Evidence map›Paper›PMID 27965136›Full record

ReviewNeuroscience research2017

Activity-dependent proteolytic cleavage of cell adhesion molecules regulates excitatory synaptic development and function.

Sivapratha Nagappan-Chettiar, Erin M Johnson-Venkatesh, Hisashi Umemori

Open access · greenAbstract readReview
In one paragraph

Review in Neuroscience research, 2017. 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
1.3field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. The intracellular domain of the epilepsy protein PCDH19 regulates spine density in cortical neurons in vivo viaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
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  3. Activity-Dependent Synapse Refinement: From Mechanisms to Molecules.The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry · 2024
    Review
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  11. Neuropsin in mental health.The journal of physiological sciences : JPS · 2020
    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

3 authors at 2 institutions in 1 country.

Sivapratha Nagappan-ChettiarDepartment of Neurology, F.M. Kirby Neurobiology Center, Boston Children's Hospital, Harvard Medical School, Boston, MA 02115, USA; Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA.
Erin M Johnson-VenkateshDepartment of Neurology, F.M. Kirby Neurobiology Center, Boston Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.
Hisashi UmemoriDepartment of Neurology, F.M. Kirby Neurobiology Center, Boston Children's Hospital, Harvard Medical School, Boston, MA 02115, USA; Program in Neuroscience, Harvard Medical School, Boston, MA 02115, USA. Electronic address: hisashi.umemori@childrens.harvard.edu.
Boston Children's Hospital · USHarvard University · US

Funding

Mouse Neurodevelopmental Behavior CoreU54HD090255 · NICHD · BOSTON CHILDREN'S HOSPITAL · PI POMEROY, SCOTT LOREN · 2016 to 2020
$5.2M
Mechanisms of Activity-dependent Microglia-neuron Interactions in Development and DiseaseRF1NS092578 · NINDS · BOSTON CHILDREN'S HOSPITAL · PI STEVENS, BETH ANN, UMEMORI, HISASHI · 2021 to 2023
$3.5M
Investigating CD47-SIRPa as novel protective signals during CNS synaptic pruningR01NS092578 · NINDS · BOSTON CHILDREN'S HOSPITAL · PI STEVENS, BETH ANN, UMEMORI, HISASHI · 2015 to 2019
$2.9M
NICHD NIH HHS U54 HD090255NINDS NIH HHS R01 NS092578NINDS NIH HHS RF1 NS092578
6 · The paper itself

Abstract

Activity-dependent remodeling of neuronal connections is critical to nervous system development and function. These processes rely on the ability of synapses to detect neuronal activity and translate it into the appropriate molecular signals. One way to convert neuronal activity into downstream signaling is the proteolytic cleavage of cell adhesion molecules (CAMs). Here we review studies demonstrating the mechanisms by which proteolytic processing of CAMs direct the structural and functional remodeling of excitatory glutamatergic synapses during development and plasticity. Specifically, we examine how extracellular proteolytic cleavage of CAMs switches on or off molecular signals to 1) permit, drive, or restrict synaptic maturation during development and 2) strengthen or weaken synapses during adult plasticity. We will also examine emerging studies linking improper activity-dependent proteolytic processing of CAMs to neurological disorders such as schizophrenia, brain tumors, and Alzheimer's disease. Together these findings suggest that the regulation of activity-dependent proteolytic cleavage of CAMs is vital to proper brain development and lifelong function.

Indexed as

Alzheimer DiseaseAnimalsBrainBrain NeoplasmsCell Adhesion MoleculesHumansNeuronal PlasticityNeuronsProteolysisSchizophreniaSynapsesCell Adhesion MoleculesCell adhesion moleculesNeuronal activityProteolytic cleavageSynaptic developmentSynaptic plasticity

Identifiers

PMID27965136
PMCPMC5376514
OpenAlexW2560695034

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.