ArticleThe Journal of biological chemistry2002
Real-time observation of coiled-coil domains and subunit assembly in intermediate filaments.
Article in The Journal of biological chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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
20 citing papers in PubMed, 42 citations in OpenAlex.
- Review
- Molecular Insight into the Regulation of Vimentin by Cysteine Modifications and Zinc Binding.Antioxidants (Basel, Switzerland) · 2021Article
- Separation of Coiled-Coil Structures in Lamin A/C Is Required for the Elongation of the Filament.Cells · 2020Article
- 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
- 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
- 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
- Probing of the assembly structure and dynamics within nanoparticles during interaction with blood proteins.ACS nano · 2012Article
- Postprandial apoE isoform and conformational changes associated with VLDL lipolysis products modulate monocyte inflammation.PloS one · 2012Article
- A differential association of Apolipoprotein E isoforms with the amyloid-β oligomer in solution.Proteins · 2011Article
- Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.The Journal of biological chemistry · 2010Article
- Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation.Physical chemistry chemical physics : PCCP · 2009Article
- 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
- Treatment of keratin intermediate filaments with sulfur mustard analogs.Biochemical and biophysical research communications · 2007Article
- Sequential and combinatorial roles of maf family genes define proper lens development.Molecular vision · 2007Article
- Characterization of the linker 2 region in human vimentin using site-directed spin labeling and electron paramagnetic resonance.Biochemistry · 2006Article
- A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability.The Journal of cell biology · 2005Article
- Characterization of structural changes in vimentin bearing an epidermolysis bullosa simplex-like mutation using site-directed spin labeling and electron paramagnetic resonance.The Journal of biological chemistry · 2005Article
- 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.The Journal of biological chemistry · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have utilized electron paramagnetic resonance spectroscopy to study secondary structure, subunit interaction, and molecular orientation of vimentin molecules within intact intermediate filaments and assembly intermediates. Spectroscopy data prove alpha-helical coiled-coil structures at individual amino acids 316-336 located in rod 2B. Analysis of positions 305, 309, and 312 identify this region as conforming to the helical pattern identified within 316-336 and thus demonstrates that, contrary to some previous predictions, this region is in an alpha-helical conformation. We show that by varying the position of the spin label, we can identify both intra- and inter-dimer interactions. With a label attached to the outside of the alpha-helix, we have been able to measure interactions between positions 348 of separate dimers as they align together in intact filaments, identifying the exact point of overlap. By mixing different spin-labeled proteins, we demonstrate that the interaction at position 348 is the result of an anti-parallel arrangement of dimers. This approach provides high resolution structural information (<2 nm resolution), can be used to identify molecular arrangements between subunits in an intact intermediate filament, and should be applicable to other noncrystallizable filamentous systems as well as to the study of protein fibrils.
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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.