The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
PeroxiBase: The peroxidase database
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. Analyzing their evolution and their distribution among various phyla could certainly help to elucidate the mystery of their extremely widespread and diversified presence in almost all living organisms. PeroxiBase was originally created for the exhaustive collection of class III peroxidase sequences from plants (Bakalovic, N., Passardi, F., et al., 2006. PeroxiBase: a class III plant peroxidase database. Phytochemistry 67, 534-539). The extension of the class III peroxidase database to all proteins capable to reduce peroxide molecules appears as a necessity. Our database contains haem and non-haem peroxidase sequences originated from annotated or not correctly annotated sequences deposited in the main repositories such as GenBank or UniProt KnowledgeBase. This new database will allow obtaining a global overview of the evolution the protein families and superfamilies capable of peroxidase reaction. In this rapidly growing field, there is a need for continual updates and corrections of the peroxidase protein sequences. Following the lack of unified nomenclature, we also introduced a unique abbreviation for each different family of peroxidases. This paper thus aims to report the evolution of the PeroxiBase database, which is freely accessible through a web server (http://peroxibase.isb-sib.ch). In addition to new categories of peroxidases, new specific tools have been created to facilitate query, classification and submission of peroxidase sequences.
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
Lignin degradation: microorganisms, enzymes involved, genomes analysis and evolution
Janusz, G., Pawlik, A., Sulej, J., Świderska-Burek, U., Jarosz-Wilkołazka, A., & Paszczyński, A. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux049 · Cited by 984
New and classic families of secreted fungal heme peroxidases
Hofrichter, M., Ullrich, R., Pecyna, M. J., Liers, C., & Lundell, T. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2633-0 · Cited by 527
Evolution of Catalases from Bacteria to Humans
Zamocky, M., Furtmüller, P. G., & Obinger, C. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2046 · Cited by 465
Self-citationCytochrome c/cardiolipin relations in mitochondria: a kiss of death
Kagan, V. E., Bayır, H. A., Belikova, N. A., Kapralov, O., Tyurina, Y. Y., Tyurin, V. A., Jiang, J., Stoyanovsky, D. A., Wipf, P., Kochanek, P. M., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.004 · Cited by 444
Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
Mishra, S., & Imlay, J. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.04.014 · Cited by 411
Metadata
- Authors
- Passardi, F., Theiler, G., Zamocky, M., Cosio, C., Rouhier, N., Teixera, F., Margis-Pinheiro, M., Ioannidis, V., Penel, C., Falquet, L., & Dunand, C.
- Venue
- Phytochemistry
- Publisher
- Elsevier BV
- Published
- 2007-06
- Volume
- 68
- Issue
- 12
- Pages
- 1605-1611
- ISSN
- 0031-9422 (ISSN-L)
- OpenAlex
- W2007239014
- Cited by
- 237
- References
- 1
- FWCI
- 5.87
- Type
- journal article
- Language
- en
- Open access
- green
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: The peroxidase database. https://app.cochat.ai/papers/10.1016/j.phytochem.2007.04.005
- The paper
- Passardi, F., Theiler, G., Zamocky, M., Cosio, C., Rouhier, N., Teixera, F., Margis-Pinheiro, M., Ioannidis, V., Penel, C., Falquet, L., & Dunand, C. (2007). PeroxiBase: The peroxidase database. Phytochemistry. https://doi.org/10.1016/j.phytochem.2007.04.005
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.
