The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
PeroxiBase: a database with new tools for peroxidase family classification
Open accessAbstract
Peroxidases (EC 1.11.1.x), which are encoded by small or large multigenic families, are involved in several important physiological and developmental processes. They use various peroxides as electron acceptors to catalyse a number of oxidative reactions and are present in almost all living organisms. We have created a peroxidase database (http://peroxibase.isb-sib.ch) that contains all identified peroxidase-encoding sequences (about 6000 sequences in 940 organisms). They are distributed between 11 superfamilies and about 60 subfamilies. All the sequences have been individually annotated and checked. PeroxiBase can be consulted using six major interlink sections 'Classes', 'Organisms', 'Cellular localisations', 'Inducers', 'Repressors' and 'Tissue types'. General documentation on peroxidases and PeroxiBase is accessible in the 'Documents' section containing 'Introduction', 'Class description', 'Publications' and 'Links'. In addition to the database, we have developed a tool to classify peroxidases based on the PROSITE profile methodology. To improve their specificity and to prevent overlaps between closely related subfamilies the profiles were built using a new strategy based on the silencing of residues. This new profile construction method and its discriminatory capacity have been tested and validated using the different peroxidase families and subfamilies present in the database. The peroxidase classification tool called PeroxiScan is accessible at the following address: http://peroxibase.isb-sib.ch/peroxiscan.php.
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
Active site structure and catalytic mechanisms of human peroxidases
Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., & Obinger, C. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.09.017 · Cited by 358
Cited by
Hasanuzzaman, M., Bhuyan, M. H. M. B., Parvin, K., Bhuiyan, T. F., Anee, T. I., Nahar, K., Hossen, M. S., Zulfiqar, F., Alam, M. M., & Fujita, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228695 · Cited by 586
Enzymatic decolorization and degradation of azo dyes – A review
Singh, R. L., Singh, P. K., & Singh, R. P. (2015) · International Biodeterioration & Biodegradation · doi:10.1016/j.ibiod.2015.04.027 · Cited by 543
Chen, C., Shrestha, R., Jia, K., Gao, P. F., Geisbrecht, B. V., Bossmann, S. H., Shi, J., & Li, P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.658807 · Cited by 124
Engineering Biocatalytic Material for the Remediation of Pollutants: A Comprehensive Review
Mishra, B., Varjani, S., Agrawal, D. C., Mandal, S. K., Ngo, H. H., Taherzadeh, M. J., Chang, J.-S., You, S., & Guo, W. (2020) · Environmental Technology & Innovation · doi:10.1016/j.eti.2020.101063 · Cited by 118
Crystal structures of dye‐decolorizing peroxidase with ascorbic acid and 2,6‐dimethoxyphenol
Yoshida, T., Tsuge, H., Hisabori, T., & Sugano, Y. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.10.049 · Cited by 46
Metadata
- Authors
- Koua, D., Cerutti, L., Falquet, L., Sigrist, C. J. A., Theiler, G., Hulo, N., & Dunand, C.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-01-01
- Volume
- 37
- Issue
- Database
- Pages
- D261-D266
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2080037118
- Cited by
- 171
- References
- 1
- FWCI
- 2.98
- Type
- journal article
- Language
- en
- Open access
- gold
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: PeroxiBase: a database with new tools for peroxidase family classification. https://app.cochat.ai/papers/10.1093/nar/gkn680
- The paper
- Koua, D., Cerutti, L., Falquet, L., Sigrist, C. J. A., Theiler, G., Hulo, N., & Dunand, C. (2009). PeroxiBase: a database with new tools for peroxidase family classification. Nucleic Acids Research. https://doi.org/10.1093/nar/gkn680
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.