The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The AMP deaminase of the mollusk Helix pomatia is an unexpected member of the adenosine deaminase-related growth factor (ADGF) family
Open accessPreprint — published as 10.1371/journal.pone.0286435
Abstract
We report here the first occurrence of an adenosine deaminase-related growth factor (ADGF) that deaminates adenosine 5’ monophosphate (AMP) in preference to adenosine. The ADGFs are a group of secreted deaminases found throughout the animal kingdom that affect the extracellular concentration of adenosine by converting it to inosine. The AMP deaminase studied here was first isolated and biochemically characterized from the roman snail Helix pomatia in 1983. Determination of the amino acid sequence of the AMP deaminase enabled sequence comparisons to protein databases and revealed it as a member of the ADGF family. Cloning and expression of its cDNA in Pichia pastoris allowed the comparison of the biochemical characteristics of the native and recombinant forms of the enzyme and confirmed they correspond to the previously reported activity. Uncharacteristically, the H. pomatia AMP deaminase was determined to be dissimilar to the AMP deaminase family by sequence comparison while demonstrating similarity to the ADGFs despite having AMP as its preferred substrate rather than adenosine.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 29
- 10.1007/s00239-005-0046-y · DOI
- 1984, Non-specific Adenylate Deaminase from Snail Foot Muscle, Adva Exp Med Biol, 165, 457
- 10.1042/bj2150039 · DOI
- 1995, Conversion of adenosine 5’ oligophospho 5’ adenosines into inosine 5” oligophospho 5’ inosines by non-specific adenylate deaminase from the snail Helix pomatia, Biochim Biophys Acta, 1234, 78
- 2001, Mollusk-derived growth factor: cloning and developmental expression in the central nervous system and reproductive tract of Aplysia, Mol Brain Res, 91, 163
- 10.1006/geno.1999.6099 · DOI
- 2014, De Novo sequencing and transcriptome analysis for Tetramorium bicarinatum: a comprehensive venom gland transcriptome analysis from an ant species, BMC Genomics, 15, 987, 10.1186/1471-2164-15-987 · DOI
- 10.1038/nmeth.2227 · DOI · Paper page
- 1947, Differential spectrometry of purine compounds by means of specific enzymes, J Biol Chem, 167, 461, 10.1016/S0021-9258(17)30999-7 · DOI
- 1986, Nonspecific Snail Muscle Adenylate Deaminase: Simplified Purification, Characterization and Use for the Preparation of Deamino Derivatives of NAD, NADH and AMP-P(NH)P, Enzyme, 36, 187, 10.1159/000469291 · DOI
- 10.1074/mcp.M114.046995 · DOI
- 10.1038/nmeth.1701 · DOI · Paper page
- 2022, ColabFold: making protein folding accessible to all, Nat Methods, 19, 679, 10.1038/s41592-022-01488-1 · DOI · Paper page
- 10.1093/NAR/GKAC993 · DOI
- 10.1371/journal.pone.0009490 · DOI · Paper page
- 10.1093/molbev/mst010 · DOI · Paper page
- 2022, SignalP 6.0 predicts all five types of signal peptides using protein language models, Nat Biotechnol, 40, 1023, 10.1038/s41587-021-01156-3 · DOI
- 10.1074/jbc.M109.083527 · DOI
- 10.1038/nsb1203-980 · DOI · Paper page
- 10.1002/jobm.3620280410 · DOI
- 10.1074/jbc.M709279200 · DOI
- 2020, A Literature Review of Gene Function Prediction by Modeling Gene Ontology, Front Genet, 11, 400, 10.3389/fgene.2020.00400 · DOI
- 2018, Secreted bacterial adenosine deaminase is an evolutionary precursor of adenosine deaminase growth factor, Mol Biol Evol, 35, 2851
- 2022, Signalling by extracellular nucleotides in health and disease, Biochim Biophys Acta BBA - Mol Cell Res, 1869, 119237, 10.1016/j.bbamcr.2022.119237 · DOI
- 2018, Purine and purinergic receptors, Brain Neurosci Adv, 2, 239821281881749, 10.1177/2398212818817494 · DOI
- 2011, Cutadapt removes adapter sequences from high-throughput sequencing reads, EMBnet.journal, 17, 10, 10.14806/ej.17.1.200 · DOI · Paper page
- 10.1038/nbt.1883 · DOI
- 10.2144/000113672 · DOI
- 2006, Production of recombinant protein in Pichia pastoris by fermentation, Nat Protoc, 1, 1006, 10.1038/nprot.2006.126 · DOI
Metadata
- Authors
- Tzertzinis, G., Ganatra, M. B., Ruse, C., Taron, C. H., Causey, B., Wang, L., & Schildkraut, I.
- Affiliations
- New England Biolabs (United States) (US)
- Corresponding author
- Schildkraut, Ira
- Venue
- PLoS ONE
- Publisher
- openRxiv
- Published
- 2023-05-17
- Volume
- 18
- Issue
- 7
- Pages
- e0286435-e0286435
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC10358891
- OpenAlex
- W4384925082
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 3 · 2025: 6
- FWCI
- 0.80
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- PLoS ONE (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- New England Biolabs
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Health Sciences › Medicine › Nephrology › Gout, Hyperuricemia, Uric Acid
- Keywords
- AMP deaminase, Helix pomatia, adenosine metabolism, inosine, enzyme substrate specificity, cDNA cloning, recombinant enzyme expression, Pichia pastoris
- MeSH terms
- Adenosine, Adenosine Deaminase, Adenosine Monophosphate, AMP Deaminase, Animals, Mollusca, Intercellular Signaling Peptides and Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
