The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides
Abstract
Made and Modified: The polytheonamides are 48-residue toxins derived from marine sponges that include 18 D -amino acids, as well as many other unusual amino acid modifications. Given the complexity, one might guess that these peptides are the product of nonribosomal, peptide synthetase (NRPS). However, Freeman et al. (p. 387 , published online 13 September now show that polytheonamides are produced by a bacterial symbiont using a ribosomal pathway. Six candidate enzymes for the 48 posttranslational modifications were identified and three were functionally validated. Such ribosomal systems could be useful in bioengineering.
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
Sofia, H. J. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.5.1097 · Cited by 1,019
Piel, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222481399 · Cited by 609
Self-citationSchmidt, E. W., Nelson, J. T., Rasko, D. A., Sudek, S., Eisen, J. A., Haygood, M. G., & Ravel, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501424102 · Cited by 567
Frey, P. A., Hegeman, A. D., & Ruzicka, F. J. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701829169 · Cited by 551
Piel, J., Hui, D., Wen, G., Butzke, D., Platzer, M., Fusetani, N., & Matsunaga, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405976101 · Cited by 543
Self-citationBacterial Protection of Beetle-Fungus Mutualism
Scott, J. J., Oh, D.-C., Yuceer, M. C., Klepzig, K. D., Clardy, J., & Currie, C. R. (2008) · Science · doi:10.1126/science.1160423 · Cited by 478
Nonribosomal peptide synthetases: structures and dynamics
Strieker, M., Tanović, A., & Marahiel, M. A. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.01.009 · Cited by 441
Follow the leader: the use of leader peptides to guide natural product biosynthesis
Oman, T. J., & van der Donk, W. A. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.286 · Cited by 408
Nguyen, T., Ishida, K., Jenke-Kodama, H., Dittmann, E., Gurgui, C., Hochmuth, T., Taudien, S., Platzer, M., Hertweck, C., & Piel, J. (2008) · Nature Biotechnology · doi:10.1038/nbt1379 · Cited by 390
Self-citationRibosomal peptide natural products: bridging the ribosomal and nonribosomal worlds
McIntosh, J. A., Donia, M. S., & Schmidt, E. W. (2009) · Natural Product Reports · doi:10.1039/b714132g · Cited by 269
Cited by
The re-emergence of natural products for drug discovery in the genomics era
Harvey, A. L., Edrada-Ebel, R., & Quinn, R. J. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4510 · Cited by 2,572
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20085f · Cited by 2,076
Self-citationBacteriocins—A viable alternative to antibiotics?
Cotter, P. D., Ross, R. P., & Hill, C. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro2937 · Cited by 1,793
Insights into Secondary Metabolism from a Global Analysis of Prokaryotic Biosynthetic Gene Clusters
Cimermancic, P., Medema, M. H., Claesen, J., Kurita, K., Wieland Brown, L. C., Mavrommatis, K., Pati, A., Godfrey, P. A., Koehrsen, M., Clardy, J., et al. (2014) · Cell · doi:10.1016/j.cell.2014.06.034 · Cited by 981
New developments in RiPP discovery, enzymology and engineering
Montalbán-López, M., Scott, T. A., Ramesh, S., Rahman, I. R., van Heel, A. J., Viel, J. H., Bandarian, V., Dittmann, E., Genilloud, O., Goto, Y., et al. (2021) · Natural Product Reports · doi:10.1039/d0np00027b · Cited by 787
Self-citation
Metadata
- Authors
- Freeman, M. F., Gurgui, C., Helf, M. J., Morinaka, B. I., Uria, A. R., Oldham, N. J., Sahl, H.-G., Matsunaga, S., & Piel, J.
- Venue
- Science
- Published
- 2012-10-19
- Volume
- 338
- Issue
- 6105
- Pages
- 387-390
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2045636632
- Cited by
- 347
- References
- 28
- FWCI
- 15.90
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides. https://app.cochat.ai/papers/10.1126/science.1226121
- The paper
- Freeman, M. F., Gurgui, C., Helf, M. J., Morinaka, B. I., Uria, A. R., Oldham, N. J., Sahl, H.-G., Matsunaga, S., & Piel, J. (2012). Metagenome Mining Reveals Polytheonamides as Posttranslationally Modified Ribosomal Peptides. Science. https://doi.org/10.1126/science.1226121
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.