The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence
Abstract
The 2A region of the foot-and-mouth disease virus (FMDV) polyprotein is only 16 amino acids in length. During synthesis of the FMDV polyprotein a primary proteolytic processing event occurs between the 2A and 2B regions of the polyprotein. The activity responsible for this cleavage is not known but it is thought that either an unidentified virus-encoded proteinase may be responsible, or that 2A acts as a substrate for a host cell proteinase. A series of recombinant FMDV polyproteins has been constructed in which sequences to the N- or C-terminal side of the 2A region have been deleted. Analysis of the processing of these polyproteins shows that a 19 amino acid sequence spanning 2A is sufficient to mediate polyprotein cleavage at a site immediately C-terminal to 2A, whereas deletions extending into the 2A region prevent cleavage.
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A second virus-encoded proteinase involved in proteolytic processing of poliovirus polyprotein
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PROTEOLYTIC PROCESSING OF PICORNAVIRAL POLYPROTEIN
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A second protease of foot-and-mouth disease virus
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Specificity of enzyme-substrate interactions in foot-and-mouth disease virus polyprotein processing
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Self-citationTwo Initiation Sites for Foot-and-Mouth Disease Virus Polyprotein in vivo
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Cited by
Szymczak, A. L., Workman, C. J., Wang, Y., Vignali, K. M., Dilioglou, S., Vanin, E. F., & Vignali, D. A. A. (2004) · Nature Biotechnology · doi:10.1038/nbt957 · Cited by 1,059
ATR prohibits replication catastrophe by preventing global exhaustion of RPA
Toledo, L. I., Altmeyer, M., Rask, M.-B., Lukas, C., Larsen, D. H., Povlsen, L. K., Bekker-Jensen, S., Mailand, N., Bartek, J., & Lukas, J. (2013) · Cell · doi:10.1016/j.cell.2013.10.043 · Cited by 911
Targeted base editing in rice and tomato using a CRISPR-Cas9 cytidine deaminase fusion
Shimatani, Z., Kashojiya, S., Takayama, M., Terada, R., Arazoe, T., Ishii, H., Teramura, H., Yamamoto, T., Komatsu, H., Miura, K., et al. (2017) · Nature Biotechnology · doi:10.1038/nbt.3833 · Cited by 812
Systematic comparison of 2A peptides for cloning multi-genes in a polycistronic vector
Liu, Z., Chen, O., Wall, J. B. J., Zheng, M., Zhou, Y., Wang, L., Ruth Vaseghi, H., Qian, L., & Liu, J. (2017) · Scientific Reports · doi:10.1038/s41598-017-02460-2 · Cited by 745
A nonviral minicircle vector for deriving human iPS cells
Jia, F., Wilson, K. D., Sun, N., Gupta, D. M., Huang, M., Li, Z., Panetta, N. J., Chen, Z. Y., Robbins, R. C., Kay, M. A., et al. (2010) · Nature Methods · doi:10.1038/nmeth.1426 · Cited by 734
Metadata
- Authors
- Ryan, M. D., King, A. M. Q., & Thomas, G. P.
- Venue
- Journal of General Virology
- Publisher
- Microbiology Society
- Published
- 1991-11-01
- Volume
- 72
- Issue
- 11
- Pages
- 2727-2732
- ISSN
- 0022-1317 (ISSN-L)
- 1465-2099
- OpenAlex
- W2080576612
- Cited by
- 477
- References
- 11
- FWCI
- 7.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence. https://app.cochat.ai/papers/10.1099/0022-1317-72-11-2727
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- Ryan, M. D., King, A. M. Q., & Thomas, G. P. (1991). Cleavage of foot-and-mouth disease virus polyprotein is mediated by residues located within a 19 amino acid sequence. Journal of General Virology. https://doi.org/10.1099/0022-1317-72-11-2727
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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