The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism
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Citations
Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,085
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
BIOLOGICAL MEDIATORS OF INSECT IMMUNITY
Gillespie and, J. P., Kanost, M. R., & Trenczek, T. (1997) · Annual Review of Entomology · doi:10.1146/annurev.ento.42.1.611 · Cited by 1,347
Role of the prophenoloxidase-activating system in invertebrate immunity
Söderhäll, K., & Cerenius, L. (1998) · Current Opinion in Immunology · doi:10.1016/s0952-7915(98)80026-5 · Cited by 1,335
Mayer, A. M., & Harel, E. (1979) · Phytochemistry · doi:10.1016/0031-9422(79)80057-6 · Cited by 1,258
Tyrosinase: a comprehensive review of its mechanism
Sánchez-Ferrer, Á., Neptuno Rodríguez-López, J., García-Cánovas, F., & García-Carmona, F. (1995) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)00204-t · Cited by 1,239
Copper-Dioxygen Complexes. Inorganic and Bioinorganic Perspectives
Kitajima, N., & Moro-oka, Y. (1994) · Chemical Reviews · doi:10.1021/cr00027a010 · Cited by 875
Crystal structure of a plant catechol oxidase containing a dicopper center
Klabunde, T., Eicken, C., Sacchettini, J. C., & Krebs, B. (1998) · Nature Structural Biology · doi:10.1038/4193 · Cited by 870
Enzymatic control of pigmentation in mammals
Hearing, V. J., & Tsukamoto, K. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.14.1752358 · Cited by 761
Riley, P. A. (1997) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(97)00013-7 · Cited by 670
Cited by
Durán, N., Rosa, M. A., D’Annibale, A., & Gianfreda, L. (2002) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(02)00214-4 · Cited by 629
Rolff, M., Schottenheim, J., Decker, H., & Tuczek, F. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00202j · Cited by 441
Self-citationFirst Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity
Sendovski, M., Kanteev, M., Ben-Yosef, V. S., Adir, N., & Fishman, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.10.048 · Cited by 299
The molecular basis of innate immunity in the horseshoe crab
Iwanaga, S. (2002) · Current Opinion in Immunology · doi:10.1016/s0952-7915(01)00302-8 · Cited by 256
Respiratory protein–generated reactive oxygen species as an antimicrobial strategy
Jiang, N., Tan, N. S., Ho, B., & Ding, J. L. (2007) · Nature Immunology · doi:10.1038/ni1501 · Cited by 243
Metadata
- Authors
- Decker, H., & Tuczek, F.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2000-08
- Volume
- 25
- Issue
- 8
- Pages
- 392-397
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W1974781567
- Cited by
- 377
- References
- 29
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. https://app.cochat.ai/papers/10.1016/s0968-0004(00)01602-9
- The paper
- Decker, H., & Tuczek, F. (2000). Tyrosinase/catecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends in Biochemical Sciences. https://doi.org/10.1016/s0968-0004(00)01602-9
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.