The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
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Citations
Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · cited 1×
“A similar topology to that of the b-sheet core is present in other proteins, as detected by comparison of the firefly luciferase molecule with known protein structures using the program DALI [15].”
MethodDo general anaesthetics act by competitive binding to specific receptors?
Franks, N. P., & Lieb, W. R. (1984) · Nature · doi:10.1038/310599a0 · Cited by 572 · cited 1×
“Luciferase has also been studied as a model for possible protein–anaesthetic interactions, being one of the few soluble proteins sensitive to a wide range of general anaesthetics [7].”
BackgroundSelf-citationArtymiuk, P. J., Rice, D. W., Poirrette, A. R., & Willet, P. (1994) · Nature Structural Biology · doi:10.1038/nsb1194-758 · Cited by 83 · cited 1×
“The same active-site architecture has been reported for biotin synthetase [41,42], a protein which activates vitamin H.”
Background
Cited by
Nonribosomal peptide synthetases: structures and dynamics
Strieker, M., Tanović, A., & Marahiel, M. A. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.01.009 · Cited by 441
Applications of bioluminescence in biotechnology and beyond
Syed, A. J., & Anderson, J. C. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01492c · Cited by 341
Firefly luciferase mutants as sensors of proteome stress
Gupta, R., Kasturi, P., Bracher, A., Loew, C., Zheng, M., Villella, A., Garza, D., Hartl, F. U., & Raychaudhuri, S. (2011) · Nature Methods · doi:10.1038/nmeth.1697 · Cited by 219
Modeling Flexible Protein Structure With AlphaFold2 and Crosslinking Mass Spectrometry
(2024) · doi:10.1016/j.mcpro.2024.100724 · Cited by 33
Beyond luciferase-luciferin system: modification, improved imaging and biomedical application
Jiang, Y., Shi, X., Tang, C., & Wang, F. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215045 · Cited by 22
Metadata
- Authors
- Conti, E., Franks, N. P., & Brick, P.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 4
- Issue
- 3
- Pages
- 287-298
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1984216534
- Cited by
- 620
- References
- 5
- FWCI
- 8.04
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
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- CoChat. (2026). Citation check: Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. https://app.cochat.ai/papers/10.1016/s0969-2126(96)00033-0
- The paper
- Conti, E., Franks, N. P., & Brick, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure. https://doi.org/10.1016/s0969-2126(96)00033-0
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.