ArticleNature structural & molecular biology2024
Vimentin filaments integrate low-complexity domains in a complex helical structure.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Cardiomyocyte vulnerability to lamin polymer disruption revealed by saturation mutagenesis.bioRxiv : the preprint server for biology · 2026Article
- Too rigid to strike: Excess desmin at Z-discs underlies a restrictive cardiomyopathy in GAN mice.iScience · 2026Article
- Article
- Vimentin remodeling in response to oxidants and electrophiles is modulated by pH.Science advances · 2026Article
- Article
- Vimentin's Journey from "Background Scaffold" to Multi-Scale Regulator of Neuronal Growth and Function: Historical, Conceptual and Epistemic Perspectives.International journal of molecular sciences · 2026Review
- Solid state NMR characterization of wild-type and mutant GFAP intermediate filament assemblies.bioRxiv : the preprint server for biology · 2026Article
- Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026Article
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The myofibrillar myopathy-linked variant DES-p.T341P impairs desmin filament assembly.Molecular biology reports · 2026Article
- Unraveling the molecular mechanisms of vimentin interaction with G-quadruplex repeats.Nucleic acids research · 2026Article
- Architects of the Developing Brain: Cytoskeleton-Organizing Molecules in Neurodevelopmental Disorders.Cells · 2026Review
- Modulating Vimentin: A Systems-Level Therapeutic Strategy for Sepsis and Complex Diseases.Life (Basel, Switzerland) · 2026Article
- Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Intermediate Filaments: Structure-Mechanics Crosstalk.Sub-cellular biochemistry · 2026Review
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Vimentin Dynamics in Viral Infection: Shield or Sabotage?International journal of molecular sciences · 2025Review
- Desmin-p.L112Q Disturbs Filament Formation and Is a Likely-Pathogenic Variant Associated with Dilated Cardiomyopathy.Journal of cardiovascular development and disease · 2025Article
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.bioRxiv : the preprint server for biology · 2025Article
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11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intermediate filaments (IFs) are integral components of the cytoskeleton. They provide cells with tissue-specific mechanical properties and are involved in numerous cellular processes. Due to their intricate architecture, a 3D structure of IFs has remained elusive. Here we use cryo-focused ion-beam milling, cryo-electron microscopy and tomography to obtain a 3D structure of vimentin IFs (VIFs). VIFs assemble into a modular, intertwined and flexible helical structure of 40 α-helices in cross-section, organized into five protofibrils. Surprisingly, the intrinsically disordered head domains form a fiber in the lumen of VIFs, while the intrinsically disordered tails form lateral connections between the protofibrils. Our findings demonstrate how protein domains of low sequence complexity can complement well-folded protein domains to construct a biopolymer with striking mechanical strength and stretchability.
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