<?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%">Joshi, C. V.</style></author><author><style face="normal" font="default" size="100%">Ghormade, Vandana</style></author><author><style face="normal" font="default" size="100%">Kunde, P.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, P.</style></author><author><style face="normal" font="default" size="100%">Mamgain, H.</style></author><author><style face="normal" font="default" size="100%">Bhat, Suresh K.</style></author><author><style face="normal" font="default" size="100%">Paknikar, K. M.</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%">Flocculation of dimorphic yeast benjaminiella poitrasii is altered by modulation of NAD-glutamate dehydrogenase</style></title><secondary-title><style face="normal" font="default" size="100%">Bioresource Technology</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%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">flocculation</style></keyword><keyword><style  face="normal" font="default" size="100%">NAD-glutamate dehydrogenase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">FEB</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">4</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCI LTD</style></publisher><pub-location><style face="normal" font="default" size="100%">THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND</style></pub-location><volume><style face="normal" font="default" size="100%">101</style></volume><pages><style face="normal" font="default" size="100%">1393-1395</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 strategy to control flocculation is investigated using dimorphic yeast, Benjaminiella poitrasii as a model. Parent form of this yeast (Y) exhibited faster flocculation (11.1 min) than the monomorphic yeast form mutant Y-5 (12.6 min). Atomic force microscopy revealed higher surface roughness of Y (439.34 rms) than Y-5 (52 rms). Also, the former had a zeta potential of -65.97 +/- 3.45 as against -50.21 +/- 2.49 for the latter. Flocculation of both Y and Y-5 could be altered by supplementing either substrates or inhibitor of NAD-glutamate dehydrogenase (NAD-GDH) in the growth media. The rate of flocculation was promoted by alpha-ketoglutarate or isophthalic acid and decelerated by glutamate with a statistically significant inverse correlation to corresponding NAD-GDH levels. These interesting findings open up new possibilities of using NAD-GDH modulating agents to control flocculation in fermentations for easier downstream processing. (C) 2009 Elsevier Ltd. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.365</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%">Mondal, Bipul</style></author><author><style face="normal" font="default" size="100%">Banerjee, Rahul</style></author><author><style face="normal" font="default" size="100%">Ghosh, Tapas</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synthesis and structural characterization of a solvated dimorph of a hydrazonato-oxovanadium(v) complex with [OV(mu-O)VO] core</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of the Indian Chemical Society</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">crystal structure</style></keyword><keyword><style  face="normal" font="default" size="100%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">hydrazone complex</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxovanadium(v) complex</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">7</style></number><publisher><style face="normal" font="default" size="100%">SCIENTIFIC PUBL-INDIA</style></publisher><pub-location><style face="normal" font="default" size="100%">5-A, NEW PALI RD, PO BOX 91, NEAR HOTEL TAJ HARI MAHAL, JODHPUR, 342 003, INDIA</style></pub-location><volume><style face="normal" font="default" size="100%">88</style></volume><pages><style face="normal" font="default" size="100%">937-941</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In this paper we report the synthesis and structural characterization of a different monoclinic variety of the title complex [V2O3(L)(2)], incorporating the doubly deprotonated benzoyl hydrazone of 5-chloro-2-hydroxyacetophenone (H2L) with P2(1)/c space group that showed some differences in bonding patterns in the solid state with respect to its another monoclinic variety with C2/c space group reported earlier.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">7</style></issue><custom3><style face="normal" font="default" size="100%">Indian</style></custom3><custom4><style face="normal" font="default" size="100%">0.359
</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%">Tupe, S. G.</style></author><author><style face="normal" font="default" size="100%">Kulkarni, R. R.</style></author><author><style face="normal" font="default" size="100%">Shirazi, F.</style></author><author><style face="normal" font="default" size="100%">Sant, D. G.</style></author><author><style face="normal" font="default" size="100%">Joshi, Swati P.</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%">Possible mechanism of antifungal phenazine-1-carboxamide from pseudomonas sp against dimorphic fungi Benjaminiella poitrasii and human pathogen Candida albicans</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Applied Microbiology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Apoptosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Candida albicans</style></keyword><keyword><style  face="normal" font="default" size="100%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">phenazines</style></keyword><keyword><style  face="normal" font="default" size="100%">Pseudomonas sp</style></keyword><keyword><style  face="normal" font="default" size="100%">reactive oxygen species</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%">JAN</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">1</style></number><publisher><style face="normal" font="default" size="100%">WILEY-BLACKWELL</style></publisher><pub-location><style face="normal" font="default" size="100%">111 RIVER ST, HOBOKEN 07030-5774, NJ USA</style></pub-location><volume><style face="normal" font="default" size="100%">118</style></volume><pages><style face="normal" font="default" size="100%">39-48</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;AimInvestigation of antifungal mechanism of phenazine 1-carboxamide (PC) produced by a Pseudomonas strain MCC2142. Methods and ResultsAn antifungal metabolite produced by a Pseudomonas was purified and identified as PC. Human pathogenic fungi such as Candida albicans, Candidaglabrata, Cryptococcus neoformans, Fusarium oxysporum, Aspergillus fumigatus and Aspergillus niger were found to be inhibited by PC (MIC90 32-64gml(-1)). Addition of PC (20gml(-1)) during yeast (Y)-hypha (H) transitions inhibited germ tube formation by &amp;gt;90% and &amp;gt;99% in C.albicans National Collection of Industrial Microorganisms (NCIM) 3471 and nonpathogenic model Benjaminiella poitrasii, respectively. After exposure to PC (20gml(-1)), 75-80% yeast cells of B.poitrasii and C.albicans NCIM 3471 showed rhodamine 123 fluorescence indicating high intracellular reactive oxygen species (ROS) production. ROS further led to hyperpolarization of mitochondrial membrane, subsequently induction of apoptosis as evident by externalization of phosphatidylserine, DNA fragmentation, chromatin condensation and finally death in B.poitrasii. In C.albicans NCIM 3471, PC (20gml(-1)) induced apoptosis. ConclusionsThe antifungal effect of PC in B.poitrasii and C.albicans may be due to ROS-mediated apoptotic death. Significance and Impact of the StudyInhibition of Y-H transition of B.poitrasii and C.albicans by PC indicates that it may prove useful in the control of dimorphic human pathogens.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">1</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%">2.156</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%">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;
</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%">Kumaravel, Nalayeni</style></author><author><style face="normal" font="default" size="100%">Ebinezer, Leonard Barnabas</style></author><author><style face="normal" font="default" size="100%">Ashwin, N. M. R.</style></author><author><style face="normal" font="default" size="100%">Franchin, Cinzia</style></author><author><style face="normal" font="default" size="100%">Battisti, Ilaria</style></author><author><style face="normal" font="default" size="100%">Carletti, Paolo</style></author><author><style face="normal" font="default" size="100%">Sundar, Amalraj Ramesh</style></author><author><style face="normal" font="default" size="100%">Masi, Antonio</style></author><author><style face="normal" font="default" size="100%">Malathi, Palaniyandi</style></author><author><style face="normal" font="default" size="100%">Viswanathan, Rasappa</style></author><author><style face="normal" font="default" size="100%">Arrigoni, Giorgio</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Comparative proteomics of sugarcane smut fungus- Sporisorium scitamineum unravels dynamic proteomic alterations during the dimorphic transition</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Proteomics</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">dimorphism</style></keyword><keyword><style  face="normal" font="default" size="100%">fungi</style></keyword><keyword><style  face="normal" font="default" size="100%">iTRAQ</style></keyword><keyword><style  face="normal" font="default" size="100%">Smut</style></keyword><keyword><style  face="normal" font="default" size="100%">Sugarcane</style></keyword><keyword><style  face="normal" font="default" size="100%">Virulence</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%">JUL </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">304</style></volume><pages><style face="normal" font="default" size="100%">105230</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Life cycle of the dimorphic sugarcane smut fungi, Sporisorium scitamineum , involves recognition and mating of compatible saprophytic yeast -like haploid sporidia (MAT -1 and MAT -2) that upon fusion, develop into infective dikaryotic mycelia. Although the dimorphic transition is intrinsically linked with the pathogenicity and virulence of S. scitamineum , it has never been studied using a proteomic approach. In the present study, an iTRAQ-based comparative proteomic analysis of three distinct stages was carried out. The stages were: the dimorphic transition period - haploid sporidial stage (MAT -1 and MAT -2); the transition phase (24 h post co -culturing (hpc)) and the dikaryotic mycelial stage (48 hpc). Functional categorization of differentially abundant proteins showed that the most altered biological processes were energy production, primary metabolism, especially, carbohydrate, amino acid, fatty acid, followed by translation, post -translation and protein turnover. Several differentially abundant proteins (DAPs), especially in the dikaryotic mycelial stage were predicted as effectors. Taken together, key molecular mechanisms underpinning the dimorphic transition in S. scitamineum at the proteome level were highlighted. The catalogue of stage -specific and dimorphic transition -associated -proteins and potential effectors identified herein represents a list of potential candidates for defective mutant screening to elucidate their functional role in the dimorphic transition and pathogenicity in S. scitamineum . Biological significance: Being the first comparative proteomics analysis of S. scitamineum , this study comprehensively examined three pivotal life cycle stages of the pathogen: the non-pathogenic haploid phase, the transition phase, and the pathogenic dikaryotic mycelial stage. While previous studies have reported the sugarcane and S. scitamineum interactions, this study endeavored to specifically identify the proteins responsible for pathogenicity. By analyzing the proteomic alterations between the haploid and dikaryotic mycelial phases, the study revealed significant changes in metabolic pathway -associated proteins linked to energy production, notably oxidative phosphorylation, and the citrate cycle. Furthermore, this study successfully identified key metabolic pathways that undergo reprogramming during the transition from the non-pathogenic to the pathogenic stage. The study also deciphered the underlying mechanisms driving the morphological and physiological alterations crucial for the S. scitamineum virulence. By studying its life cycle stages, identifying the key metabolic pathways and stage -specific proteins, it provides unprecedented insights into the pathogenicity and potential avenues for intervention. As proteomics continues to advance, such studies pave the way for a deeper understanding of plantpathogen interactions and the development of innovative strategies to mitigate the impact of devastating pathogens like S. scitamineum.&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;
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	2.8&lt;/p&gt;
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