ReviewAnnual review of biophysics2015
Structural Symmetry in Membrane Proteins.
Review in Annual review of biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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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.
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Who cites it
87 citing papers in PubMed.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- Structures of the sodium-coupled phosphate importer SLC34A2 reveal a distinct architecture and gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Functional role of a structural water in the elevator domain of dicarboxylate transporter VcINDY.PNAS nexus · 2026Article
- Structural basis for pH-responsive amino acid transport via SLC7A4.Nature communications · 2026Article
- Precise Regulation of Membrane Proteins: From Physical Technology to Biomolecular Strategy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Structural basis of drug recognition by human MATE1 transporter.Nature communications · 2025Article
- Potential Transmembrane Proteins-transporters of Chelidonic Acid for its Intracellular Uptake: In Silico Simulation.Pharmaceutical research · 2025Article
- Quantification of Membrane Protein Conformational Free Energy from Mutations and a Single Atom.Journal of the American Chemical Society · 2025Article
- TmDet 4.0: determining membrane orientation of transmembrane proteins from 3D structure.Nucleic acids research · 2025Article
- PIPNature communications · 2025Article
- Rapid and accurate prediction of protein homo-oligomer symmetry using Seq2Symm.Nature communications · 2025Article
- The Arabidopsis AtSWEET13 transporter discriminates sugars by selective facial and positional substrate recognition.Communications biology · 2024Article
- Peripheral positions encode transport specificity in the small multidrug resistance exporters.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Oligomerization of drug transporters: Forms, functions, and mechanisms.Acta pharmaceutica Sinica. B · 2024Review
- Rapid and accurate prediction of protein homo-oligomer symmetry with Seq2Symm.Research square · 2024Article
- Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- EncoMPASS: An encyclopedia of membrane proteins analyzed by structure and symmetry.Structure (London, England : 1993) · 2024Article
- Review
- Buffering of genetic dominance by allele-specific protein complex assembly.Science advances · 2023Article
27 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Symmetry is a common feature among natural systems, including protein structures. A strong propensity toward symmetric architectures has long been recognized for water-soluble proteins, and this propensity has been rationalized from an evolutionary standpoint. Proteins residing in cellular membranes, however, have traditionally been less amenable to structural studies, and thus the prevalence and significance of symmetry in this important class of molecules is not as well understood. In the past two decades, researchers have made great strides in this area, and these advances have provided exciting insights into the range of architectures adopted by membrane proteins. These structural studies have revealed a similarly strong bias toward symmetric arrangements, which were often unexpected and which occurred despite the restrictions imposed by the membrane environment on the possible symmetry groups. Moreover, membrane proteins disproportionately contain internal structural repeats resulting from duplication and fusion of smaller segments. This article discusses the types and origins of symmetry in membrane proteins and the implications of symmetry for protein function.
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