The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease–helicase
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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
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
Isolation of a cDNA cLone Derived from a Blood-Borne Non-A, Non-B Viral Hepatitis Genome
Choo, Q.-L., Kuo, G., Weiner, A. J., Overby, L. R., Bradley, D. W., & Houghton, M. (1989) · Science · doi:10.1126/science.2523562 · Cited by 6,875
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/8.2.127 · Cited by 5,690
On the size of the active site in proteases. I. Papain
Schechter, I., & Berger, A. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(67)80055-x · Cited by 5,204
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. J. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,739
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Expression and identification of hepatitis C virus polyprotein cleavage products
Grakoui, A., Wychowski, C., Lin, C., Feinstone, S. M., & Rice, C. M. (1993) · Journal of Virology · doi:10.1128/jvi.67.3.1385-1395.1993 · Cited by 898
Hepatitis C: the clinical spectrum of disease.
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Cited by
Helicase structure and mechanism
Caruthers, J. M., & McKay, D. B. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00298-1 · Cited by 566
Kümmerer, B. M., & Rice, C. M. (2002) · Journal of Virology · doi:10.1128/jvi.76.10.4773-4784.2002 · Cited by 301
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development
Luo, D., Vasudevan, S. G., & Lescar, J. (2015) · Antiviral Research · doi:10.1016/j.antiviral.2015.03.014 · Cited by 288
Tunable and reversible drug control of protein production via a self-excising degron
Chung, H. K., Jacobs, C. L., Huo, Y., Yang, J., Krumm, S. A., Plemper, R. K., Tsien, R. Y., & Lin, M. Z. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1869 · Cited by 233
Metadata
- Authors
- Yao, N., Reichert, P., Taremi, S. S., Prosise, W. W., & Weber, P. C.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 1999-11
- Volume
- 7
- Issue
- 11
- Pages
- 1353-1363
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2145130602
- Cited by
- 391
- References
- 32
- FWCI
- 8.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease–helicase. https://app.cochat.ai/papers/10.1016/s0969-2126(00)80025-8
- The paper
- Yao, N., Reichert, P., Taremi, S. S., Prosise, W. W., & Weber, P. C. (1999). Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease–helicase. Structure. https://doi.org/10.1016/s0969-2126(00)80025-8
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.