The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Crystal structure of horseradish peroxidase C at 2.15 Å resolution
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Citations
Cites
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Solvent content of protein crystals
Matthews, B. W. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90205-2 · Cited by 7,961
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,953
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424
Accurate bond and angle parameters for X-ray protein structure refinement
Engh, R. A., & Huber, R. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767391001071 · Cited by 2,489
SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
Evans, S. V. (1993) · Journal of Molecular Graphics · doi:10.1016/0263-7855(93)87009-t · Cited by 1,279
ALSCRIPT: a tool to format multiple sequence alignments
Barton, G. J. (1993) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/6.1.37 · Cited by 1,136
The stereochemistry of peroxidase catalysis.
Poulos, T. L., & Kraut, J. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70630-9 · Cited by 685
Self-citationRussell, R. B., & Barton, G. J. (1992) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340140216 · Cited by 647
Cited by
Horseradish peroxidase: a modern view of a classic enzyme
Veitch, N. C. (2004) · Phytochemistry · doi:10.1016/j.phytochem.2003.10.022 · Cited by 1,379
Ruiz‐Dueñas, F. J., & Martínez, Á. T. (2009) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2008.00078.x · Cited by 561
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
Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana
Welinder, K. G., Justesen, A. F., Kjærsgård, I. V. H., Jensen, R. B., Rasmussen, S. K., Jespersen, H. M., & Duroux, L. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03311.x · Cited by 277
Horseradish peroxidase: a valuable tool in biotechnology
Azevedo, A. M., Martins, V. C., Prazeres, D. M. F., Vojinović, V., Cabral, J. M. S., & Fonseca, L. P. (2003) · Biotechnology Annual Review · doi:10.1016/s1387-2656(03)09003-3 · Cited by 243
Metadata
- Authors
- Gajhede, M., Schuller, D. J., Henriksen, A., Smith, A. T., & Poulos, T. L.
- Venue
- Nature Structural Biology
- Published
- 1997-12
- Volume
- 4
- Issue
- 12
- Pages
- 1032-1038
- ISSN
- 1072-8368 (ISSN-L)
- OpenAlex
- W2165898505
- Cited by
- 710
- References
- 40
- FWCI
- 27.12
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Crystal structure of horseradish peroxidase C at 2.15 Å resolution. https://app.cochat.ai/papers/10.1038/nsb1297-1032
- The paper
- Gajhede, M., Schuller, D. J., Henriksen, A., Smith, A. T., & Poulos, T. L. (1997). Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nature Structural Biology. https://doi.org/10.1038/nsb1297-1032
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.