Evidence map›Paper›PMID 29788979›Full record

ReviewJournal of biomedical science2018

MARCKS and MARCKS-like proteins in development and regeneration.

Mohamed El Amri, Una Fitzgerald, Gerhard Schlosser

Open access · diamondAbstract readReview
In one paragraph

Review in Journal of biomedical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

86 citing papers in PubMed, 167 citations in OpenAlex.

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  18. Allergen-induced activation of epithelial P2YThe Journal of allergy and clinical immunology · 2025
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26 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

3 authors at 1 institution in 1 country.

Mohamed El AmriCentre for Research in Medical Devices (CÚRAM), National University of Ireland, Galway, Biomedical Sciences Building, Newcastle Road, Galway, Ireland.
Una FitzgeraldGalway Neuroscience Centre, School of Natural Sciences, Biomedical Sciences Building, National University of Ireland, Newcastle Road, Galway, Ireland.
Gerhard SchlosserCentre for Research in Medical Devices (CÚRAM), National University of Ireland, Galway, Biomedical Sciences Building, Newcastle Road, Galway, Ireland. gerhard.schlosser@nuigalway.ie.ORCID http://orcid.org/0000-0002-1300-1331
Ollscoil na Gaillimhe – University of Galway · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe Myristoylated Alanine-Rich C-kinase Substrate (MARCKS) and MARCKS-like protein 1 (MARCKSL1) have a wide range of functions, ranging from roles in embryonic development to adult brain plasticity and the inflammatory response. Recently, both proteins have also been identified as important players in regeneration. Upon phosphorylation by protein kinase C (PKC) or calcium-dependent calmodulin-binding, MARCKS and MARCKSL1 translocate from the membrane into the cytosol, modulating cytoskeletal actin dynamics and vesicular trafficking and activating various signal transduction pathways. As a consequence, the two proteins are involved in the regulation of cell migration, secretion, proliferation and differentiation in many different tissues. MAIN BODY: Throughout vertebrate development, MARCKS and MARCKSL1 are widely expressed in tissues derived from all germ layers, with particularly strong expression in the nervous system. They have been implicated in the regulation of gastrulation, myogenesis, brain development, and other developmental processes. Mice carrying loss of function mutations in either Marcks or Marcksl1 genes die shortly after birth due to multiple deficiencies including detrimental neural tube closure defects. In adult vertebrates, MARCKS and MARCKL1 continue to be important for multiple regenerative processes including peripheral nerve, appendage, and tail regeneration, making them promising targets for regenerative medicine.

conclusionThis review briefly summarizes the molecular interactions and cellular functions of MARCKS and MARCKSL1 proteins and outlines their vital roles in development and regeneration.

Indexed as

AnimalsCell MovementIntracellular Signaling Peptides and ProteinsMyristoylated Alanine-Rich C Kinase SubstrateRegenerationVertebratesIntracellular Signaling Peptides and ProteinsMyristoylated Alanine-Rich C Kinase SubstrateCell migrationDevelopmentMARCKSMARCKS-like proteinRegeneration

Identifiers

PMID29788979
PMCPMC5964646
OpenAlexW2805557625

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.