Evidence map›Paper›PMID 22054923›Full record

ReviewCurrent opinion in neurobiology2012

Protein SUMOylation in spine structure and function.

Tim J Craig, Jeremy M Henley

Abstract readReview
In one paragraph

Review in Current opinion in neurobiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  7. Regulation of axon repulsion by MAX-1 SUMOylation and AP-3.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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  10. Commentary: Analysis of SUMO1-conjugation at synapses.Frontiers in cellular neuroscience · 2017
    Article
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  15. Review
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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

2 authors at 1 institution in 1 country.

Tim J CraigMRC Centre for Synaptic Plasticity, School of Biochemistry Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Jeremy M Henley
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0601810Medical Research Council G0601810(80974)Wellcome Trust 083721
6 · The paper itself

Abstract

The active regulation of spine structure and function is of fundamental importance for information storage in the brain. Many proteins involved in spine development and activity-dependent remodelling are potential or validated substrates for modification by the Small Ubiquitin-like Modifier (SUMO). The functional consequences of neuronal protein SUMOylation appear diverse and, in many cases, have not yet been determined. However, for several proteins SUMOylation has been shown to be a key regulator, which has a profound impact on spine dynamics and protein trafficking and function. Here we provide an overview of neuronal SUMOylation and discuss how greater understanding of this relatively recently discovered posttranslational modification will provide insight into the complexity of protein interactions that control synaptic activity and dysfunction.

Indexed as

AnimalsBrainDendritic SpinesModels, BiologicalNeuronsSmall Ubiquitin-Related Modifier ProteinsSumoylationSynapsesSmall Ubiquitin-Related Modifier Proteins

Identifiers

PMID22054923
PMCPMC3379963
OpenAlexW2069181545

What OpenQuestion holds

Textmetadata
LicenceTDM
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.