ReviewPharmacy world & science : PWS1994
Molecular biology of AMP deaminase deficiency.
Review in Pharmacy world & science : PWS, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Does theGenes · 2026Article
- Structural basis for the substrate specificity of Helix pomatia AMP deaminase and a chimeric ADGF adenosine deaminase.The Journal of biological chemistry · 2025Article
- AMPD3 promotes doxorubicin-induced cardiomyopathy through HSP90α-mediated ferroptosis.iScience · 2024Article
- Inborn Errors of Purine Salvage and Catabolism.Metabolites · 2023Review
- Hidden Pool of Cardiac Adenine Nucleotides That Controls Adenosine Production.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Article
- Ovarian cancer detection by DNA methylation in cervical scrapings.Clinical epigenetics · 2019Article
- Structure ofRNA biology · 2019Article
- A mutation in Ampd2 is associated with nephrotic syndrome and hypercholesterolemia in mice.Lipids in health and disease · 2014Article
- Counteracting roles of AMP deaminase and AMP kinase in the development of fatty liver.PloS one · 2012Article
- Phylogenetic analysis reveals a novel protein family closely related to adenosine deaminase.Journal of molecular evolution · 2005Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In man, there are at least four isoforms of adenosine monophosphate deaminase (AMPD): myoadenylate deaminase in skeletal muscle, the L isoform in liver, and the E1 and E2 isoforms in erythrocytes. Myoadenylate deaminase is encoded by the AMPD1 gene located on chromosome 1 p13-p21, the L isoform by the AMPD2 gene, and both isoforms in erythrocytes by the AMPD3 gene. Myoadenylate deaminase deficiency is found in 2-3% of all muscle biopsies. The inborn type of myoadenylate deaminase deficiency is caused by a single mutant allele harbouring two mutations: C34-->T (Gln-->Stop) and C143-->T (Pro-48-->Leu). Population studies revealed a frequency of the mutant allele of 0.12 in Caucasian Americans and Germans. The C34-->T mutation is located in exon 2, which is alternatively spliced in part of the AMPD1 transcript in human muscle. Since the second mutation does not affect enzyme function, alternatively spliced mRNA encodes a catalytically active enzyme. Only one patient with a disorder linked to liver AMPD has been described so far. In this patient the decreased inhibition of this enzyme by GTP resulted in uric acid overproduction and gout. A complete lack of erythroyte AMPD activity is found in asymptomatic subjects. The molecular basis of both disorders is not yet known.
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Registered trials
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.