ArticlePLoS computational biology2013
Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins.
Article in PLoS computational biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- AraR Transcription Factor Affects the Sugar Metabolism and Acid Tolerance ofFoods (Basel, Switzerland) · 2025Article
- Specificity determinants revealed by the structure of glycosyltransferase Campylobacter concisus PglA.Protein science : a publication of the Protein Society · 2024Article
- Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Monotopic Membrane Proteins Join the Fold.Trends in biochemical sciences · 2019Review
- Metazoans evolved by taking domains from soluble proteins to expand intercellular communication network.Scientific reports · 2015Article
- Membrane protein stability can be compromised by detergent interactions with the extramembranous soluble domains.Protein science : a publication of the Protein Society · 2014Article
- Kinetics and thermodynamics of membrane protein folding.Biomolecules · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Of the membrane proteins of known structure, we found that a remarkable 67% of the water soluble domains are structurally similar to water soluble proteins of known structure. Moreover, 41% of known water soluble protein structures share a domain with an already known membrane protein structure. We also found that functional residues are frequently conserved between extramembrane domains of membrane and soluble proteins that share structural similarity. These results suggest membrane and soluble proteins readily exchange domains and their attendant functionalities. The exchanges between membrane and soluble proteins are particularly frequent in eukaryotes, indicating that this is an important mechanism for increasing functional complexity. The high level of structural overlap between the two classes of proteins provides an opportunity to employ the extensive information on soluble proteins to illuminate membrane protein structure and function, for which much less is known. To this end, we employed structure guided sequence alignment to elucidate the functions of membrane proteins in the human genome. Our results bridge the gap of fold space between membrane and water soluble proteins and provide a resource for the prediction of membrane protein function. A database of predicted structural and functional relationships for proteins in the human genome is provided at sbi.postech.ac.kr/emdmp.
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Registered trials
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