ArticleNature communications2021
Ligand-directed two-step labeling to quantify neuronal glutamate receptor trafficking.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 51 citations in OpenAlex.
- Chemical reactions for the ligand-directed modification of native proteins.Chemical Society reviews · 2026Review
- Advancements and applications of click chemistry in protein labeling and bioconjugation.RSC advances · 2026Review
- Single-cell synaptome mapping of endogenous protein subpopulations in mammalian brain.Nature communications · 2025Article
- The synaptic vesicle cluster as a controller of pre- and postsynaptic structure and function.The Journal of physiology · 2025Review
- Rapid and reversible fluorescent probe enables repeated snapshot imaging of AMPA receptors during synaptic plasticity.Science advances · 2025Article
- Review
- Lipid-Directed Covalent Labeling of Plasma Membranes for Long-Term Imaging, Barcoding and Manipulation of Cells.JACS Au · 2025Article
- One-Step Maleimide-Based Dual Functionalization of Protein N-Termini.Angewandte Chemie (International ed. in English) · 2025Article
- AMPA receptors in the evolving synapse: structure, function, and disease implications.Frontiers in synaptic neuroscience · 2025Review
- Article
- Genetic code expansion, click chemistry, and light-activated PI3K reveal details of membrane protein trafficking downstream of receptor tyrosine kinases.bioRxiv : the preprint server for biology · 2024Article
- Late-Stage Functionalization of Living Organisms: Rethinking Selectivity in Biology.Chemical reviews · 2024Review
- Electroacupuncture protective effects after cerebral ischemia are mediated through miR-219a inhibition.Biological research · 2023Article
- Chemically programmable bacterial probes for the recognition of cell surface proteins.Materials today. Bio · 2023Article
- Single-molecule characterization of a bright and photostable deep-red fluorescent squaraine-figure-eight (SF8) dye.Dyes and pigments : an international journal · 2023Article
- High-resolution imaging and manipulation of endogenous AMPA receptor surface mobility during synaptic plasticity and learning.Science advances · 2022Article
- Organocatalytic atroposelective construction of axially chiral N, N- and N, S-1,2-azoles through novel ring formation approach.Nature communications · 2022Article
- The Shaping of AMPA Receptor Surface Distribution by Neuronal Activity.Frontiers in synaptic neuroscience · 2022Review
- Photoswitching endogenous glutamate receptors in neural ensembles and single synapses in vivo.Brain stimulationArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulation of glutamate receptor localization is critical for development and synaptic plasticity in the central nervous system. Conventional biochemical and molecular biological approaches have been widely used to analyze glutamate receptor trafficking, especially for α-amino-3-hydroxy-5-methyl-4-isoxazole-propionate-type glutamate receptors (AMPARs). However, conflicting findings have been reported because of a lack of useful tools for analyzing endogenous AMPARs. Here, we develop a method for the rapid and selective labeling of AMPARs with chemical probes, by combining affinity-based protein labeling and bioorthogonal click chemistry under physiological temperature in culture medium. This method allows us to quantify AMPAR distribution and trafficking, which reveals some unique features of AMPARs, such as a long lifetime and a rapid recycling in neurons. This method is also successfully expanded to selectively label N-methyl-D-aspartate-type glutamate receptors. Thus, bioorthogonal two-step labeling may be a versatile tool for investigating the physiological and pathophysiological roles of glutamate receptors in neurons.
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.