ArticleThe Biochemical journal2015
Arc is a flexible modular protein capable of reversible self-oligomerization.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
47 citing papers in PubMed, 81 citations in OpenAlex.
- Nanoscale Spatial Organization of ARC High- and Low-Order Assemblies at Excitatory Synapses.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- A retroelement-derived mammalian ARC protein exhibits selective RNA recognition and nucleic acid chaperone functions.Nucleic acids research · 2026Article
- A Nanobody-Based Proximity Ligation Assay Detects Constitutive and Stimulus-Regulated Native Arc/Arg3.1 Oligomers in Hippocampal Neuronal Dendrites.Molecular neurobiology · 2025Article
- "Arc - A viral vector of memory and synaptic plasticity".Current opinion in neurobiology · 2025Review
- Human Virus-Like Proteins: Implications for Gene Therapy.Current gene therapy · 2025Review
- Endogenous capsid-forming protein ARC for self-assembling nanoparticle vaccines.Journal of nanobiotechnology · 2024Article
- Phosphatidylinositol-3-phosphate mediates Arc capsid secretion through the multivesicular body pathway.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Analysis of Arc/Arg3.1 Oligomerization In Vitro and in Living Cells.International journal of molecular sciences · 2024Article
- Mimicking Protein Kinase C Phosphorylation Inhibits Arc/Arg3.1 Palmitoylation and Its Interaction with Nucleic Acids.International journal of molecular sciences · 2024Article
- Structural characterization of two nanobodies targeting the ligand-binding pocket of human Arc.PloS one · 2024Article
- Article
- Domain tethering impacts dimerization and DNA-mediated allostery in the human transcription factor FoxP1.The Journal of chemical physics · 2023Article
- Extending fluorescence anisotropy to large complexes using reversibly switchable proteins.Nature biotechnology · 2023Article
- ARC/Arg3.1 expression in the lateral geniculate body of monocular form deprivation amblyopic kittens.BMC ophthalmology · 2023Article
- Detection of Arc/Arg3.1 oligomers in rat brain: constitutive and synaptic activity-evoked dimer expressionFrontiers in molecular neuroscience · 2023Article
- Molecular physiology of Arc/Arg3.1: The oligomeric state hypothesis of synaptic plasticity.Acta physiologica (Oxford, England) · 2022Review
- Development and Validation of Arc Nanobodies: New Tools for Probing Arc Dynamics and Function.Neurochemical research · 2022Article
- 'Arc'-hitecture of normal cognitive aging.Ageing research reviews · 2022Review
- High-affinity anti-Arc nanobodies provide tools for structural and functional studies.PloS one · 2022Article
- Phosphorylation-dependent control of Activity-regulated cytoskeleton-associated protein (Arc) protein by TNIK.Journal of neurochemistry · 2021Article
Corrections and comments
- Commented on by
Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The immediate early gene product Arc (activity-regulated cytoskeleton-associated protein) is posited as a master regulator of long-term synaptic plasticity and memory. However, the physicochemical and structural properties of Arc have not been elucidated. In the present study, we expressed and purified recombinant human Arc (hArc) and performed the first biochemical and biophysical analysis of hArc's structure and stability. Limited proteolysis assays and MS analysis indicate that hArc has two major domains on either side of a central more disordered linker region, consistent with in silico structure predictions. hArc's secondary structure was estimated using CD, and stability was analysed by CD-monitored thermal denaturation and differential scanning fluorimetry (DSF). Oligomerization states under different conditions were studied by dynamic light scattering (DLS) and visualized by AFM and EM. Biophysical analyses show that hArc is a modular protein with defined secondary structure and loose tertiary structure. hArc appears to be pyramid-shaped as a monomer and is capable of reversible self-association, forming large soluble oligomers. The N-terminal domain of hArc is highly basic, which may promote interaction with cytoskeletal structures or other polyanionic surfaces, whereas the C-terminal domain is acidic and stabilized by ionic conditions that promote oligomerization. Upon binding of presenilin-1 (PS1) peptide, hArc undergoes a large structural change. A non-synonymous genetic variant of hArc (V231G) showed properties similar to the wild-type (WT) protein. We conclude that hArc is a flexible multi-domain protein that exists in monomeric and oligomeric forms, compatible with a diverse, hub-like role in plasticity-related processes.
Indexed as
Identifiers
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.