ArticleOpen biology2022
Protein phase separation hotspots at the presynapse.
Article in Open biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed.
- Review
- Dissecting the propensity of RIM1 subdomains to form phase condensates.Scientific reports · 2026Article
- Active Zone: Linking Resolution Levels of Microscopic Modalities.Advances in neurobiology · 2026Review
- Article
- Stress-Induced Membraneless Organelles in Neurons: Bridging Liquid-Liquid Phase Separation and Neurodevelopmental Dysfunction.International journal of molecular sciences · 2025Review
- Loss of intracellular ATP affects axoplasmic viscosity and pathological protein aggregation in mammalian neurons.Science advances · 2025Article
- Tau forms synaptic nano-biomolecular condensates controlling the dynamic clustering of recycling synaptic vesicles.Nature communications · 2023Article
- Orchestrating vesicular and nonvesicular membrane dynamics by intrinsically disordered proteins.EMBO reports · 2023Review
- Looking for answers far away from the soma-the (un)known axonal functions of TDP-43, and their contribution to early NMJ disruption in ALS.Molecular neurodegeneration · 2023Review
- Neuronal biomolecular condensates and their implications in neurodegenerative diseases.Frontiers in aging neuroscience · 2023Review
- Protein phase separation hotspots at the presynapse.Open biology · 2022Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fundamental discoveries have shaped our molecular understanding of presynaptic processes, such as neurotransmitter release, active zone organization and mechanisms of synaptic vesicle (SV) recycling. However, certain regulatory steps still remain incompletely understood. Protein liquid-liquid phase separation (LLPS) and its role in SV clustering and active zone regulation now introduce a new perception of how the presynapse and its different compartments are organized. This article highlights the newly emerging concept of LLPS at the synapse, providing a systematic overview on LLPS tendencies of over 500 presynaptic proteins, spotlighting individual proteins and discussing recent progress in the field. Newly discovered LLPS systems like ELKS/liprin-alpha and Eps15/FCho are put into context, and further LLPS candidate proteins, including epsin1, dynamin, synaptojanin, complexin and rabphilin-3A, are highlighted.
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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.