ArticleProceedings of the National Academy of Sciences of the United States of America2012
Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed, 175 citations in OpenAlex.
- Whole-exome sequencing to identify a novel LMNA gene mutation associated with inherited cardiac conduction disease.PloS one · 2013Trial
- Keratin filaments and soluble vimentin interact with isoform specificity to organize cell signaling.Genes & development · 2026Article
- DirectContacts2: a wiring diagram of human physical protein interactions.Nature communications · 2026Article
- 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
- Unraveling the molecular mechanisms of vimentin interaction with G-quadruplex repeats.Nucleic acids research · 2026Article
- Intermediate Filaments: Structure-Mechanics Crosstalk.Sub-cellular biochemistry · 2026Review
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- A dynamic biointerface in mussels mediated by a mechanoresponsive intermediate filament-based biopolymer.Nature communications · 2025Article
- Article
- [Advances in the Structure and Function of Neurofilament Protein and Its Application in Early Diagnosis of Amyotrophic Lateral Sclerosis].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2025Review
- Vimentin Fragmentation and Its Role in Amyloid-Beta Plaque Deposition in Alzheimer's Disease.International journal of molecular sciences · 2025Article
- The GFAP proteoform puzzle: How to advance GFAP as a fluid biomarker in neurological diseases.Journal of neurochemistry · 2025Review
- Deciphering vimentin assembly: Bridging theoretical models and experimental approaches.Molecules and cells · 2024Review
- Vimentin-mediated buffering of internal integrin β1 pool increases survival of cells from anoikis.BMC biology · 2024Article
- Vimentin filaments integrate low-complexity domains in a complex helical structure.Nature structural & molecular biology · 2024Article
- Review
- Article
- From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain.The European physical journal. E, Soft matter · 2024Article
- Filament structure and subcellular organization of the bacterial intermediate filament-like protein crescentin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Together with actin filaments and microtubules, intermediate filaments (IFs) are the basic cytoskeletal components of metazoan cells. Over 80 human diseases have been linked to mutations in various IF proteins to date. However, the filament structure is far from being resolved at the atomic level, which hampers rational understanding of IF pathologies. The elementary building block of all IF proteins is a dimer consisting of an α-helical coiled-coil (CC) "rod" domain flanked by the flexible head and tail domains. Here we present three crystal structures of overlapping human vimentin fragments that comprise the first half of its rod domain. Given the previously solved fragments, a nearly complete atomic structure of the vimentin rod has become available. It consists of three α-helical segments (coils 1A, 1B, and 2) interconnected by linkers (L1 and L12). Most of the CC structure has a left-handed twist with heptad repeats, but both coil 1B and coil 2 also exhibit untwisted, parallel stretches with hendecad repeats. In the crystal structure, linker L1 was found to be α-helical without being involved in the CC formation. The available data allow us to construct an atomic model of the antiparallel tetramer representing the second level of vimentin assembly. Although the presence of the nonhelical head domains is essential for proper tetramer stabilization, the precise alignment of the dimers forming the tetramer appears to depend on the complementarity of their surface charge distribution patterns, while the structural plasticity of linker L1 and coil 1A plays a role in the subsequent IF assembly process.
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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.