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Nirupama Mulherkar
Researcher at Yeshiva University
Publications - 10
Citations - 1678
Nirupama Mulherkar is an academic researcher from Yeshiva University. The author has contributed to research in topics: Ebola virus & Viral entry. The author has an hindex of 10, co-authored 10 publications receiving 1502 citations. Previous affiliations of Nirupama Mulherkar include University of Illinois at Chicago & Albert Einstein College of Medicine.
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Journal ArticleDOI
Ebola virus entry requires the cholesterol transporter Niemann–Pick C1
Jan E. Carette,Jan E. Carette,Matthijs Raaben,Anthony C. Wong,Andrew S. Herbert,Gregor Obernosterer,Gregor Obernosterer,Nirupama Mulherkar,Ana I. Kuehne,Philip J. Kranzusch,April M. Griffin,Gordon Ruthel,Paola Dal Cin,John M. Dye,Sean P. J. Whelan,Kartik Chandran,Thijn R. Brummelkamp,Thijn R. Brummelkamp +17 more
TL;DR: It is shown that membrane fusion mediated by filovirus glycoproteins and viral escape from the vesicular compartment require the NPC1 protein, independent of its known function in cholesterol transport, which indicates potential antiviral strategies to combat these deadly agents.
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A Forward Genetic Strategy Reveals Destabilizing Mutations in the Ebolavirus Glycoprotein That Alter Its Protease Dependence during Cell Entry
TL;DR: Ebolavirus entry into cells requires proteolytic disassembly of the viral glycoprotein, GP, and CatB cleavage is required to facilitate the triggering of viral membrane fusion by destabilizing the prefusion conformation of EBOV GP.
Journal ArticleDOI
The Ebola virus glycoprotein mediates entry via a non-classical dynamin-dependent macropinocytic pathway.
Nirupama Mulherkar,Matthijs Raaben,Juan Carlos de la Torre,Sean P. J. Whelan,Kartik Chandran +4 more
TL;DR: Evidence is provided that EBOV uses an atypical dynamin-dependent macropinocytosis-like entry pathway to enter Vero cells, adherent human peripheral blood-derived monocytes, and a mouse dendritic cell line.
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Impact of Ebola Mucin-Like Domain on Antiglycoprotein Antibody Responses Induced by Ebola Virus-Like Particles
TL;DR: It is concluded that the EBOV GP mucin-like domain can increase relative anti-GP titers, however these titers appear to be directed, at least partly, to denatured GP.
Journal ArticleDOI
MADD, a Splice Variant of IG20, Is Indispensable for MAPK Activation and Protection against Apoptosis upon Tumor Necrosis Factor-α Treatment
Bapi Raju V.V.S.N. Kurada,Liang Cheng Li,Nirupama Mulherkar,Mahesh Subramanian,K. V S Prasad,Bellur S. Prabhakar +5 more
TL;DR: The essential role of MADD is demonstrated in protecting cancer cells from TNFα-induced apoptosis by specifically activating MAPKs through Grb2 and Sos1/2 recruitment, and its potential as a novel cancer therapeutic target is demonstrated.