ArticleACS nano2021
Mechanisms of Scaffold-Mediated Microcompartment Assembly and Size Control.
Article in ACS nano, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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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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.
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Who cites it
21 citing papers in PubMed.
- Unlocking the bacterial condensome: from "dark matter" to design.Molecular biology of the cell · 2026Article
- Peptide-Ligand Cooperative Interplay Drives Gold Nanoparticle Encapsulation by Protein Cages.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Many paths, similar destinations: viruses and bacterial microcompartments form polyhedra inside cells.Journal of virology · 2026Review
- Carbon dioxide concentration alters cyanobacterial carboxysome encapsulation and redox state in Synechococcus sp. PCC 7002.Communications biology · 2026Article
- [COResearch square · 2026Article
- Robust Synthetic Biology Toolkit to Advance Carboxysome Study and Redesign.ACS synthetic biology · 2025Article
- Kinetic Description of Viral Capsid Self-Assembly Using Mesoscopic Non-Equilibrium Thermodynamics.Entropy (Basel, Switzerland) · 2025Article
- α-Carboxysome Size Is Controlled by the Disordered Scaffold Protein CsoS2.Biochemistry · 2024Article
- Modeling bacterial microcompartment architectures for enhanced cyanobacterial carbon fixation.Frontiers in plant science · 2024Review
- Effect of ionic strength on the assembly of simian vacuolating virus capsid protein around poly(styrene sulfonate).The European physical journal. E, Soft matter · 2023Article
- Temporal control by cofactors prevents kinetic trapping in retroviral Gag lattice assembly.Biophysical journal · 2023Article
- Heterologous Assembly of Pleomorphic Bacterial Microcompartment Shell Architectures Spanning the Nano- to Microscale.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- Self-assembly coupled to liquid-liquid phase separation.PLoS computational biology · 2023Article
- Performance efficient macromolecular mechanics via sub-nanometer shape based coarse graining.Nature communications · 2023Article
- Inferring assembly-curving trends of bacterial micro-compartment shell hexamers from crystal structure arrangements.PLoS computational biology · 2023Article
- Article
- Linking the Salmonella enterica 1,2-Propanediol Utilization Bacterial Microcompartment Shell to the Enzymatic Core via the Shell Protein PduB.Journal of bacteriology · 2022Article
- Microcompartment assembly around multicomponent fluid cargoes.The Journal of chemical physics · 2022Article
- Chemical probing provides insight into the native assembly state of a bacterial microcompartment.Structure (London, England : 1993) · 2022Article
- Recent structural insights into bacterial microcompartment shells.Current opinion in microbiology · 2021Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
This article describes a theoretical and computational study of the dynamical assembly of a protein shell around a complex consisting of many cargo molecules and long, flexible scaffold molecules. Our study is motivated by bacterial microcompartments, which are proteinaceous organelles that assemble around a condensed droplet of enzymes and reactants. As in many examples of cytoplasmic liquid-liquid phase separation, condensation of the microcompartment interior cargo is driven by flexible scaffold proteins that have weak multivalent interactions with the cargo. Our results predict that the shell size, amount of encapsulated cargo, and assembly pathways depend sensitively on properties of the scaffold, including its length and valency of scaffold-cargo interactions. Moreover, the ability of self-assembling protein shells to change their size to accommodate scaffold molecules of different lengths depends crucially on whether the spontaneous curvature radius of the protein shell is smaller or larger than a characteristic elastic length scale of the shell. Beyond natural microcompartments, these results have important implications for synthetic biology efforts to target alternative molecules for encapsulation by microcompartments or viral shells. More broadly, the results elucidate how cells exploit coupling between self-assembly and liquid-liquid phase separation to organize their interiors.
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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.