@article { ISI:000313165500057,
	title = {Cinnamate 4-hydroxylase (C4H) genes from leucaena leucocephala: a pulp yielding leguminous tree},
	journal = {Molecular Biology Reports},
	volume = {40},
	number = {2},
	year = {2013},
	month = {FEB},
	pages = {1265-1274},
	publisher = {SPRINGER},
	address = {VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS},
	abstract = {<p>Leucaena leucocephala is a leguminous tree species accounting for one-fourth of raw material supplied to paper and pulp industry in India. Cinnamate 4-Hydroxylase (C4H, EC 1.14.13.11) is the second gene of phenylpropanoid pathway and a member of cytochrome P450 family. There is currently intense interest to alter or modify lignin content of L. leucocephala. Three highly similar C4H alleles of LlC4H1 gene were isolated and characterized. The alleles shared more than 98 \% sequence identity at amino acid level to each other. Binding of partial promoter of another C4H gene LlC4H2, to varying amounts of crude nuclear proteins isolated from leaf and stem tissues of L. leucocephala formed two loose and one strong complex, respectively, suggesting that the abundance of proteins that bind with the partial C4H promoter is higher in stem tissue than in leaf tissue. Quantitative Real Time PCR study suggested that among tissues of same age, root tissues had highest level of C4H transcripts. Maximum transcript level was observed in 30 day old root tissue. Among the tissues investigated, C4H activity was highest in 60 day old root tissues. Tissue specific quantitative comparison of lignin from developing seedling stage to 1 year old tree stage indicated that Klason lignin increased in tissues with age.</p>},
	keywords = {Cinnamate 4-Hydroxylase (C4H), Leucaena leucocephala, lignin, Phenylpropanoid},
	issn = {0301-4851},
	doi = {10.1007/s11033-012-2169-8},
	author = {Kumar, Santosh and Omer, Sumita and Patel, Krunal and Khan, Bashir Mohammad}
}
@article { ISI:000367464000006,
	title = {c Squalene synthase gene from medicinal herb bacopa monniera: molecular characterization, differential expression, comparative modeling, and docking studies},
	journal = {Plant Molecular Biology Reporter},
	volume = {33},
	number = {6},
	year = {2015},
	month = {DEC},
	pages = {1675-1685},
	publisher = {SPRINGER},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>The widespread pharmaceutically important triterpenoid saponins are synthesized via isoprenoid pathway. The formation of squalene is the key regulatory point in triterpene biosynthesis, catalyzed by squalene synthase (SQS). The present study deals with the detailed characterization of SQS by molecular, biochemical, and computational means from Bacopa monniera, an immensely important medicinal plant rich in triterpenoid saponin, bacosides. A full-length SQS gene was isolated from B. monniera, characterized as B. monniera squalene synthase (BmSQS) (1242 bp) encoding 414 amino acids. Deduced amino acid sequence of BmSQS showed highly conserved consensus aspartate-rich motifs (DXXXD) and catalytic site residues. Phylogenetic analysis showed that BmSQS belongs to dicot group having closest relationship with Salvia miltiorrhiza. Semiquantitative and real-time PCR studies showed that the BmSQS messenger RNA (mRNA) expression level was higher in vegetative parts (roots) as compared to floral parts. Methyl jasmonate induces the BmSQS mRNA expression in all tissues tested, while salicylic acid, cold, and salt induce much higher expression in roots. Homology modeling and docking simulations of BmSQS showed the pivotal roles of Asp77, Asp81, Asp213, Asp217, and Tyr168 in catalysis.</p>},
	keywords = {Abiotic stress, Bacopa monniera, Comparative modeling and docking, Differential expression, Isoprenoid pathway, Squalene synthase},
	issn = {0735-9640},
	doi = {10.1007/s11105-015-0864-z},
	author = {Vishwakarma, Rishi K. and Patel, Krunal and Sonawane, Prashant and Kumari, Uma and Singh, Somesh and Ruby and Shakeel Abbassi and Agrawal, Dinesh C. and Tsay, Hsin-Sheng and Khan, Bashir Mohammad}
}
