<?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%">Pathan, Ejaj K.</style></author><author><style face="normal" font="default" size="100%">Ghormade, Vandana</style></author><author><style face="normal" font="default" size="100%">Panwar, Sneh Lata</style></author><author><style face="normal" font="default" size="100%">Prasad, Rajendra</style></author><author><style face="normal" font="default" size="100%">Deshpande, Mukund V.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Molecular studies of NAD- and NADP-glutamate dehydrogenases decipher the conundrum of yeast-hypha dimorphism in zygomycete Benjaminiella poitrasii</style></title><secondary-title><style face="normal" font="default" size="100%">Fems Yeast Research</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Benjaminiella poitrasii</style></keyword><keyword><style  face="normal" font="default" size="100%">Candida glabrata</style></keyword><keyword><style  face="normal" font="default" size="100%">differential gene expression</style></keyword><keyword><style  face="normal" font="default" size="100%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">monomorphic mutant</style></keyword><keyword><style  face="normal" font="default" size="100%">NAD/NADP-glutamate dehydrogenase</style></keyword><keyword><style  face="normal" font="default" size="100%">yeast-hypha transition</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2019</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">19</style></volume><pages><style face="normal" font="default" size="100%">foz074</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Benjaminiella poitrasii, a zygomycete, shows glucose- and temperature-dependent yeast (Y)-hypha (H) dimorphic transition. Earlier, we reported the biochemical correlation of relative proportion of NAD- and NADP-glutamate dehydrogenases (GDHs) with Y-H transition. Further, we observed the presence of one NAD-GDH and two form-specific NADP-GDH isoenzymes in B. poitrasii. However, molecular studies are necessary to elucidate the explicit role of GDHs in regulating Y-H reversible transition. Here, we report the isolation and characterization of one NAD (BpNADGDH, 2.643 kb) and two separate genes, BpNADPGDH I (Y-form specific, 1.365 kb) and BpNADPGDH II (H-form specific, 1.368 kb) coding for NADP-GDH isoenzymes in B. poitrasii. The transcriptional profiling during Y-H transition showed higher BpNADPGDH I expression in Y cells while expression of BpNADPGDH II was higher in H cells. Moreover, the yeast-form monomorphic mutant (Y-5) did not show BpNADPGDH II expression under normal dimorphism triggering conditions. Transformation with H-form specific BpNADPGDH II induced the germ tube formation in Y-5, which confirmed the cause-effect relationship between BpNADPGDH genes and morphological outcome in B. poitrasii. Interestingly, expression of H-form specific BpNADPGDH II also induced germ tube formation in human pathogenic, non-dimorphic yeast Candida glabrata, which further corroborated our findings.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><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;3.193&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%">Pathan, Ejaj K.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, Anand M.</style></author><author><style face="normal" font="default" size="100%">Prasanna, Nallaballe V. L.</style></author><author><style face="normal" font="default" size="100%">Ramana, V, Chepuri</style></author><author><style face="normal" font="default" size="100%">Deshpande, V, Mukund</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">NADP-dependent glutamate dehydrogenases in a dimorphic zygomycete Benjaminiella poitrasii: purification, characterization and their evaluation as an antifungal drug target</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica Et Biophysica Acta-General Subjects</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Antifungal compound</style></keyword><keyword><style  face="normal" font="default" size="100%">Benjaminiella poitrasii</style></keyword><keyword><style  face="normal" font="default" size="100%">Candida albicans</style></keyword><keyword><style  face="normal" font="default" size="100%">Dimethyl esters and amides of isophthalic acid</style></keyword><keyword><style  face="normal" font="default" size="100%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme inhibition</style></keyword><keyword><style  face="normal" font="default" size="100%">NADP-glutamate dehydrogenases</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2020</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1864</style></volume><pages><style face="normal" font="default" size="100%">129696</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Background: It has been reported that the genes coding for NADP-dependent glutamate dehydrogenases (NADP-GDHs) showed a cause-effect relationship with Yeast-Hypha (Y-H) reversible transition in a zygomycete Benjaminiella poitrasii. As Y-H transition is significant in human pathogenic fungi for their survival and proliferation in the host, the NADP-GDHs can be explored as antifungal drug targets. Methods: The yeast-form specific BpNADPGDH I and hyphal-form specific BpNADPGDH II of B. poitrasii were purified by heterologous expression in E. coll. BL-21 cells and characterized. The structural analogs of L-glutamate, dimethyl esters of isophthalic acid (DMIP) and its derivatives were designed, synthesized and screened for inhibition of NADP-GDH activity as well as Y-H transition in B. poitrasii, and also in human pathogenic Candida albicans strains. Results: The BpNADPGDH I and BpNADPGDH II were found to be homo-hexameric proteins with native molecular mass of 282 kDa and 298 kDa, respectively and subunit molecular weights of 47 kDa and 49 kDa, respectively. Besides the distinct kinetic properties, BpNADPGDH I and BpNADPGDH II were found to be regulated by cAMP-dependent- and Calmodulin (CaM) dependent- protein kinases, respectively. The DMIP compounds showed a more pronounced effect on H-form specific BpNADPGDH II and inhibited Y-H transition as well as growth in B. poitrasii and C. albicans strains. Conclusion: The present study will be useful to design and develop antifungal drugs against dimorphic human pathogens using glutamate dehydrogenase as a target. Significance: Glutamate dehydrogenases can be explored as a target against human pathogenic fungi.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">11</style></issue><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;3.422&lt;/p&gt;
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