ArticleThe Journal of biological chemistry2004
Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance.
Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Metal Ion Binding of Vimentin Tail Domain Fragments.Chembiochem : a European journal of chemical biology · 2026Article
- The important interplay between metal ions and the intermediate filament protein vimentin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Impact of N-Terminal Tags on De Novo Vimentin Intermediate Filament Assembly.International journal of molecular sciences · 2022Article
- Review
- Completion of the Vimentin Rod Domain Structure Using Experimental Restraints: A New Tool for Exploring Intermediate Filament Assembly and Mutations.Structure (London, England : 1993) · 2019Article
- Structural basis for lamin assembly at the molecular level.Nature communications · 2019Article
- A crystal structure of coil 1B of vimentin in the filamentous form provides a model of a high-order assembly of a vimentin filament.The FEBS journal · 2018Article
- Production of recombinant human tektin 1, 2, and 4 and in vitro assembly of human tektin 1.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Structural Dynamics of the Vimentin Coiled-coil Contact Regions Involved in Filament Assembly as Revealed by Hydrogen-Deuterium Exchange.The Journal of biological chemistry · 2016Article
- Methods for Determining the Cellular Functions of Vimentin Intermediate Filaments.Methods in enzymology · 2016Article
- Electron paramagnetic resonance analysis of the vimentin tail domain reveals points of order in a largely disordered region and conformational adaptation upon filament assembly.Protein science : a publication of the Protein Society · 2013Article
- The bipolar assembly domain of the mitotic motor kinesin-5.Nature communications · 2013Article
- Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The structure of vimentin linker 1 and rod 1B domains characterized by site-directed spin-labeling electron paramagnetic resonance (SDSL-EPR) and X-ray crystallography.The Journal of biological chemistry · 2012Article
- Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.The Journal of biological chemistry · 2010Article
- Head and rod 1 interactions in vimentin: identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance.The Journal of biological chemistry · 2009Article
- Identification of phosphorylation-induced changes in vimentin intermediate filaments by site-directed spin labeling and electron paramagnetic resonance.Biochemistry · 2008Article
- Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin.Investigative ophthalmology & visual science · 2007Article
- Treatment of keratin intermediate filaments with sulfur mustard analogs.Biochemical and biophysical research communications · 2007Article
- Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have previously established the utility of site-directed spin labeling and electron paramagnetic resonance to determine structural relationships among proteins in intact intermediate filaments. Using this same approach we have introduced spin labels at 21 residues between amino acids 169 and 193 in rod domain 1 of human vimentin. The electron paramagnetic resonance spectra provide direct evidence for the coiled coil nature of the vimentin dimer in this region. This finding is consistent with predictions but has never been demonstrated previously. In a previous study we identified residue 348 in the rod domain 2 as one point of overlap between adjacent dimers in intact filaments. In the present study we defined residue 191 in the rod domain 1 as a second point of overlap and established that the dimers are arranged in an anti-parallel and staggered orientation at this site. Finally, by isolating spin-labeled samples at successive stages during the dialysis that lead to filament assembly in vitro, we have been able to establish a sequence of interactions that occurs during in vitro assembly, starting with the alpha helix and loose coiled coil dimer formation, then the formation of tetrameric species centered on residue 191, followed by interactions centered on residue 348 suggestive of octamer or higher order multimer formation. A continuation of this strategy revealed that both 191-191 and 348-348 interactions are present in low ionic strength Tris buffers when vimentin is maintained at the "protofilament" stage of assembly.
Indexed as
Identifiers
What OpenQuestion holds
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.