ArticleStructure (London, England : 1993)2015
Structural plasticity of helical nanotubes based on coiled-coil assemblies.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed, 120 citations in OpenAlex.
- Amphipathic β‑Sheet-Forming Octapeptide Self-Assembly Using the Martini Potential Family.ACS omega · 2026Article
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- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
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- Structure of the virulence-associatedProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Amphipathic Antimicrobial Peptides Illuminate a Reciprocal Relationship Between Self-assembly and Cytolytic Activity.Angewandte Chemie (International ed. in English) · 2025Article
- Article
- Fragment-Based Approach for Hierarchical Nanotube Assembly of Small Molecules in Aqueous Phase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Tuning Helical Peptide Nanofibers as a Sublingual Vaccine Platform for a Variety of Peptide Epitopes.Advanced healthcare materials · 2025Article
- Genetically Fusing Order-Promoting and Thermoresponsive Building Blocks to Design Hybrid Biomaterials.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Review
- Structural Analyses of Designed α-Helix and β-Sheet Peptide Nanofibers Using Solid-State Nuclear Magnetic Resonance and Cryo-Electron Microscopy and Introduction of Structure-Based Metal-Responsive Properties.International journal of molecular sciences · 2024Article
- Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Single-molecule visualization determines conformational substate ensembles in β-sheet-rich peptide fibrils.Science advances · 2023Article
- Electron cryo-microscopy reveals the structure of the archaeal thread filament.Nature communications · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Multiepitope supramolecular peptide nanofibers eliciting coordinated humoral and cellular antitumor immune responses.Science advances · 2022Article
- Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Atomic structure of Lanreotide nanotubes revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Numerous instances can be seen in evolution in which protein quaternary structures have diverged while the sequences of the building blocks have remained fairly conserved. However, the path through which such divergence has taken place is usually not known. We have designed two synthetic 29-residue α-helical peptides, based on the coiled-coil structural motif, that spontaneously self-assemble into helical nanotubes in vitro. Using electron cryomicroscopy with a newly available direct electron detection capability, we can achieve near-atomic resolution of these thin structures. We show how conservative changes of only one or two amino acids result in dramatic changes in quaternary structure, in which the assemblies can be switched between two very different forms. This system provides a framework for understanding how small sequence changes in evolution can translate into very large changes in supramolecular structure, a phenomenon that may have significant implications for the de novo design of synthetic peptide assemblies.
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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.