Evidence map›Paper›PMID 34538002›Full record

ArticleProtein science : a publication of the Protein Society2021

Zinc-chelating postsynaptic density-95 N-terminus impairs its palmitoyl modification.

Yonghong Zhang, Xiaoqian Fang, Luis Ascota, Libo Li, Lili Guerra, Audrey Vega, Amanda Salinas, Andrea Gonzalez, Claudia Garza, Andrew Tsin and 2 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 46% of its field
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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Review
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  4. Zinc-chelating postsynaptic density-95 N-terminus impairs its palmitoyl modification.Protein science : a publication of the Protein Society · 2021
    Article
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

12 authors at 3 institutions in 2 countries.

Yonghong ZhangDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.ORCID 0000-0002-7305-9295
Xiaoqian FangDepartment of Molecular Science, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Luis AscotaDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Libo LiDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Lili GuerraDepartment of Molecular Science, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Audrey VegaDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Amanda SalinasDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Andrea GonzalezDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Claudia GarzaDepartment of Chemistry, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Andrew TsinDepartment of Molecular Science, The University of Texas Rio Grande Valley, Edinburg, Texas, USA.
Johannes W HellDepartment of Pharmacology, University of California, Davis, California, USA.
James B AmesDepartment of Chemistry, University of California, Davis, California, USA.
The University of Texas Rio Grande Valley · USUniversity of California, Davis · USHarbin University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chemical synaptic transmission represents the most sophisticated dynamic process and is highly regulated with optimized neurotransmitter balance. Imbalanced transmitters can lead to transmission impairments, for example, intracellular zinc accumulation is a hallmark of degenerating neurons. However, the underlying mechanisms remain elusive. Postsynaptic density protein-95 (PSD-95) is a primary postsynaptic membrane-associated protein and the major scaffolding component in the excitatory postsynaptic densities, which performs substantial functions in synaptic development and maturation. Its membrane association induced by palmitoylation contributes largely to its regulatory functions at postsynaptic sites. Unlike other structural domains in PSD-95, the N-terminal region (PSD-95NT) is flexible and interacts with various targets, which modulates its palmitoylation of two cysteines (C3/C5) and glutamate receptor distributions in postsynaptic densities. PSD-95NT contains a putative zinc-binding motif (C2H2) with undiscovered functions. This study is the first effort to investigate the interaction between Zn

Indexed as

Chelating AgentsDisks Large Homolog 4 ProteinLipoylationZincAmino Acid MotifsHEK293 CellsHumansProtein DomainsChelating AgentsDisks Large Homolog 4 ProteinDLG4 protein, humanZincN-terminal domainpalmitoylationPSD-95zinc binding

Identifiers

PMID34538002
PMCPMC8521293
OpenAlexW3201500007

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.