ArticleProceedings of the National Academy of Sciences of the United States of America2016
Energy landscapes of a mechanical prion and their implications for the molecular mechanism of long-term memory.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- An Anti-Amyloidogenic Approach to Specifically Block Memory Consolidation in Mice for Therapeutic Intervention.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Generating the polymorph landscapes of amyloid fibrils using AI: RibbonFold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Invasive mussels fashion silk-like byssus via mechanical processing of massive horizontally acquired coiled coils.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Exploring the structural acrobatics of fold-switching proteins using simplified structure-based models.Biophysical reviews · 2023Review
- Finite element modeling of α-helices and tropocollagen molecules referring to spike of SARS-CoV-2.Biophysical journal · 2022Article
- Article
- Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold.BMC biology · 2021Article
- Exploring the F-actin/CPEB3 interaction and its possible role in the molecular mechanism of long-term memory.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Coiled-Coil Motifs of RNA-Binding Proteins: Dynamicity in RNA Regulation.Frontiers in cell and developmental biology · 2020Article
- A continuous model of physiological prion aggregation suggests a role for Orb2 in gating long-term synaptic information.Royal Society open science · 2018Article
- Template-Guided Protein Structure Prediction and Refinement Using Optimized Folding Landscape Force Fields.Journal of chemical theory and computation · 2018Article
- Trans-acting translational regulatory RNA binding proteins.Wiley interdisciplinary reviews. RNA · 2018Review
- Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protein Folding and Structure Prediction from the Ground Up II: AAWSEM for α/β Proteins.The journal of physical chemistry. B · 2017Article
- Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.Journal of molecular biology · 2017Article
- Article
- The Aggregation Free Energy Landscapes of Polyglutamine Repeats.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Aplysia cytoplasmic polyadenylation element binding (CPEB) protein, a translational regulator that recruits mRNAs and facilitates translation, has been shown to be a key component in the formation of long-term memory. Experimental data show that CPEB exists in at least a low-molecular weight coiled-coil oligomeric form and an amyloid fiber form involving the Q-rich domain (CPEB-Q). Using a coarse-grained energy landscape model, we predict the structures of the low-molecular weight oligomeric form and the dynamics of their transitions to the β-form. Up to the decamer, the oligomeric structures are predicted to be coiled coils. Free energy profiles confirm that the coiled coil is the most stable form for dimers and trimers. The structural transition from α to β is shown to be concentration dependent, with the transition barrier decreasing with increased concentration. We observe that a mechanical pulling force can facilitate the α-helix to β-sheet (α-to-β) transition by lowering the free energy barrier between the two forms. Interactome analysis of the CPEB protein suggests that its interactions with the cytoskeleton could provide the necessary mechanical force. We propose that, by exerting mechanical forces on CPEB oligomers, an active cytoskeleton can facilitate fiber formation. This mechanical catalysis makes possible a positive feedback loop that would help localize the formation of CPEB fibers to active synapse areas and mark those synapses for forming a long-term memory after the prion form is established. The functional role of the CPEB helical oligomers in this mechanism carries with it implications for targeting such species in neurodegenerative diseases.
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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.