The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Purification and species distribution of Rubisco activase.
Open accessAbstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) activase, a soluble chloroplast protein which promotes light-dependent rubisco activation, was partially purified from spinach chloroplasts by ion-exchange and gel-filtration fast protein liquid chromatography. The protein could also be isolated using rate zonal centrifugation in sucrose gradients followed by conventional ion-exchange on DEAE-cellulose. The active enzyme was composed of 44 and 41 kilodalton subunits. Antibodies to the activase polypeptides were produced in tumor-induced mouse ascites fluid and used as probes for activase on immunoblots of soluble proteins from a number of species. One or both of the activase polypeptides were recognized in all higher plant species examined including Arabidopsis thaliana, soybean, kidney bean, pea, tobacco, maize, oat, barley, celery, tomato, pigweed, purslane, dandelion, sorghum, and crabgrass. The polypeptides were not present in a mutant of Arabidopsis which is incapable of activating rubisco in vivo. The activase polypeptides were also detected in cell extracts of the green alga Chlamydomonas reinhardii. Activase activity, which had been demonstrated previously in wild-type Arabidopsis and in spinach, was measured in protoplast extracts of Nicotiana rustica. The results suggest that control of rubisco by activase may be an ubiquitous form of regulation in eucaryotic photosynthetic organisms.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Some species, such as maize and tobacco, do not appear to contain significant amounts of the longer redox-sensitive α-isoform of Rca.
“Some species, such as maize and tobacco, however, do not appear to contain significant amounts of the longer redox-sensitive α-isoform (e.g., Salvucci et al., 1987).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Salvucci et al., 1987
The correlation between decreased Rubisco activation state and electron transport rate did not hold for maize, a species that does not contain significant amounts of the large Rubisco activase isoform.
“This correlation did not hold for maize, a species that does not contain significant amounts of the large Rca isoform (Supplementary Figure S2; Salvucci et al., 1987).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Salvucci et al., 1987
Rubisco activase is composed of small and large isoforms.
“Rca is composed of small and large isoforms (Salvucci et al., 1987).”
From Rubisco and Rubisco Activase Play an Important Role in the Biochemical Limitations of Photosynthesis in Rice, Wheat, and Maize under High Temperature and Water Deficit (2017) · cites this paper as Salvucci et al., 1987
Citations
Cites
COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS
Arnon, D. I. (1949) · PLANT PHYSIOLOGY · doi:10.1104/pp.24.1.1 · Cited by 22,508
Refinement of the Coomassie blue method of protein quantitation
Spector, T. (1978) · Analytical Biochemistry · doi:10.1016/0003-2697(78)90327-5 · Cited by 1,591
Role of Light in the Regulation of Chloroplast Enzymes
Buchanan, B. B. (1980) · Annual Review of Plant Physiology · doi:10.1146/annurev.pp.31.060180.002013 · Cited by 978
RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE-OXYGENASE
Miziorko, H. M., & Lorimer, G. H. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.002451 · Cited by 675
Internal Inorganic Carbon Pool of Chlamydomonas reinhardtii
Badger, M. R., Kaplan, A., & Berry, J. A. (1980) · PLANT PHYSIOLOGY · doi:10.1104/pp.66.3.407 · Cited by 460
[40] Electrophoretic analysis of chloroplast proteins
Chua, N. (1980) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(80)69042-9 · Cited by 345
Salvucci, M. E., Portis, A. R., & Ogren, W. L. (1985) · Photosynthesis Research · doi:10.1007/bf00037012 · Cited by 243
Self-citationInhibition of ribulose bisphosphate carboxylase by substrate ribulose 1,5-bisphosphate.
Jordan, D. B., & Chollet, R. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43982-2 · Cited by 191
Portis, A. R., Salvucci, M. E., & Ogren, W. L. (1986) · PLANT PHYSIOLOGY · doi:10.1104/pp.82.4.967 · Cited by 183
Self-citationHatch, M. D. (1971) · Biochemical Journal · doi:10.1042/bj1250425 · Cited by 174
A Mutant of Arabidopsis thaliana Which Lacks Activation of RuBP Carboxylase In Vivo
Somerville, C. R., Portis, A. R., & Ogren, W. L. (1982) · PLANT PHYSIOLOGY · doi:10.1104/pp.70.2.381 · Cited by 163
Self-citationThe Activation State of Ribulose 1,5-bisphosphate Carboxylase in Maize Leaves in Dark and Light
Usuda, H. (1985) · Plant and Cell Physiology · doi:10.1093/oxfordjournals.pcp.a077047 · Cited by 162
Seemann, J. R., Berry, J. A., Freas, S., & Krump, M. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.8024 · Cited by 145
Jordan, D. B., & Ogren, W. L. (1981) · PLANT PHYSIOLOGY · doi:10.1104/pp.67.2.237 · Cited by 133
Self-citationSalvucci, M. E., Portis, A. R., & Ogren, W. L. (1986) · PLANT PHYSIOLOGY · doi:10.1104/pp.80.3.655 · Cited by 119
Self-citationVu, J. C. V., Allen, L. H., & Bowes, G. (1984) · PLANT PHYSIOLOGY · doi:10.1104/pp.76.3.843 · Cited by 110
Servaites, J. C. (1985) · PLANT PHYSIOLOGY · doi:10.1104/pp.78.4.839 · Cited by 102
Photosynthesis and Activation of Ribulose Bisphosphate Carboxylase in Wheat Seedlings
Perchorowicz, J. T., & Jensen, R. G. (1983) · PLANT PHYSIOLOGY · doi:10.1104/pp.71.4.955 · Cited by 84
Plant carbonic anhydrase. Properties and carbon dioxide hydration kinetics
Pocker, Y., & Ng, J. S. Y. (1973) · Biochemistry · doi:10.1021/bi00749a016 · Cited by 78
Burnell, J. N., & Hatch, M. D. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90302-9 · Cited by 64
A modified method to induce immune polyclonal ascites fluid in BALB/c mice using Sp2/0-Ag14 cells
Lacy, M. J., & Voss, E. W. (1986) · Journal of Immunological Methods · doi:10.1016/0022-1759(86)90527-2 · Cited by 62
Salvucci, M. E., Portis, A. R., & Ogren, W. L. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90066-7 · Cited by 43
Self-citationYokota, A., & Canvin, D. T. (1986) · PLANT PHYSIOLOGY · doi:10.1104/pp.80.2.341 · Cited by 35
Ribulose 1,5-Bisphosphate and Activation of the Carboxylase in the Chloroplast
Sicher, R. C., Hatch, A. L., Stumpf, D. K., & Jensen, R. G. (1981) · PLANT PHYSIOLOGY · doi:10.1104/pp.68.1.252 · Cited by 28
Distribution of the immunoglobulins G, A and M in the prostatic fluid of patients with prostatitis
Gray, S. P., Billings, J., & Blacklock, N. J. (1974) · Clinica Chimica Acta · doi:10.1016/0009-8981(74)90425-2 · Cited by 24
Salvucci, M. E., & Ogren, W. L. (1985) · Planta · doi:10.1007/bf00392230 · Cited by 21
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
R UBISCO : Structure, Regulatory Interactions, and Possibilities for a Better Enzyme
Spreitzer, R. J., & Salvucci, M. E. (2002) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.53.100301.135233 · Cited by 876
Self-citationSunflecks And Photosynthesis In Plant Canopies
Pearcy, R. W. (1990) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.pp.41.060190.002225 · Cited by 689
Rubisco activase – Rubisco's catalytic chaperone
Portis, A. R. (2003) · Photosynthesis Research · doi:10.1023/a:1022458108678 · Cited by 565
Self-citationMechanisms Regulating the Dynamics of Photosynthesis Under Abiotic Stresses
Muhammad, I., Shalmani, A., Ali, M., Yang, Q., Ahmad, H., & Li, F. B. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2020.615942 · Cited by 474
Redox regulation of the Calvin–Benson cycle: something old, something new
Michelet, L., Zaffagnini, M., Morisse, S., Sparla, F., Pérez‐Pérez, M. E., Francia, F., Danon, A., Marchand, C. H., Fermani, S., Trost, P., et al. (2013) · Frontiers in Plant Science · doi:10.3389/fpls.2013.00470 · Cited by 452
Biochemical changes in barley plants after excessive supply of copper and manganese
Demirevska-Kepova, K., Simova‐Stoilova, L., Stoyanova, Z., Hölzer, R., & Feller, U. (2004) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2004.02.004 · Cited by 390
Perdomo, J. A., Capó-Bauçà, S., Carmo-Silva, E., & Galmés, J. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00490 · Cited by 364
“Rca is composed of small and large isoforms (Salvucci et al., 1987).”
BackgroundInfluentialOptimizing R ubisco and its regulation for greater resource use efficiency
Carmo‐Silva, E., Scales, J. C., Madgwick, P. J., & Parry, M. A. J. (2014) · Plant Cell & Environment · doi:10.1111/pce.12425 · Cited by 353
A short history of RubisCO: the rise and fall (?) of Nature's predominant CO2 fixing enzyme
Erb, T. J., & Zarzycki, J. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.07.017 · Cited by 349
Zhang, N., & Portis, A. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.9438 · Cited by 323
Self-citationExceptional Sensitivity of Rubisco Activase to Thermal Denaturation in Vitro and in Vivo
Salvucci, M. E., Osteryoung, K. W., Crafts‐Brandner, S. J., & Vierling, E. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.010357 · Cited by 271
Self-citationInto the Shadows and Back into Sunlight: Photosynthesis in Fluctuating Light
Long, S. P., Taylor, S. H., Burgess, S., Carmo‐Silva, E., Lawson, T., de Souza, A. P., Leonelli, L., & Wang, Y. (2022) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-070221-024745 · Cited by 251
Carmo-Silva, A. E., & Salvucci, M. E. (2013) · Plant Physiology · doi:10.1104/pp.112.213348 · Cited by 225
Self-citationWerneke, J. M., Chatfield, J. M., & Ogren, W. L. (1989) · The Plant Cell · doi:10.1105/tpc.1.8.815 · Cited by 194
Self-citationThe Role of Arabidopsis Rubisco Activase in Jasmonate-Induced Leaf Senescence
Shan, X., Wang, J., Chua, L., Jiang, D., Peng, W., & Xie, D. (2010) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.166595 · Cited by 191
Feng, L., Wang, K., Li, Y., Tan, Y., Kong, J., Li, Y., Li, Y., & Zhu, Y. (2007) · Plant Cell Reports · doi:10.1007/s00299-006-0299-y · Cited by 177
Progression and Specificity of Protein Oxidation in the Life Cycle of Arabidopsis thaliana
Johansson, E., Olsson, O., & Nyström, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402652200 · Cited by 164
Salvucci, M. E., & Ogren, W. L. (1996) · Photosynthesis Research · doi:10.1007/bf00017748 · Cited by 162
Self-citationRegulation of Rubisco activity in crops
Amaral, J., Lobo, A. K. M., & Carmo‐Silva, E. (2023) · New Phytologist · doi:10.1111/nph.19369 · Cited by 149
Crafts‐Brandner, S. J., van de Loo, F. J., & Salvucci, M. E. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.2.439 · Cited by 144
Self-citationvon Caemmerer, S., & Quick, W. P. (2000) · Advances in photosynthesis and respiration · doi:10.1007/0-306-48137-5_4 · Cited by 127
OOSTEN, J. ‐. V., & Besford, R. T. (1995) · Plant Cell & Environment · doi:10.1111/j.1365-3040.1995.tb00185.x · Cited by 125
Pelloux, J., Jolivet, Y., Fontaine, V., Banvoy, J., & Dizengremel, P. (2001) · Plant Cell & Environment · doi:10.1046/j.1365-3040.2001.00665.x · Cited by 124
Questions about the complexity of chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase
Spreitzer, R. J. (1999) · Photosynthesis Research · doi:10.1023/a:1006240202051 · Cited by 121
Rubisco activase: an enzyme with a temperature‐dependent dual function?
Rokka, A., Zhang, L., & Aro, E. (2001) · The Plant Journal · doi:10.1046/j.1365-313x.2001.00981.x · Cited by 118
Law, R. D., & Crafts‐Brandner, S. J. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2225 · Cited by 117
To, K., Suen, D., & Chen, S.-C. G. (1999) · Planta · doi:10.1007/s004250050607 · Cited by 109
Evolutionary Development of Redox Regulation in Chloroplasts
Balsera, M., Uberegui, E., Schürmann, P., & Buchanan, B. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5817 · Cited by 108
On the physiological significance of alternative splicing events in higher plants
Carvalho, R. F., Feijão, C. V., & Duque, P. (2012) · PROTOPLASMA · doi:10.1007/s00709-012-0448-9 · Cited by 105
Wang, D., Li, X., Zhou, Z.-J., Feng, X., Yang, W.-J., & Jiang, D. (2010) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2009.01344.x · Cited by 107
Kaiser, E., Morales, A., Harbinson, J., Heuvelink, E., Prinzenberg, A. E., & Marcelis, L. F. M. (2016) · Scientific Reports · doi:10.1038/srep31252 · Cited by 104
Robinson, S. P., & Portis, A. R. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80473-3 · Cited by 103
Self-citationYamori, W., & von Caemmerer, S. (2009) · Plant Physiology · doi:10.1104/pp.109.146514 · Cited by 98
Law, R. D., Crafts‐Brandner, S. J., & Salvucci, M. E. (2001) · Planta · doi:10.1007/s004250100592 · Cited by 96
Self-citationRubisco activase and wheat productivity under heat-stress conditions
Ristic, Z., Momčilović, I., Bukovnik, U., Prasad, P. V. V., Fu, J., DeRidder, B. P., Elthon, T. E., & Mladenov, N. (2009) · Journal of Experimental Botany · doi:10.1093/jxb/erp241 · Cited by 95
Portis, A. R. (1990) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(90)90211-l · Cited by 92
Self-citationPurification and Assay of Rubisco Activase from Leaves
Robinson, S. P., Streusand, V. J., Chatfield, J. M., & Portis, A. R. (1988) · PLANT PHYSIOLOGY · doi:10.1104/pp.88.4.1008 · Cited by 90
Self-citationWerneke, J. M., Zielinski, R. E., & Ogren, W. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.3.787 · Cited by 90
Self-citationRubisco Assembly in the Chloroplast
Gruber, A. V., & Feiz, L. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00024 · Cited by 87
Eckardt, N. A., & Portis, A. R. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.1.243 · Cited by 86
Self-citationThe activity of Rubisco’s molecular chaperone, Rubisco activase, in leaf extracts.
Carmo-Silva, A. E., & Salvucci, M. E. (2011) · Photosynthesis Research · doi:10.1007/s11120-011-9667-8 · Cited by 86
Self-citationMolecular evolution and genetic engineering of C4 photosynthetic enzymes
Miyao, M. (2003) · Journal of Experimental Botany · doi:10.1093/jxb/erg026 · Cited by 85
The value of mutants unable to carry out photorespiration
Blackwell, R. D., Murray, A. J. S., Lea, P. J., Kendall, A. C., HALL, N. P., Turner, J. C., & Wallsgrove, R. M. (1988) · Photosynthesis Research · doi:10.1007/bf00039491 · Cited by 85
Rundle, S. J., & Zielinski, R. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67702-1 · Cited by 84
Robinson, S. P., & Portis, A. R. (1989) · PLANT PHYSIOLOGY · doi:10.1104/pp.90.3.968 · Cited by 82
Self-citationNuclear Pre-mRna Processing in Higher Plants
Luehrsen, K. R., Taha, S. A., & Walbot, V. (1994) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60252-4 · Cited by 82
RuBisCo activase is present in the pyrenoid of green algae
McKay, R. M. L., Gibbs, S. P., & Vaughn, K. C. (1991) · PROTOPLASMA · doi:10.1007/bf01403899 · Cited by 80
Two isoforms of Rubisco activase in cotton, the products of separate genes not alternative splicing
Salvucci, M. E., van de Loo, F. J., & Stecher, D. S. (2003) · Planta · doi:10.1007/s00425-002-0923-1 · Cited by 80
Self-citationExpression Quantitative Trait Loci Analysis of Two Genes Encoding Rubisco Activase in Soybean
Yin, Z., Meng, F., Song, H., Wang, X., Xu, X., & Yu, D. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.148312 · Cited by 74
Enhancing crop yield by using Rubisco activase to improve photosynthesis under elevated temperatures
Wijewardene, I., Shen, G., & Zhang, H. (2021) · Stress Biology · doi:10.1007/s44154-021-00002-5 · Cited by 70
Zhang, N., Schürmann, P., & Portis, A. R. (2001) · Photosynthesis Research · doi:10.1023/a:1011845506196 · Cited by 70
Self-citationSalvucci, M. E. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90467-b · Cited by 69
Self-citationRegulation of Rubisco activity in vivo
Salvucci, M. E. (1989) · Physiologia Plantarum · doi:10.1111/j.1399-3054.1989.tb05993.x · Cited by 66
Self-citationSalvucci, M. E., & Anderson, J. C. (1987) · PLANT PHYSIOLOGY · doi:10.1104/pp.85.1.66 · Cited by 66
Self-citationEffect of activase level and isoform on the thermotolerance of photosynthesis in Arabidopsis.
Salvucci, M. E., DeRidder, B. P., & Portis, A. R. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erl140 · Cited by 65
Self-citationSeemann, J. R., Kobza, J., & Moore, B. D. (1990) · Photosynthesis Research · doi:10.1007/bf00035005 · Cited by 58
Kobza, J., & Seemann, J. R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.3815 · Cited by 56
Sage, R. F., & Seemann, J. R. (1993) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.1.21 · Cited by 55
Evolution of Rubisco activase gene in plants
Nagarajan, R., & Gill, K. S. (2017) · Plant Molecular Biology · doi:10.1007/s11103-017-0680-y · Cited by 54
MacIntyre, H. L., Sharkey, T. D., & Geider, R. J. (1997) · Photosynthesis Research · doi:10.1023/a:1005755621305 · Cited by 51
Yin, Z., Zhang, Z., Deng, D., Chao, M., Gao, Q., Wang, Y., Yang, Z., Bian, Y., Hao, D., & Xu, C. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.230854 · Cited by 50
von Caemmerer, S., Hendrickson, L., Quinn, V., Vella, N. G. F., Millgate, A. G., & Furbank, R. T. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.056077 · Cited by 50
Developmental and circadian pattern of rubisco activase mRNA accumulation in apple plants
Watillon, B., Kettmann, R., Boxus, P., & Burny, A. (1993) · Plant Molecular Biology · doi:10.1007/bf00019298 · Cited by 50
Chen, J., Wang, P., Mi, H., Chen, G., & Xu, D.-Q. (2010) · Journal of Experimental Botany · doi:10.1093/jxb/erq122 · Cited by 50
Limiting Factors in Photosynthesis
Arulanantham, A. R., Rao, I. M., & Terry, N. (1990) · PLANT PHYSIOLOGY · doi:10.1104/pp.93.4.1466 · Cited by 49
Antisense RNA inhibition of Rubisco activase expression
Jiang, C., Quick, W. P., Alred, R., Kliebenstein, D. J., & Rodermel, S. R. (1994) · The Plant Journal · doi:10.1046/j.1365-313x.1994.5060787.x · Cited by 49
Coordinate Expression of Rubisco Activase and Rubisco during Barley Leaf Cell Development
Zielinski, R. E., Werneke, J. M., & Jenkins, M. E. (1989) · PLANT PHYSIOLOGY · doi:10.1104/pp.90.2.516 · Cited by 49
Self-citationRubisco in planta kcat is regulated in balance with photosynthetic electron transport
Eichelmann, H. Y., Talts, E., Oja, V., Padu, E., & Laisk, A. (2009) · Journal of Experimental Botany · doi:10.1093/jxb/erp242 · Cited by 44
C4 Photosynthesis: Mechanism and Regulation
Furbank, R. T., Hatch, M. D., & Jenkins, C. L. D. (2000) · Advances in photosynthesis and respiration · doi:10.1007/0-306-48137-5_18 · Cited by 43
Rundle, S. J., & Zielinski, R. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98756-9 · Cited by 40
Chao, M., Yin, Z., Hao, D., Zhang, J., Song, H., Ning, A., Xu, X., & Yu, D. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ert346 · Cited by 39
Control of Metabolism and Development in Higher Plant Plastids
Emes, M. J., & Tobin, A. K. (1993) · International review of cytology · doi:10.1016/s0074-7696(08)60427-1 · Cited by 38
Keown, J. R., & Pearce, F. G. (2014) · Biochemical Journal · doi:10.1042/bj20140676 · Cited by 37
Orozco, B. M., McClung, C. R., Werneke, J. M., & Ogren, W. L. (1993) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.1.227 · Cited by 36
Self-citationKim, S. Y., Slattery, R. A., & Ort, D. R. (2020) · GCB Bioenergy · doi:10.1111/gcbb.12768 · Cited by 36
Lilley, R. M., & Portis, A. R. (1997) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.2.605 · Cited by 35
Self-citationHeat sensitivity of Rubisco, Rubisco activase and Rubisco binding protein in higher plants
Demirevska-Kepova, K., & Feller, U. (2004) · Acta Physiologiae Plantarum · doi:10.1007/s11738-004-0050-7 · Cited by 34
The relative abundance of wheat Rubisco activase isoforms is post-transcriptionally regulated
Perdomo, J. A., Büchner, P., & Carmo‐Silva, E. (2021) · Photosynthesis Research · doi:10.1007/s11120-021-00830-6 · Cited by 35
Sharkey, T. D. (2022) · Journal of Experimental Botany · doi:10.1093/jxb/erac254 · Cited by 36
Molecular Regulation and Evolution of Redox Homeostasis in Photosynthetic Machinery
Riaz, A., Deng, F., Chen, G. J., Jiang, W. J., Zheng, Q., Riaz, B., Mak, M., Zeng, F., & Chen, Z. (2022) · Antioxidants · doi:10.3390/antiox11112085 · Cited by 32
Liu, C., Hong, F., Wu, K., Ma, H.-B., Zhang, X., Hong, C.-J., Wu, C., Gao, F., Yang, F., Zheng, L., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.105 · Cited by 32
Rubisco activase chaperone activity is regulated by a post-translational mechanism in maize leaves
Vargas‐Suárez, M. (2004) · Journal of Experimental Botany · doi:10.1093/jxb/erh268 · Cited by 32
The effects of Rubisco activase on C4 photosynthesis and metabolism at high temperature
Hendrickson, L., Sharwood, R. E., Ludwig, M. L., Whitney, S. M., Badger, M. R., & von Caemmerer, S. (2007) · Journal of Experimental Botany · doi:10.1093/jxb/erm373 · Cited by 31
Steinberg, N. A., & Meeks, J. C. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.11.6227-6233.1989 · Cited by 31
Werneke, J. M., Chatfield, J. M., & Ogren, W. L. (1988) · PLANT PHYSIOLOGY · doi:10.1104/pp.87.4.917 · Cited by 31
Self-citationSalvucci, M. E., Holbrook, G. P., Anderson, J. C., & Bowes, G. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80730-0 · Cited by 31
Self-citationImproving photosynthetic efficiency in fluctuating light to enhance yield of C3 and C4 crops
Wang, Y. (2024) · Crop and Environment · doi:10.1016/j.crope.2024.06.003 · Cited by 31
Characterization of the Photosynthetic Apparatus from the Marine Dinoflagellate Gonyaulax polyedra
Knoetzel, J., & Rensing, L. (1990) · Journal of Plant Physiology · doi:10.1016/s0176-1617(11)80049-0 · Cited by 28
Gontero, B., & Salvucci, M. E. (2014) · Aquatic Botany · doi:10.1016/j.aquabot.2014.05.011 · Cited by 26
Self-citationActivation of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase (Rubisco) by Rubisco Activase
Lilley, R. M., & Portis, A. R. (1990) · PLANT PHYSIOLOGY · doi:10.1104/pp.94.1.245 · Cited by 24
Self-citationLi, L. A., & Tabita, F. R. (1994) · Journal of Bacteriology · doi:10.1128/jb.176.21.6697-6706.1994 · Cited by 24
Wang, D., Lu, Q., Li, X. F., Jiang, Q. S., Wu, J., & Jiang, D. A. (2009) · Photosynthetica · doi:10.1007/s11099-009-0089-1 · Cited by 23
Symbiotic Root Nodules of the Actinorhizal PlantDatisca glomerata Express Rubisco Activase mRNA1
Okubara, P. A., Pawlowski, K., Murphy, T. M., & Berry, A. M. (1999) · PLANT PHYSIOLOGY · doi:10.1104/pp.120.2.411 · Cited by 23
Klein, R. R., & Salvucci, M. E. (1995) · Photosynthesis Research · doi:10.1007/bf00029934 · Cited by 21
Self-citationChanges in Rubisco activase gene expression and polypeptide content in Brachypodium distachyon
Bayramov, S., & Guliyev, N. (2014) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2014.01.013 · Cited by 19
Purification of Rubisco Activase from Leaves or after Expression in Escherichia coli
Barta, C. É., Carmo‐Silva, E., & Salvucci, M. E. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-925-3_28 · Cited by 19
Self-citationJurczyk, B., Pociecha, E., Grzesiak, M. T., Kalita, K., & Rapacz, M. (2016) · Journal of Plant Physiology · doi:10.1016/j.jplph.2016.03.021 · Cited by 18
Jean, N., Dumont, E., Herzi, F., Balliau, T., Laabir, M., Masseret, E., & Mounier, S. J. L. (2017) · Aquatic Toxicology · doi:10.1016/j.aquatox.2017.04.011 · Cited by 16
Cloning and characterization of the Rubisco activase gene from Ipomoea batatas (L.) Lam
Xu, K., He, B., Zhou, S., Li, Y., & Zhang, Y. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9510-x · Cited by 16
Characterization of the Photosynthetic Apparatus from the Marine Dinoflagellate Gonyaulax polyedra
Knoetzel, J., & Rensing, L. (1990) · Journal of Plant Physiology · doi:10.1016/s0176-1617(11)80050-7 · Cited by 16
Metadata
- Authors
- Salvucci, M. E., Werneke, J. M., Ogren, W. L., & Portis, A. R.
- Affiliations
- Agricultural Research Service (US)
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 1987-07-01
- Volume
- 84
- Issue
- 3
- Pages
- 930-936
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- PMC
- PMC1056697
- OpenAlex
- W2068760724
- Cited by
- 152
- References
- 26
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 6 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 1 · 2018: 2 · 2017: 9 · 2016: 4 · 2015: 1 · 2014: 7 · 2013: 4 · 2012: 1
- FWCI
- 3.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- PLANT PHYSIOLOGY (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Keywords
- Rubisco activase, Rubisco activation, chloroplast proteins, spinach, protein purification, species distribution, antibody probes, Arabidopsis thaliana, Chlamydomonas reinhardtii, Nicotiana rustica, photosynthesis regulation, higher plants, green algae
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
