Molecular modeling

Cloning and expression of ethylene receptor ERS1 at various developmental and ripening stages of mango fruit

C. A. Contreras-Vergara, Stephens-Camacho, N. A., Yepiz-Plascencia, G., González-Aguilar, G. A., Arvizu-Flores, A. A., Sanchez-Sanchez, E., and Islas-Osuna, M. A., Cloning and expression of ethylene receptor ERS1 at various developmental and ripening stages of mango fruit, vol. 11, pp. 4081-4092, 2012.

Ethylene induces characteristic ripening reactions in climacteric fruits through its binding to histidine-kinase (HK) receptors, activating the expression of ripening genes. Ethylene receptors have been found in Arabidopsis thaliana (Brassicaceae) and some fruits; number and expression patterns differ among species. In mango, only ethylene receptor ETR1 was known. We cloned ERS1 cDNA from mango, and evaluated the expression of Mi-ERS1 and Mi-ETR1 by qPCR in developmental and ripening stages of this fruit.

Cloning and molecular modeling of Litopenaeus vannamei (Penaeidae) C-type lectin homologs with mutated mannose binding domain-2

F. H. F. Costa, Valença, N. S. M. S., Silva, A. R. B. P., Bezerra, G. A., Cavada, B. S., and Rádis-Baptista, G., Cloning and molecular modeling of Litopenaeus vannamei (Penaeidae) C-type lectin homologs with mutated mannose binding domain-2, vol. 10, pp. 650-664, 2011.

C-type lectins are animal proteins that contain at least one carbohydrate recognition domain (CRD) capable of mediating sugar and calcium binding. Carbohydrate recognition is directly required for some biological functions, including the innate immune response. We cloned two novel C-type lectin (CTL) precursors from the commercial marine shrimp Litopenaeus vannamei. The cloned cDNAs encompass ORFs of 1044 nucleotides and encode highly similar two-domain polypeptides of 347 residues.

Proteinase inhibition using small Bowman-Birk-type structures

J. H. Fernandez, Mello, M. O., Tanaka, A. S., Silva-Filho, M. C., Neshich, G., and Galgaro, L., Proteinase inhibition using small Bowman-Birk-type structures, vol. 6, pp. 846-858, 2007.

Bowman-Birk inhibitors (BBIs) are cysteine-rich and highly cross-linked small proteins that function as specific pseudosubstrates for digestive proteinases. They typically display a "double-headed" structure containing an independent proteinase-binding loop that can bind and inhibit trypsin, chymotrypsin and elastase.

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