Evidence map›Paper›PMID 31325491›Full record

ArticleMethods (San Diego, Calif.)2020

Quantification of trans-synaptic protein alignment: A data analysis case for single-molecule localization microscopy.

Jia-Hui Chen, Thomas A Blanpied, Ai-Hui Tang

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
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  6. Distinct SAP102 and PSD-95 Nano-organization Defines Multiple Types of Synaptic Scaffold Protein Domains at Single Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  7. Article
  8. Structural and functional reorganization of inhibitory synapses by activity-dependent cleavage of neuroligin-2.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Molecular definition of distinct active zone protein machineries for CabioRxiv : the preprint server for biology · 2023
    Article
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  11. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Jia-Hui ChenCAS Key Laboratory of Brain Function and Disease and Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, China.
Thomas A BlanpiedProgram in Neuroscience and Department of Physiology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
Ai-Hui TangCAS Key Laboratory of Brain Function and Disease and Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230026, China. Electronic address: tangah@ustc.edu.cn.

Funding

Internal Dynamics of the Postsynaptic DensityR37MH080046 · NIMH · UNIVERSITY OF MARYLAND BALTIMORE · PI Thomas A Blanpied · 2020 to 2026
$5.0M
Internal Dynamics of the Postsynaptic DensityR01MH080046 · NIMH · UNIVERSITY OF MARYLAND BALTIMORE · PI BLANPIED, THOMAS A · 2007 to 2019
$4.5M
CRCNS: Transmitter Release Site Organization in Plasticity and Disease at the NMJR01NS090644 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BLANPIED, THOMAS A, LAGHAEI, ROZITA · 2014 to 2018
$1.9M
NIMH NIH HHS R01 MH080046NIMH NIH HHS R37 MH080046NINDS NIH HHS R01 NS090644
6 · The paper itself

Abstract

Nanoscale distribution of proteins and their relative positioning within a defined subcellular region are key to their physiological functions. Thanks to the super-resolution imaging methods, especially single-molecule localization microscopy (SMLM), mapping the three-dimensional distribution of multiple proteins has been easier and more efficient than ever. Nevertheless, in spite of the many tools available for efficient localization detection and image rendering, it has been a challenge to quantitatively analyze the 3D distribution and relative positioning of proteins in these SMLM data. Here, using heterogeneously distributed synaptic proteins as examples, we describe in detail a series of analytical methods including detection of nanoscale density clusters, quantification of the trans-synaptic alignment between these protein densities, and automatic en face projection and averaging. These analyses were performed within customized Matlab routines and we make the full scripts available. The concepts behind these analytical methods and the scripts can be adapted for quantitative analysis of spatial organization of other macromolecular complexes.

Indexed as

Chromosome PairingDisks Large Homolog 4 ProteinGTP-Binding ProteinsHippocampusImage Processing, Computer-AssistedImaging, Three-DimensionalNerve Tissue ProteinsNeuronsProteinsProtein Structure, Tertiaryrab3 GTP-Binding ProteinsSingle Molecule ImagingSynaptic TransmissionDisks Large Homolog 4 ProteinGTP-Binding ProteinsNerve Tissue ProteinsProteinsrab3 GTP-Binding ProteinsRIMS1 protein, humanRIMS2 protein, humanLocalization microscopyNanoclusterNanocolumnsProtein enrichmentStochastic optical reconstruction microscopy (STORM)Three-dimensional

Identifiers

PMID31325491
PMCPMC6980469

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Registered trials

None linked

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.