ArticleStructure (London, England : 1993)2024
EncoMPASS: An encyclopedia of membrane proteins analyzed by structure and symmetry.
Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- MetaMP Ecosystem for Unified, Auditable, and Benchmark-Ready Data for Reliable Membrane Protein Annotation.Computational and structural biotechnology journal · 2026Article
- Memorization bias impacts modeling of alternative conformational states of solute carrier membrane proteins with methods from deep learning.PLoS computational biology · 2025Article
- Refining pairwise sequence alignments of membrane proteins by the incorporation of anchors.PloS one · 2021Article
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3 authors.
Funding
Abstract
Protein structure determination and prediction, active site detection, and protein sequence alignment techniques all exploit information about protein structure and structural relationships. For membrane proteins, however, there is limited agreement among available online tools for highlighting and mapping such structural similarities. Moreover, no available resource provides a systematic overview of quaternary and internal symmetries, and their orientation relative to the membrane, despite the fact that these properties can provide key insights into membrane protein function and evolution. Here, we describe the Encyclopedia of Membrane Proteins Analyzed by Structure and Symmetry (EncoMPASS), a database for relating integral membrane proteins of known structure from the points of view of sequence, structure, and symmetry. EncoMPASS is accessible through a web interface, and its contents can be easily downloaded. This allows the user not only to focus on specific proteins, but also to study general properties of the structure and evolution of membrane proteins.
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