volume | 372 |
| Q82783399 | A multi-faceted world of transporters | cites work | P2860 |
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