ArticleProceedings of the National Academy of Sciences of the United States of America2020
Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- A simple method for mapping the location of cross-β-forming regions within protein domains of low sequence complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Cryo-EM and solid state NMR together provide a more comprehensive structural investigation of protein fibrils.Protein science : a publication of the Protein Society · 2024Article
- Cryo-EM and Solid State NMR Together Provide a More Comprehensive Structural Investigation of Protein Fibrils.bioRxiv : the preprint server for biology · 2024Article
- Review
- Protein domains of low sequence complexity-dark matter of the proteome.Genes & development · 2024Article
- Labile assembly of a tardigrade protein induces biostasis.Protein science : a publication of the Protein Society · 2024Article
- CRISPR screen for protein inclusion formation uncovers a role for SRRD in the regulation of intermediate filament dynamics and aggresome assembly.PLoS genetics · 2024Article
- The Mechanoreception inCells · 2023Article
- Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain.Journal of the American Chemical Society · 2023Article
- Alternative splicing of a single exon causes a major impact on the affinity ofFrontiers in cell and developmental biology · 2023Article
- Single Cell in a Gravity Field.Life (Basel, Switzerland) · 2022Review
- Mutations linked to neurological disease enhance self-association of low-complexity protein sequences.Science (New York, N.Y.) · 2022Article
- Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies.Nature structural & molecular biology · 2022Article
- Bioinformatic identification of previously unrecognized amyloidogenic proteins.The Journal of biological chemistry · 2022Article
- Modeling the Structure and Interactions of Intrinsically Disordered Peptides with Multiple Replica, Metadynamics-Based Sampling Methods and Force-Field Combinations.Journal of chemical theory and computation · 2022Article
- How do protein domains of low sequence complexity work?RNA (New York, N.Y.) · 2022Review
- Keratin 1 as a cell-surface receptor in cancer.Biochimica et biophysica acta. Reviews on cancer · 2022Review
- Redox-mediated regulation of low complexity domain self-association.Current opinion in genetics & development · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The coiled-coil domains of intermediate filament (IF) proteins are flanked by regions of low sequence complexity. Whereas IF coiled-coil domains assume dimeric and tetrameric conformations on their own, maturation of eight tetramers into cylindrical IFs is dependent on either "head" or "tail" domains of low sequence complexity. Here we confirm that the tail domain required for assembly of
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Registered trials
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