<?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%">Thakre, Archana</style></author><author><style face="normal" font="default" size="100%">Jadhav, Vyankatesh</style></author><author><style face="normal" font="default" size="100%">Kazi, Rubina</style></author><author><style face="normal" font="default" size="100%">Shelar, Amruta</style></author><author><style face="normal" font="default" size="100%">Patil, Rajendra</style></author><author><style face="normal" font="default" size="100%">Kharat, Kiran</style></author><author><style face="normal" font="default" size="100%">Zore, Gajanan</style></author><author><style face="normal" font="default" size="100%">Karuppayil, S. Mohan</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Oxidative stress induced by piperine leads to apoptosis in Candida albicans</style></title><secondary-title><style face="normal" font="default" size="100%">Medical Mycology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Apoptosis</style></keyword><keyword><style  face="normal" font="default" size="100%">C. albicans</style></keyword><keyword><style  face="normal" font="default" size="100%">drug resistance</style></keyword><keyword><style  face="normal" font="default" size="100%">piperine</style></keyword><keyword><style  face="normal" font="default" size="100%">proteomics</style></keyword><keyword><style  face="normal" font="default" size="100%">synergy</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">59</style></volume><pages><style face="normal" font="default" size="100%">366-378</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Candida albicans is a member of pathogens with potential drug resistance threat that needs novel chemotherapeutic strategies. Considering the multifarious biological activities including bioenhancer activity, anti-Candida potential of piperine was evaluated against planktonic/biofilm and hyphal growth of C. albicans alone or in combination as a synergistic agent with fluconazole. Piperine inhibits planktonic growth at or less than 15 mu g/ml, hyphae induction at 5 mu g/ml concentration, and exhibits stage-dependent activity against biofilm growth of a fluconazole-resistant strain of C. albicans (ATCC10231). Though piperine couldn't kill inoculum completely at minimum inhibitory concentration (MIC), it is fungicidal at higher concentrations, as shown in apoptosis assay. FIC index values indicate that piperine exhibits excellent synergistic activity with fluconazole against planktonic (0.123) and biofilm (0.215) growth of an FLC resistant strain. Mode of anti-Candida activity was studied by identifying piperine responsive proteins wherein the abundance of 25 proteins involved in stress response, signal transduction and cell cycle were modulated (22 up and 3 downregulated) significantly in response to piperine (MIC50). Modulation of the proteins involved suggests that piperine affectsmembrane integrity leading to oxidative stress followed by cell cycle arrest and apoptosis in C. albicans. Flow cytometry-basedmitochondrialmembrane potential (MMP), cell cycle and apoptosis assay, as well as real-time quantitative polymerase chain reaction analysis of selected genes, confirms piperine induced oxidative stress (TRR1), cell cycle arrest and apoptosis (CaMCA1). Based on our results, we conclude that piperine inhibits planktonic and difficult-to treat-biofilm growth of C. albicans by affecting membrane integrity thereby inducing oxidative stress and apoptosis. Lay Abstract Piperine inhibit Candida albicans growth (planktonic and biofilm) significantly in our study. Piperine exhibits excellent synergistic potential with fluconazole The proteome analysis suggests that piperine induced membrane damage leads to oxidative stress followed by cell cycle arrest and apoptosis.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</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%">4.076</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%">Abdulghani, Mazen</style></author><author><style face="normal" font="default" size="100%">Telang, Saraswati</style></author><author><style face="normal" font="default" size="100%">Desai, Manisha</style></author><author><style face="normal" font="default" size="100%">Kadam, Shivdas</style></author><author><style face="normal" font="default" size="100%">Kazi, Rubina</style></author><author><style face="normal" font="default" size="100%">Shelar, Amruta</style></author><author><style face="normal" font="default" size="100%">Patil, Rajendra</style></author><author><style face="normal" font="default" size="100%">Maurya, Radheshyam</style></author><author><style face="normal" font="default" size="100%">Zore, Gajanan</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Opaque cell-specific proteome of Candida albicans ATCC 10231</style></title><secondary-title><style face="normal" font="default" size="100%">Medical Mycology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">albicans</style></keyword><keyword><style  face="normal" font="default" size="100%">C</style></keyword><keyword><style  face="normal" font="default" size="100%">LC-MS</style></keyword><keyword><style  face="normal" font="default" size="100%">MS</style></keyword><keyword><style  face="normal" font="default" size="100%">opaque</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidative stress</style></keyword><keyword><style  face="normal" font="default" size="100%">OxPhos</style></keyword><keyword><style  face="normal" font="default" size="100%">protein</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</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%">61</style></volume><pages><style face="normal" font="default" size="100%">myad062</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Candida albicans, a polymorphic opportunistic pathogen of humans, can exist in different morphological forms like yeast, hyphae, pseudohyphae, chlamydospores, and white and opaque cells. Proteomic analysis of opaque form of C. albicans ATCC 10231 is carried out in the present study using microflow liquid chromatography-tandem mass spectrometry and validated using expression analysis of selected genes using reverse transcription quantitative real-time PCR and mitochondrial membrane potential assay. This is the first report identifying opaque cell-specific proteins of C. albicans. A total of 188 proteins were significantly modulated under opaque form compared to white cells, of which 110 were upregulated, and 78 were downregulated. It was observed that oxidative phosphorylation (OxPhos) and oxidative stress are enhanced in C. albicans cells growing under opaque form as proteins involved in OxPhos (Atp1, Atp3, Atp16, Atp7, Cox6, Nuc2, Qcr7, and Sdh12) and oxidative stress response (Gcs1, Gtt11, Gpx2, Sod1, Ccp1, and Lys7) were significantly upregulated. The maximum upregulation of 23.16- and 13.93-fold is observed in the cases of Ccp1 and Nuc2, respectively. The downregulation of proteins, namely Als1, Csh1, Sap9, and Rho1, determining cell surface chemistry indicates modulation in cell wall integrity and reduced adhesion of opaque cells compared to white cells. This study is significant as it is the first draft of the proteomic profile of opaque cells that suggests enhanced OxPhos, oxidative stress, and modulation in cell surface chemistry indicating reduced adhesion and cell wall integrity, which could be associated with reduced virulence in opaque form. However, a deeper investigation is needed to explore it further. Lay Summary Opaque form is one of the least studied morphological forms of Candida albicans. To the best of our knowledge, this is the first report providing opaque cell-specific proteome. It suggests enhanced oxidative phosphorylation, oxidative stress, and modulation in cell surface chemistry, which could be associated with reduced virulence in opaque form.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">7</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;
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	2.9&lt;/p&gt;
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