Evidence map›Paper›PMID 39497138›Full record

ArticleCell communication and signaling : CCS2024

Regulation of ADAM10 activity through microdomain-dependent intracellular calcium changes.

Federico Guillermo Gharzia, Ahmad Aljohmani, Andreas Beck, Stephan E Philipp, Daniela Yildiz

Abstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
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  6. Review
  7. Review
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

5 authors.

Federico Guillermo GharziaMolecular Pharmacology, PZMS, Saarland University, Campus Homburg Building 46, 66421, Homburg, Germany.
Ahmad AljohmaniMolecular Pharmacology, PZMS, Saarland University, Campus Homburg Building 46, 66421, Homburg, Germany.
Andreas BeckInstitute of Experimental and Clinical Pharmacology and Toxicology, PZMS, Saarland University, Homburg, Germany.
Stephan E PhilippInstitute of Experimental and Clinical Pharmacology and Toxicology, PZMS, Saarland University, Homburg, Germany.
Daniela YildizMolecular Pharmacology, PZMS, Saarland University, Campus Homburg Building 46, 66421, Homburg, Germany. daniela.yildiz@uks.eu.ORCID 0000-0002-9702-8581

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A disintegrin and metalloproteinases (ADAMs) are transmembrane proteases that cleave other proteins close to the surface in a process called shedding. The prominent member ADAM10 has been linked to several pathologies such as Alzheimer's disease, bacterial infection, cancer development and metastasis. Although the regulation of the ADAM10 activity by calcium influx and calmodulin inhibition has been reported, the spatiotemporal regulation of Ca

Indexed as

ADAM10 ProteinCalciumTrifluoperazineA549 CellsAmyloid Precursor Protein SecretasesCalmodulinDipeptidesHumansHydroxamic AcidsIonomycinMembrane Proteins3-(formylhydroxyamino)-2-(3-phenyl-1-propyl)butanoic acid (2,2-dimethyl-1-methylcarbamoyl-1-propyl)amideADAM10 ProteinADAM10 protein, humanAmyloid Precursor Protein SecretasesCalciumCalmodulinDipeptidesHydroxamic AcidsIonomycinMembrane ProteinsTrifluoperazineCalciumExosomesJunction and adhesion moleculesMetalloproteinasesProteolysisTransient receptor potential channels

Identifiers

PMID39497138
PMCPMC11533308

What OpenQuestion holds

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Registered trials

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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.