ArticleScience (New York, N.Y.)2018
Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks.
Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 259 papers.
What it found
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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
259 citing papers in PubMed, 474 citations in OpenAlex.
- Biomolecular coacervation-mediated materials: Phase states, phase transitions, and biomedical applications.Bioactive materials · 2027Review
- Structural Hierarchy and Maturation of Amyloid Fibrils Revealed by Interface Descriptor Analysis.Journal of chemical information and modeling · 2026Article
- Biomolecular Condensates Integrate Transcriptional and Epigenetic Responses to Hypoxia.International journal of molecular sciences · 2026Review
- Compositionally Biased Regions Within Structured Protein Domains.Biomolecules · 2026Article
- Programmable Multiphasic Condensates Formed via Evaporation-Induced Phase Separation of Minimal Peptide Model.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins.Nature communications · 2026Article
- Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins.PNAS nexus · 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
- FuzDrop: sequence-based prediction of the propensity of proteins for liquid-liquid phase separation and aggregation.Nature protocols · 2026Review
- Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.Biomolecules · 2026Review
- Oligomerization of PER2 as a dynamic mode of regulation of the mammalian circadian clock.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Biomolecular Condensates in Disease: Decoding the Material State and Engineering Precision Modulators.International journal of molecular sciences · 2026Review
- Article
- Structural and Functional Elements of the Epidermal Appendages in Birds and Reptiles: Conformations and Modes of Assembly of the Constituent β-Filaments and Keratin Intermediate Filaments (IF).Sub-cellular biochemistry · 2026Review
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Chiral inversion mutagenesis identifies geometrically constrained residues within self-associating low-complexity domains.bioRxiv : the preprint server for biology · 2025Article
- Proteome-wide computational analyses reveal links between protein condensate formation and RNA biology.Science advances · 2025Article
- Structural basis for T-cell intracellular antigen-1 amyloid fibril formation revealed by cryo-electron microscopy.PNAS nexus · 2025Article
- Article
- Visualizing liquid-liquid phase separation and protein aggregates.Communications chemistry · 2025Review
199 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Subcellular membraneless assemblies are a reinvigorated area of study in biology, with spirited scientific discussions on the forces between the low-complexity protein domains within these assemblies. To illuminate these forces, we determined the atomic structures of five segments from protein low-complexity domains associated with membraneless assemblies. Their common structural feature is the stacking of segments into kinked β sheets that pair into protofilaments. Unlike steric zippers of amyloid fibrils, the kinked sheets interact weakly through polar atoms and aromatic side chains. By computationally threading the human proteome on our kinked structures, we identified hundreds of low-complexity segments potentially capable of forming such interactions. These segments are found in proteins as diverse as RNA binders, nuclear pore proteins, and keratins, which are known to form networks and localize to membraneless assemblies.
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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.