The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Manipulation of Rubisco: the amount, activity, function and regulation
Open accessAbstract
Genetic modification to increase the specificity of Rubisco for CO(2) relative to O(2) and to increase the catalytic rate of Rubisco in crop plants would have great agronomic importance. The availability of three-dimensional structures of Rubisco at atomic resolution and the characterization of site-directed mutants have greatly enhanced the understanding of the catalytic mechanism of Rubisco. Considerable progress has been made in identifying natural variation in the catalytic properties of Rubisco from different species and in developing the tools for introducing both novel and foreign Rubisco genes into plants. The additional complexities of assembling copies of the two distinct polypeptide subunits of Rubisco into a functional holoenzyme in vivo (requiring sufficient expression, post-translational modification, interaction with chaperonins, and interaction with Rubisco activase) remain a major challenge. The consequences of changing the amount of Rubisco present in leaves have been investigated by the use of antisense constructs. The manipulation of genes encoding Rubisco activase has provided a means to investigate the regulation of Rubisco activity.
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Cites
A biochemical model of photosynthetic CO2 assimilation in leaves of C3 species
Farquhar, G. D., von Caemmerer, S., & Berry, J. A. (1980) · Planta · doi:10.1007/bf00386231 · Cited by 8,796
STITT, M., & KRAPP, A. (1999) · Plant, Cell & Environment · doi:10.1046/j.1365-3040.1999.00386.x · Cited by 1,044
Mechanism of Rubisco: the carbamate as general base
Cleland, W. W., Andrews, T. J., Gutteridge, S., Hartman, F. C., & Lorimer, G. H. (1998) · Chemical Reviews · doi:10.1021/cr970010r · Cited by 430
Zhang, N., & Portis, A. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9438 · Cited by 323
Salvucci, M. E., Portis, A. R., & Ogren, W. L. (1985) · Photosynthesis Research · doi:10.1007/bf00037012 · Cited by 243
Cited by
Plant Nitrogen Assimilation and Use Efficiency
Xu, G., Fan, X., & Miller, A. J. (2012) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042811-105532 · Cited by 2,114
Improving photosynthetic efficiency for greater yield.
Zhu, X.-G., Long, S. P., & Ort, D. R. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112206 · Cited by 1,902
Rubisco activity and regulation as targets for crop improvement
Parry, M. A. J., Andralojc, P. J., Scales, J. C., Salvucci, M. E., Carmo-Silva, A. E., Alonso, H., & Whitney, S. M. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ers336 · Cited by 432
Self-citationKurek, I., Chang, T. K., Bertain, S. M., Madrigal, A., Liu, L., Lassner, M. W., & Zhu, G. (2007) · The Plant Cell · doi:10.1105/tpc.107.054171 · Cited by 343
Spectral Signatures of Photosynthesis. I. Review of Earth Organisms
Kiang, N. Y., Siefert, J., Govindjee, & Blankenship, R. E. (2007) · Astrobiology · doi:10.1089/ast.2006.0105 · Cited by 327
“For example, on Earth, the inefficiency of Rubisco (the carbon-fixing enzyme on which all photosynthesis depends and which sometimes is rendered useless for carbon fixation, because it also functions as an oxygenase) is the subject of much lament and agricultural biotechnological research (Parry et al., 2003).”
Metadata
- Authors
- Parry, M. A. J.
- Venue
- Journal of Experimental Botany
- Publisher
- Oxford University Press (OUP)
- Published
- 2003-03-14
- Volume
- 54
- Issue
- 386
- Pages
- 1321-1333
- ISSN
- 0022-0957 (ISSN-L)
- 1460-2431
- OpenAlex
- W2014881533
- Cited by
- 377
- References
- 5
- FWCI
- 5.36
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.