ReviewPharmacological reviews2008
Vertebrate membrane proteins: structure, function, and insights from biophysical approaches.
Review in Pharmacological reviews, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 99 citations in OpenAlex.
- Nuclear transmembrane protein 199 promotes immune escapes by up-regulating programmed death ligand 1.iScience · 2024Article
- Characterizing the West Nile Virus's polyprotein from nucleotide sequence to protein structure - Computational tools.Journal of Taibah University Medical Sciences · 2024Article
- Article
- Insights into Membrane Curvature Sensing and Membrane Remodeling by Intrinsically Disordered Proteins and Protein Regions.The Journal of membrane biology · 2022Review
- Mechanism of interactions between tripeptide NCW on cellular membrane using molecular dynamic simulation.Frontiers in nutrition · 2022Article
- A multiscale approach for bridging the gap between potency, efficacy, and safety of small molecules directed at membrane proteins.Scientific reports · 2021Article
- Characterization of Five Transmembrane Proteins: With Focus on the Tweety, Sideroflexin, and YIP1 Domain Families.Frontiers in cell and developmental biology · 2021Article
- Bridging protein structure, dynamics, and function using hydrogen/deuterium-exchange mass spectrometry.Protein science : a publication of the Protein Society · 2020Review
- Site-Specific Peptide Probes Detect Buried Water in a Lipid Membrane.Biophysical journal · 2019Article
- ProLIF - quantitative integrin protein-protein interactions and synergistic membrane effects on proteoliposomes.Journal of cell science · 2018Article
- Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies.Communications biology · 2018Article
- Genome-wide comparative analysis of putative Pth11-related G protein-coupled receptors in fungi belonging to Pezizomycotina.BMC microbiology · 2017Article
- Article
- Topology based identification and comprehensive classification of four-transmembrane helix containing proteins (4TMs) in the human genome.BMC genomics · 2016Article
- Disruption of Rhodopsin Dimerization with Synthetic Peptides Targeting an Interaction Interface.The Journal of biological chemistry · 2015Article
- Nanoscale monitoring of drug actions on cell membrane using atomic force microscopy.Acta pharmacologica Sinica · 2015Review
- Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy.Nature communications · 2015Article
- Crystallization of proteins from crude bovine rod outer segments.Methods in enzymology · 2015Article
- Chemistry of the retinoid (visual) cycle.Chemical reviews · 2014Review
- From atomic structures to neuronal functions of g protein-coupled receptors.Annual review of neuroscience · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Membrane proteins are key targets for pharmacological intervention because they are vital for cellular function. Here, we analyze recent progress made in the understanding of the structure and function of membrane proteins with a focus on rhodopsin and development of atomic force microscopy techniques to study biological membranes. Membrane proteins are compartmentalized to carry out extra- and intracellular processes. Biological membranes are densely populated with membrane proteins that occupy approximately 50% of their volume. In most cases membranes contain lipid rafts, protein patches, or paracrystalline formations that lack the higher-order symmetry that would allow them to be characterized by diffraction methods. Despite many technical difficulties, several crystal structures of membrane proteins that illustrate their internal structural organization have been determined. Moreover, high-resolution atomic force microscopy, near-field scanning optical microscopy, and other lower resolution techniques have been used to investigate these structures. Single-molecule force spectroscopy tracks interactions that stabilize membrane proteins and those that switch their functional state; this spectroscopy can be applied to locate a ligand-binding site. Recent development of this technique also reveals the energy landscape of a membrane protein, defining its folding, reaction pathways, and kinetics. Future development and application of novel approaches during the coming years should provide even greater insights to the understanding of biological membrane organization and function.
Indexed as
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What OpenQuestion holds
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.