Evidence map›Paper›PMID 10818142›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2000

Identification of proteins in the postsynaptic density fraction by mass spectrometry.

R S Walikonis, O N Jensen, M Mann, D W Provance, J A Mercer, M B Kennedy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed, 1 pooled it
11.1field-weighted citation impact, top 1% 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

130 citing papers in PubMed, 1 synthesis or guideline pooled it, 398 citations in OpenAlex.

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70 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

R S WalikonisDivision of Biology, California Institute of Technology, Pasadena, California 91125, USA.
O N Jensen
M Mann
D W Provance
J A Mercer
M B Kennedy
California Institute of Technology · USEuropean Molecular Biology Laboratory · DEMcLaughlin Research Institute · US

Funding

MOLECULAR STRUCTURE OF CNS POSTSYNAPTIC DENSITIESR01NS028710 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI KENNEDY, MARY B · 1990 to 2009
$2.9M
NINDS NIH HHS NS28710NINDS NIH HHS R01 NS028710
6 · The paper itself

Abstract

Our understanding of the organization of postsynaptic signaling systems at excitatory synapses has been aided by the identification of proteins in the postsynaptic density (PSD) fraction, a subcellular fraction enriched in structures with the morphology of PSDs. In this study, we have completed the identification of most major proteins in the PSD fraction with the use of an analytical method based on mass spectrometry coupled with searching of the protein sequence databases. At least one protein in each of 26 prominent protein bands from the PSD fraction has now been identified. We found 7 proteins not previously known to be constituents of the PSD fraction and 24 that had previously been associated with the PSD by other methods. The newly identified proteins include the heavy chain of myosin-Va (dilute myosin), a motor protein thought to be involved in vesicle trafficking, and the mammalian homolog of the yeast septin protein cdc10, which is important for bud formation in yeast. Both myosin-Va and cdc10 are threefold to fivefold enriched in the PSD fraction over brain homogenates. Immunocytochemical localization of myosin-Va in cultured hippocampal neurons shows that it partially colocalizes with PSD-95 at synapses and is also diffusely localized in cell bodies, dendrites, and axons. Cdc10 has a punctate distribution in cell bodies and dendrites, with some of the puncta colocalizing with PSD-95. The results support a role for myosin-Va in transport of materials into spines and for septins in the formation or maintenance of spines.

Indexed as

Myosin Heavy ChainsMyosin Type VAmino Acid SequenceAnimalsCell Cycle ProteinsCells, CulturedCloning, MolecularDendritesDNA, ComplementaryHippocampusHydrolysisImmunoblottingImmunohistochemistryIntermediate Filament ProteinsMass SpectrometryMolecular Sequence DataCell Cycle ProteinsDNA, ComplementaryIntermediate Filament ProteinsMyo5a protein, ratMyosin Heavy ChainsMyosin Type VNerve Tissue ProteinsPeptidesTrypsin

Identifiers

PMID10818142
PMCPMC6772646
OpenAlexW2106791925

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.