<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jedhe, Ganesh S.</style></author><author><style face="normal" font="default" size="100%">Paul, Debasish</style></author><author><style face="normal" font="default" size="100%">Gonnade, Rajesh G.</style></author><author><style face="normal" font="default" size="100%">Santra, Manas K.</style></author><author><style face="normal" font="default" size="100%">Hamel, Ernest</style></author><author><style face="normal" font="default" size="100%">Tam Luong Nguyen</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Correlation of hydrogen-bonding propensity and anticancer profile of tetrazole-tethered combretastatin analogues</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Colchicine</style></keyword><keyword><style  face="normal" font="default" size="100%">Combretastatin</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystal</style></keyword><keyword><style  face="normal" font="default" size="100%">Tetrazole</style></keyword><keyword><style  face="normal" font="default" size="100%">Tubulin</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2013</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">16</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">23</style></volume><pages><style face="normal" font="default" size="100%">4680-4684</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A series of 1,5-disubstituted tetrazole-tethered combretastatin analogues with extended hydrogen-bond donors at the ortho-positions of the aryl A and B rings were developed and evaluated for their antitubulin and antiproliferative activity. We wanted to test whether intramolecular hydrogen-bonding used as a conformational locking element in these analogues would improve their activity. The correlation of crystal structures with the antitubulin and antiproliferative profiles of the modified analogues suggested that hydrogen-bond-mediated conformational control of the A ring is deleterious to the bioactivity. In contrast, although there was no clear evidence that intramolecular hydrogen bonding to the B ring enhanced activity, we found that increased substitution on the B ring had a positive effect on antitubulin and antiproliferative activity. Among the various analogues synthesized, compounds 5d and 5e, having hydrogen-bonding donor groups at the ortho and meta-positions on the 4-methoxy phenyl B ring, are strong inhibitors of tubulin polymerization and antiproliferative agents having IC50 value in micromolar concentrations. (C) 2013 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">16</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.331
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kale, Sangram S.</style></author><author><style face="normal" font="default" size="100%">Jedhe, Ganesh S.</style></author><author><style face="normal" font="default" size="100%">Meshram, Sachin N.</style></author><author><style face="normal" font="default" size="100%">Santra, Manas K.</style></author><author><style face="normal" font="default" size="100%">Hamel, Ernest</style></author><author><style face="normal" font="default" size="100%">Sanjayan, Gangadhar J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Novel hybrid nocodazole analogues as tubulin polymerization inhibitors and their antiproliferative activity</style></title><secondary-title><style face="normal" font="default" size="100%">Bioorganic &amp; Medicinal Chemistry Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Anticancer</style></keyword><keyword><style  face="normal" font="default" size="100%">Colchicine</style></keyword><keyword><style  face="normal" font="default" size="100%">Nocodazole</style></keyword><keyword><style  face="normal" font="default" size="100%">Tubulin binding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">9</style></number><publisher><style face="normal" font="default" size="100%">PERGAMON-ELSEVIER SCIENCE LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">25</style></volume><pages><style face="normal" font="default" size="100%">1982-1985</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We describe the design, synthesis and SAR profiling of a series of novel combretastatin-nocodazole conjugates as potential anticancer agents. The thiophene ring in the nocodazole moiety was replaced by a substituted phenyl ring from the combretastatin moiety to design novel hybrid analogues. The hydroxyl group at the ortho position in compounds 2, 3 and 4 was used as the conformationally locking tool by anticipated six-membered hydrogen bonding. The bioactivity profiles of all compounds as tubulin polymerization inhibitors and as antiproliferative agents against the A-549 human lung cancer cell line were investigated Compounds 1 and 4 showed mu M IC50 values in both assays. (C) 2015 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">9</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">2.486</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mahajan, Yogesh A.</style></author><author><style face="normal" font="default" size="100%">Shinde, Balkrishna A.</style></author><author><style face="normal" font="default" size="100%">Mulani, Fayaj A.</style></author><author><style face="normal" font="default" size="100%">Gade, Akshay B.</style></author><author><style face="normal" font="default" size="100%">Kasodekar, Amol K.</style></author><author><style face="normal" font="default" size="100%">Thulasiram, H. V.</style></author><author><style face="normal" font="default" size="100%">Kadoo, Narendra Y.</style></author><author><style face="normal" font="default" size="100%">Nikam, Tukaram D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Diversity assessment of Gloriosa superba accessions from Western Ghats of India based on morphological traits, ISSR markers and metabolite content</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Applied Research on Medicinal and Aromatic Plants</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Colchicine</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic diversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Gloriosa superba</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolite diversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Morphological diversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Western Ghats</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">SEP</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">30</style></volume><pages><style face="normal" font="default" size="100%">100388</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Gloriosa superba L. (glory lily) is a medicinally and horticulturally important plant used as a commercial source of the alkaloid colchicine. The Western Ghats in India is mostly unexplored for the morphological, genetic, and metabolite diversity of the species. In the current study, three methodologies were employed to assess the diversity among 50 established accessions of G. superba collected from several locations in the Western Ghats. The morphological analysis revealed that, among the studied traits, seed yield per vine and dry seed weight per 100 seeds for the established accessions were the most diverse traits. The former exhibited a significantly positive correlation with four vegetative and five yield traits. The first three principal components showed nine traits contributing to the variation. Intra-specific molecular variation based on inter simple sequence repeat markers distributed the accessions in three clusters with high polymorphism and low genetic diversity indices. Liquid chromatography high-resolution mass spectrometry analysis revealed significant variation among the screened accessions for colchicine content in tuber and seed tissue. Interestingly, an unexplored tissue, pod shell, was found to contain significantly high colchicine, which could be explored for commercial colchicine extraction. The morphogenetic and metabolite variation revealed by the study would be useful to develop elite varieties to expand the cultivation of glory lily across the country, fulfilling the increasing demand for colchicine and providing remunerative income to the farmers.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	3.945&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Mahajan, Yogesh A.</style></author><author><style face="normal" font="default" size="100%">Shinde, Balkrishna A.</style></author><author><style face="normal" font="default" size="100%">Shirke, Harshad A.</style></author><author><style face="normal" font="default" size="100%">Gandra, Jawahar</style></author><author><style face="normal" font="default" size="100%">Suravajhala, Prashanth</style></author><author><style face="normal" font="default" size="100%">Kishor, P. B. Kavi</style></author><author><style face="normal" font="default" size="100%">Kadoo, Narendra Y.</style></author><author><style face="normal" font="default" size="100%">Nikam, Tukaram D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Unlocking the genetic and biotechnological potential of Gloriosa superba to enhance its alkaloid production</style></title><secondary-title><style face="normal" font="default" size="100%">Industrial Crops and Products</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Biosynthetic pathway</style></keyword><keyword><style  face="normal" font="default" size="100%">Colchicine</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic diversity</style></keyword><keyword><style  face="normal" font="default" size="100%">Glory lily</style></keyword><keyword><style  face="normal" font="default" size="100%">Metabolite elicitation</style></keyword><keyword><style  face="normal" font="default" size="100%">Omics approaches</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">MAY</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">211</style></volume><pages><style face="normal" font="default" size="100%">118144</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Gloriosa superba is a medicinally important plant that produces the pharmaceutically precious colchicine molecule. Colchicine is being used for treating gout, for enhancing the production of interleukin-8 (inhibits human pancreatic cancer) and many other human ailments. Since its seeds and rhizomes (tuberous roots) are the chief sources of colchicine, pharmaceutical industries exploit the natural sources, thus demolishing its habitat. Chemo- and genetic diversity among the G. superba populations exist, but has not been exploited profitably. Scope exists for generating mutants using the chemical mutagens and also via breeding methods to generate superior varieties for commercial cultivation. Innovative methods for breaking seed dormancy and superior colchicine extraction, besides biotechnological interventions are imperative to save the biodiversity and to produce colchicine on a large scale. Biorhizomes produced in vitro hold great promise for biomanufacturing colchicine in bioreactors commercially. Since the biosynthetic pathway of colchicine is now known, isolation of the pathway genes and their heterologous overexpression or the application of synthetic biology methods needs to be explored in future for industrial manufacturing of colchicine. Advances made in the recent past in these fields of colchicine production from G. superba are critically evaluated in this review.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	5.9&lt;/p&gt;
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