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The structure and function of cell membranes studied by atomic force microscopy
85/85 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 85 checked references that resolve
resolves10.1021/bi2018909
Role of Mitochondrial Ca<sup>2+</sup> in the Regulation of Cellular Energetics
resolves10.1073/pnas.1332550100
Dynamic, yet structured: The cell membrane three decades after the Singer–Nicolson model
resolves10.1016/0304-4157(76)90014-9
Transmembrane control of the receptors on normal and tumor cells
resolves10.1126/science.274.5285.209
An αβ T Cell Receptor Structure at 2.5 Å and Its Orientation in the TCR-MHC Complex
resolves10.1016/S0092-8674(02)00963-7
Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains
resolves10.1016/j.jmb.2004.02.058
Crystal Structure of Human Carboxypeptidase M, A Membrane-bound Enzyme that Regulates Peptide Hormone Activity
resolves10.1194/jlr.E600002-JLR200
Rafts defined: a report on the Keystone symposium on lipid rafts and cell function
resolves10.1111/j.1582-4934.2008.00281.x
Membranes: a meeting point for lipids, proteins and therapies
resolves10.1016/j.bbamem.2013.10.019
The Fluid—Mosaic Model of Membrane Structure: Still relevant to understanding the structure, function and dynamics of biological membranes after more than 40years
resolves10.1016/j.plipres.2010.05.001
An outlook on organization of lipids in membranes: Searching for a realistic connection with the organization of biological membranes
resolves10.1016/j.bbamem.2013.04.011
Atomic force microscopy: A multifaceted tool to study membrane proteins and their interactions with ligands
resolves10.1126/science.2928794
Imaging Crystals, Polymers, and Processes in Water with the Atomic Force Microscope
resolves10.1016/S0006-3495(99)77275-9
Electrostatically Balanced Subnanometer Imaging of Biological Specimens by Atomic Force Microscope
resolves10.1016/S0022-5320(58)80008-8
The ultrastructure of the intercalated discs of frog, mouse and guinea pig cardiac muscle
resolves10.1016/j.ultramic.2005.12.020
A combined optical and atomic force microscope for live cell investigations
resolves10.1038/nmeth929
Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
resolves10.1016/j.bpj.2013.12.037
Local Viscoelastic Properties of Live Cells Investigated Using Dynamic and Quasi-Static Atomic Force Microscopy Methods
resolves10.1016/j.chemphyslip.2012.10.005
Atomic force microscopy: A versatile tool to probe the physical and chemical properties of supported membranes at the nanoscale
resolves10.1016/j.surfrep.2005.08.003
Force measurements with the atomic force microscope: Technique, interpretation and applications
resolves10.1155/2004/482680
Single‐Cell Elastography: Probing for Disease with the Atomic Force Microscope
resolves10.1038/nnano.2008.410
Early detection of aging cartilage and osteoarthritis in mice and patient samples using atomic force microscopy
resolves10.1016/j.ymeth.2006.08.016
Using atomic force microscopy to study chromatin structure and nucleosome remodeling
resolves10.1002/jemt.20156
Imaging DNA molecules on mica surface by atomic force microscopy in air and in liquid
resolves10.1016/j.ultramic.2009.12.014
Preparation of cell membranes for high resolution imaging by AFM
resolves10.1016/j.jsb.2009.02.003
Detection of metal binding sites on functional S-layer nanoarrays using single molecule force spectroscopy
resolves10.1016/S0006-3495(91)82222-6
Structure of an adsorbed dimyristoylphosphatidylcholine bilayer measured with specular reflection of neutrons
resolves10.1038/nature04321
Lipid–protein interactions in double-layered two-dimensional AQP0 crystals
resolves10.1111/j.1476-5381.2012.01917.x
The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatases
resolves10.1371/journal.pone.0091595
Studying the Nucleated Mammalian Cell Membrane by Single Molecule Approaches
resolves10.1111/j.1600-0854.2004.0170.x
Transmembrane Asymmetry and Lateral Domains in Biological Membranes
resolves10.1006/jmbi.1998.2359
Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy 1 1Edited by W. Baumeister
resolves10.1016/j.jmb.2009.12.034
pH-Induced Conformational Change of the β-Barrel-Forming Protein OmpG Reconstituted into Native E. coli Lipids
resolves10.1093/emboj/cdf365
Conformational changes in surface structures of isolated connexin 26 gap junctions
resolves10.1074/jbc.M609317200
Aminosulfonate Modulated pH-induced Conformational Changes in Connexin26 Hemichannels
resolves10.1073/pnas.1111149108
Gating of the MlotiK1 potassium channel involves large rearrangements of the cyclic nucleotide-binding domains
resolves10.1038/nnano.2010.7
High-speed atomic force microscopy shows dynamic molecular processes in photoactivated bacteriorhodopsin
resolves10.1038/nnano.2012.109
Characterization of the motion of membrane proteins using high-speed atomic force microscopy
resolves10.1016/j.jmb.2017.03.004
Real-time Visualization of Phospholipid Degradation by Outer Membrane Phospholipase A using High-Speed Atomic Force Microscopy
resolves10.1126/science.276.5315.1109
Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM
resolves10.1146/annurev.biophys.36.040306.132640
Deciphering Molecular Interactions of Native Membrane Proteins by Single-Molecule Force Spectroscopy
resolves10.1242/jcs.03035
Ligands on the string: single-molecule AFM studies on the interaction of antibodies and substrates with the Na+-glucose co-transporter SGLT1 in living cells
resolves10.1021/jp0758667
Single-Molecule Force Spectroscopy Study of Interaction between Transforming Growth Factor β1 and Its Receptor in Living Cells
resolves10.1021/nn1009648
Atomic Force Microscopy-Based Molecular Recognition of a Fibrinogen Receptor on Human Erythrocytes
resolves10.1016/j.bpj.2017.01.033
Unraveling the Receptor-Ligand Interactions between Bladder Cancer Cells and the Endothelium Using AFM
resolves10.1021/nl0700853
Single-Molecule Force Spectroscopy and Imaging of the Vancomycin/<scp>d</scp>-Ala-<scp>d</scp>-Ala Interaction
resolves10.1007/s11434-014-0290-x
Progress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy
resolves10.1021/nn800341b
Detection, Localization, and Conformational Analysis of Single Polysaccharide Molecules on Live Bacteria
resolves10.1039/c3nr00553d
A single-molecule force spectroscopy study of the interactions between lectins and carbohydrates on cancer and normal cells
resolves10.1126/science.aah7124
Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins
resolves10.1016/j.jmb.2005.10.028
Observing Folding Pathways and Kinetics of a Single Sodium-proton Antiporter from Escherichia coli
resolves10.1016/j.jmb.2004.05.026
Controlled Unfolding and Refolding of a Single Sodium-proton Antiporter using Atomic Force Microscopy
resolves10.1021/nl902803m
Localization of Na<sup>+</sup>−K<sup>+</sup> ATPases in Quasi-Native Cell Membranes
resolves10.1063/1.3262966
Atomic force microscopic study of folate receptors in live cells with functionalized tips
resolves10.1088/0957-4484/21/11/115504
Improved localization of cellular membrane receptors using combined fluorescence microscopy and simultaneous topography and recognition imaging
resolves10.1007/s00216-017-0238-5
Characterization of the specific interaction between the DNA aptamer sgc8c and protein tyrosine kinase-7 receptors at the surface of T-cells by biosensing AFM
The 3 references without a DOI — listed, not checked
no DOI — not checkedThe ultrastructure of cell membranes and their derivatives
no DOI — not checkedIs a fluid-mosaic model of biological membranes fully relevant? Studies on lipid organization in model and biological membranes
no DOI — not checkedO-type sialoglycoproteins in erythrocyte membranes of lower vertebrates: identification and study using lectins
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