ArticleNature communications2015
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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.
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.
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Who cites it
31 citing papers in PubMed, 57 citations in OpenAlex.
- Cell Adhesion and Biofilm Development via Force-Sensitive Mechanisms: A Perspective.ACS biomaterials science & engineering · 2026Review
- Predicting absolute protein folding stability using generative models.Protein science : a publication of the Protein Society · 2025Article
- Polymicrobial interactions betweenbioRxiv : the preprint server for biology · 2024Article
- Genetically encoded barcodes for correlative volume electron microscopy.Nature biotechnology · 2023Article
- S373P Mutation Stabilizes the Receptor-Binding Domain of the Spike Protein in Omicron and Promotes Binding.JACS Au · 2023Article
- Modulating the Viscoelastic Properties of Covalently Crosslinked Protein Hydrogels.Gels (Basel, Switzerland) · 2023Article
- The staphylococcal biofilm protein Aap mediates cell-cell adhesion through mechanically distinct homophilic and lectin interactions.PNAS nexus · 2022Article
- The long and the short of Periscope Proteins.Biochemical Society transactions · 2022Review
- Solution Structural Studies of Pre-amyloid Oligomer States of the Biofilm Protein Aap.Journal of molecular biology · 2022Article
- On the Effects of Disordered Tails, Supertertiary Structure and Quinary Interactions on the Folding and Function of Protein Domains.Biomolecules · 2022Review
- Periscope Proteins are variable-length regulators of bacterial cell surface interactions.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.The Journal of biological chemistry · 2020Article
- An expanded library of orthogonal split inteins enables modular multi-peptide assemblies.Nature communications · 2020Article
- Surface Proteins ofFrontiers in microbiology · 2020Review
- Binding Strength of Gram-Positive Bacterial Adhesins.Frontiers in microbiology · 2020Review
- Multistep Protein Unfolding Scenarios from the Rupture of a Complex Metal Cluster CdScientific reports · 2019Article
- Surface Proteins ofMicrobiology spectrum · 2019Review
- SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale.Protein science : a publication of the Protein Society · 2019Article
- Staphylococcal Biofilms.Microbiology spectrum · 2018Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability of its domains. The remarkable mechanical strength of SasG arises from tandemly arrayed 'clamp' motifs within the folded domains. Our findings reveal an elegant minimal solution for the assembly of monomeric mechano-resistant tethers of variable length.
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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.