ArticleProceedings of the National Academy of Sciences of the United States of America2010
Experimental detection of knotted conformations in denatured proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed.
- Generating knotted polymer and protein structures by machine learning.Communications chemistry · 2026Article
- Phosphoglycerate Kinase Can Adopt Topologically Misfolded Forms That Are More Stable Than Its Native State.Journal of the American Chemical Society · 2026Article
- Structural basis of enhanced stalling efficiency of an engineered ribosome arrest peptide.Nucleic acids research · 2025Article
- Folding of a tandemly knotted protein: Evidence that a polypeptide chain can get out of deep kinetic traps.Protein science : a publication of the Protein Society · 2025Article
- A Marcus-Type Inverted Region in the Translocation Kinetics of a Knotted Protein.The journal of physical chemistry letters · 2023Article
- Folding kinetics of an entangled protein.PLoS computational biology · 2023Article
- Long-lived metastable knots in polyampholyte chains.PloS one · 2023Article
- Revealing Topological Barriers against Knot Untying in Thermal and Mechanical Protein Unfolding by Molecular Dynamics Simulations.Biomolecules · 2021Article
- Tying up the Loose Ends: A Mathematically Knotted Protein.Frontiers in chemistry · 2021Article
- Article
- Mechanical unfolding of a knotted protein unveils the kinetic and thermodynamic consequences of threading a polypeptide chain.Scientific reports · 2020Article
- The AAA+ protease ClpXP can easily degrade a 3Scientific reports · 2019Article
- Stabilizing Effect of Inherent Knots on Proteins Revealed by Molecular Dynamics Simulations.Biophysical journal · 2018Article
- The Pathways of the iRFP713 Unfolding Induced by Different Denaturants.International journal of molecular sciences · 2018Article
- KymoKnot: A web server and software package to identify and locate knots in trajectories of linear or circular polymers.The European physical journal. E, Soft matter · 2018Article
- The energy cost of polypeptide knot formation and its folding consequences.Nature communications · 2017Article
- To Tie or Not to Tie? That Is the Question.Polymers · 2017Review
- Small methyltransferase RlmH assembles a composite active site to methylate a ribosomal pseudouridine.Scientific reports · 2017Article
- Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome.Scientific reports · 2017Article
- Knotting and unknotting proteins in the chaperonin cage: Effects of the excluded volume.PloS one · 2017Article
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3 authors.
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Abstract
Structures that contain a knot formed by the path of the polypeptide backbone represent some of the most complex topologies observed in proteins. How or why these topological knots arise remains unclear. By developing a method to experimentally trap and detect knots in nonnative polypeptide chains, we find that two knotted methyltransferases, YibK and YbeA, can exist in a trefoil-knot conformation even in their chemically unfolded states. The unique denatured-state topology of these molecules explains their ability to efficiently fold to their native knotted structures in vitro and offers insights into the potential role of knots in proteins. Furthermore, the high prevalence of the denatured-state knots identified here suggests that they are either difficult to untie or that threading of any untied molecules is rapid and spontaneous. The occurrence of such knotted topologies in unfolded polypeptide chains raises the possibility that they could play an important, and as yet unexplored, role in folding and misfolding processes in vivo.
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