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“Molecular cloning of a new wheat calreticulin gene TaCRT1 and expression analysis in plant defense responses and abiotic stress resistance”, vol. 10, pp. 3576-3585, 2011.
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http://dx.doi.org/10.1104/pp.105.064386
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http://dx.doi.org/10.1007/BF00020603
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http://dx.doi.org/10.1093/jxb/erm369
PMid:18349049
Jia XY, He LH, Jing RL and Li RZ (2009). Calreticulin: conserved protein and diverse functions in plants. Physiol. Plant. 136: 127-138.
http://dx.doi.org/10.1111/j.1399-3054.2009.01223.x
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http://dx.doi.org/10.1007/s11248-005-5694-6
PMid:16245153
Komatsu S, Yamada E and Furukawa K (2009). Cold stress changes the concanavalin A-positive glycosylation pattern of proteins expressed in the basal parts of rice leaf sheaths. Amino Acids 36: 115-123.
http://dx.doi.org/10.1007/s00726-008-0039-4
PMid:18278531
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http://dx.doi.org/10.1016/0378-1119(95)00537-G
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http://dx.doi.org/10.1046/j.1432-1327.2000.01052.x
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http://dx.doi.org/10.1248/bpb.26.256
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http://dx.doi.org/10.1104/pp.111.2.577
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http://dx.doi.org/10.1016/j.carbpol.2010.04.049
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http://dx.doi.org/10.1104/pp.103.024943
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http://dx.doi.org/10.1093/emboj/18.23.6718
PMid:10581245 PMCid:1171734
Shen W, Yan P, Gao L, Pan X, et al. (2010). Helper component-proteinase (HC-Pro) protein of Papaya ringspot virus interacts with papaya calreticulin. Mol. Plant Pathol. 11: 335-346.
http://dx.doi.org/10.1111/j.1364-3703.2009.00606.x
PMid:20447282