Evidence map›Paper›PMID 31236626›Full record

ReviewCellular and molecular life sciences : CMLS2019

Functions of 'A disintegrin and metalloproteases (ADAMs)' in the mammalian nervous system.

Hung-En Hsia, Johanna Tüshaus, Tobias Brummer, Yuanpeng Zheng, Simone D Scilabra, Stefan F Lichtenthaler

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

81 citing papers in PubMed, 126 citations in OpenAlex.

  1. Article
  2. ADAM19: biological characteristics and implications in disease pathology and clinical applications.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026
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  17. Journal of diabetes research · 2025
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21 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 4 institutions in 2 countries.

Hung-En HsiaGerman Center for Neurodegenerative Diseases (DZNE), Feodor-Lynen Strasse 17, 81377, Munich, Germany.
Johanna TüshausGerman Center for Neurodegenerative Diseases (DZNE), Feodor-Lynen Strasse 17, 81377, Munich, Germany.
Tobias BrummerGerman Center for Neurodegenerative Diseases (DZNE), Feodor-Lynen Strasse 17, 81377, Munich, Germany.
Yuanpeng ZhengGerman Center for Neurodegenerative Diseases (DZNE), Feodor-Lynen Strasse 17, 81377, Munich, Germany.
Simone D ScilabraGerman Center for Neurodegenerative Diseases (DZNE), Feodor-Lynen Strasse 17, 81377, Munich, Germany.
Stefan F LichtenthalerGerman Center for Neurodegenerative Diseases (DZNE), Feodor-Lynen Strasse 17, 81377, Munich, Germany. stefan.lichtenthaler@dzne.de.
German Center for Neurodegenerative Diseases · DETechnical University of Munich · DEKlinikum rechts der Isar · DERi.MED · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

'A disintegrin and metalloproteases' (ADAMs) are a family of transmembrane proteins with diverse functions in multicellular organisms. About half of the ADAMs are active metalloproteases and cleave numerous cell surface proteins, including growth factors, receptors, cytokines and cell adhesion proteins. The other ADAMs have no catalytic activity and function as adhesion proteins or receptors. Some ADAMs are ubiquitously expressed, others are expressed tissue specifically. This review highlights functions of ADAMs in the mammalian nervous system, including their links to diseases. The non-proteolytic ADAM11, ADAM22 and ADAM23 have key functions in neural development, myelination and synaptic transmission and are linked to epilepsy. Among the proteolytic ADAMs, ADAM10 is the best characterized one due to its substrates Notch and amyloid precursor protein, where cleavage is required for nervous system development or linked to Alzheimer's disease (AD), respectively. Recent work demonstrates that ADAM10 has additional substrates and functions in the nervous system and its substrate selectivity may be regulated by tetraspanins. New roles for other proteolytic ADAMs in the nervous system are also emerging. For example, ADAM8 and ADAM17 are involved in neuroinflammation. ADAM17 additionally regulates neurite outgrowth and myelination and its activity is controlled by iRhoms. ADAM19 and ADAM21 function in regenerative processes upon neuronal injury. Several ADAMs, including ADAM9, ADAM10, ADAM15 and ADAM30, are potential drug targets for AD. Taken together, this review summarizes recent progress concerning substrates and functions of ADAMs in the nervous system and their use as drug targets for neurological and psychiatric diseases.

Indexed as

ADAM ProteinsAnimalsBiological TransportEpilepsyHumansInflammationMyelin SheathNervous SystemPotassium ChannelsProteolysisADAM ProteinsPotassium ChannelsADAMEctodomain sheddingMetalloproteaseNeural developmentNeurological disease

Identifiers

PMID31236626
PMCPMC11105368
OpenAlexW2952734507

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.