The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms 1 1Edited by J. Thornton
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Cites
Ryckaert, J.-P., Ciccotti, G., & Berendsen, H. J. C. (1977) · Journal of Computational Physics · doi:10.1016/0021-9991(77)90098-5 · Cited by 21,239
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
Cytochrome P-450: Structure, Mechanism, and Biochemistry
de Montellano, O., & Paul, R. (1986) · Medical Entomology and Zoology · Cited by 2,663
Goodford, P. J. (1985) · Journal of Medicinal Chemistry · doi:10.1021/jm00145a002 · Cited by 2,634
High-resolution crystal structure of cytochrome P450cam
Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90190-2 · Cited by 1,411
New spherical‐cutoff methods for long‐range forces in macromolecular simulation
Steinbach, P. J., & Brooks, B. R. (1994) · Journal of Computational Chemistry · doi:10.1002/jcc.540150702 · Cited by 1,147
Ligand Binding: Molecular Mechanics Calculation of the Streptavidin-Biotin Rupture Force
Grubmüller, H., Heymann, B., & Tavan, P. (1996) · Science · doi:10.1126/science.271.5251.997 · Cited by 934
Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's
Ravichandran, K. G., Boddupalli, S. S., Hasermann, C. A., Peterson, J. A., & Deisenhofer, J. (1993) · Science · doi:10.1126/science.8342039 · Cited by 877
Molecular dynamics study of unbinding of the avidin-biotin complex
Izrailev, S., Stepaniants, S., Balsera, M., Oono, Y., & Schulten, K. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78804-0 · Cited by 787
Mammalian Microsomal Cytochrome P450 Monooxygenase
Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80408-6 · Cited by 696
Cited by
Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development
Salo-Ahen, O. M. H., Alanko, I., Bhadane, R., Bonvin, A. M. J. J., Honorato, R. V., Hossain, S., Juffer, A. H., Kabedev, A., Lahtela-Kakkonen, M., Larsen, A. S., et al. (2020) · Processes · doi:10.3390/pr9010071 · Cited by 659
Li, X., Baudry, J., Berenbaum, M. R., & Schuler, M. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308691101 · Cited by 299
G-protein coupled receptors: advances in simulation and drug discovery
Miao, Y., & McCammon, J. A. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.06.008 · Cited by 93
Metadata
- Authors
- Lüdemann, S. K., Lounnas, V., & Wade, R. C.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2000-11
- Volume
- 303
- Issue
- 5
- Pages
- 797-811
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2091392856
- Cited by
- 326
- References
- 27
- Type
- book review
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms 1 1Edited by J. Thornton. https://app.cochat.ai/papers/10.1006/jmbi.2000.4154
- The paper
- Lüdemann, S. K., Lounnas, V., & Wade, R. C. (2000). How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms 1 1Edited by J. Thornton. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.2000.4154
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.
