ReviewCellular and molecular life sciences : CMLS2012
Emergence of symmetric protein architecture from a simple peptide motif: evolutionary models.
Review in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed.
- Detection of protein symmetry and structural rearrangements using secondary structure elements.Protein science : a publication of the Protein Society · 2026Article
- Why we are made of proteins and nucleic acids: Structural biology views on extraterrestrial life.Biophysics and physicobiology · 2023Article
- Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022Article
- Evolution of a σ-(c-di-GMP)-anti-σ switch.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Ab initio folding of a trefoil-fold motif reveals structural similarity with a β-propeller blade motif.Protein science : a publication of the Protein Society · 2020Article
- Protodomains: Symmetry-Related Supersecondary Structures in Proteins and Self-Complementarity.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Insights into the molecular mechanism of dehalogenation catalyzed by D-2-haloacid dehalogenase from crystal structures.Scientific reports · 2018Article
- Designs on a curve.Nature structural & molecular biology · 2015Article
- Article
- Computational design of a self-assembling symmetrical β-propeller protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Systematic detection of internal symmetry in proteins using CE-Symm.Journal of molecular biology · 2014Article
- Inverted topologies in membrane proteins: a mini-review.Computational and structural biotechnology journal · 2013Review
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Authors and funding
3 authors.
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Abstract
Structural symmetry is observed in the majority of fundamental protein folds and gene duplication and fusion evolutionary processes are postulated to be responsible. However, convergent evolution leading to structural symmetry has also been proposed; additionally, there is debate regarding the extent to which exact primary structure symmetry is compatible with efficient protein folding. Issues of symmetry in protein evolution directly impact strategies for de novo protein design as symmetry can substantially simplify the design process. Additionally, when considering gene duplication and fusion in protein evolution, there are two competing models: "emergent architecture" and "conserved architecture". Recent experimental work has shed light on both the evolutionary process leading to symmetric protein folds as well as the ability of symmetric primary structure to efficiently fold. Such studies largely support a "conserved architecture" evolutionary model, suggesting that complex protein architecture was an early evolutionary achievement involving oligomerization of smaller polypeptides.
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