ReviewBiochimica et biophysica acta2014
Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 116 citations in OpenAlex.
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Physical Changes of Biomacromolecules upon Covalent Surface Immobilization.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Planar Lipid Bilayers and Liposomes: Essential Models for Advancing Protein Structure and Function Research.Advances in experimental medicine and biology · 2026Review
- Improved albumin binding properties of Isoguvacine upon esterification as characterized by biophysical and computational tools.Scientific reports · 2025Article
- TNF-α exacerbates calcium influx via voltage-gated calcium channels in breast cancer cells: a nanoscale multimodal AFM study.Frontiers in cell and developmental biology · 2025Article
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- Changes in cell surface properties ofFEMS microbes · 2023Article
- Structural studies of protein-nucleic acid complexes: A brief overview of the selected techniques.Computational and structural biotechnology journal · 2023Review
- Article
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- Protein-mediated interactions in the dynamic regulation of acute inflammation.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2023Article
- Tools shaping drug discovery and development.Biophysics reviews · 2022Review
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- Quantifying molecular- to cellular-level forces in living cells.Journal of physics D: Applied physics · 2021Article
- Loss of PRCD alters number and packaging density of rhodopsin in rod photoreceptor disc membranes.Scientific reports · 2020Article
- Switching behaviour in vascular smooth muscle cell-matrix adhesion during oscillatory loading.Journal of theoretical biology · 2020Article
- Photocatalytic Nanofabrication and Intracellular Raman Imaging of Living Cells with Functionalized AFM Probes.Micromachines · 2020Article
- Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019Review
- Differentiating between Inactive and Active States of Rhodopsin by Atomic Force Microscopy in Native Membranes.Analytical chemistry · 2019Article
- Transient Receptor Potential Channels and Calcium Signaling.Cold Spring Harbor perspectives in biology · 2019Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Membrane proteins are embedded in lipid bilayers and facilitate the communication between the external environment and the interior of the cell. This communication is often mediated by the binding of ligands to the membrane protein. Understanding the nature of the interaction between a ligand and a membrane protein is required to both understand the mechanism of action of these proteins and for the development of novel pharmacological drugs. The highly hydrophobic nature of membrane proteins and the requirement of a lipid bilayer for native function have hampered the structural and molecular characterizations of these proteins under physiologically relevant conditions. Atomic force microscopy offers a solution to studying membrane proteins and their interactions with ligands under physiologically relevant conditions and can provide novel insights about the nature of these critical molecular interactions that facilitate cellular communication. In this review, we provide an overview of the atomic force microscopy technique and discuss its application in the study of a variety of questions related to the interaction between a membrane protein and a ligand. This article is part of a Special Issue entitled: Structural and biophysical characterization of membrane protein-ligand binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.