H
Himani Nailwal
Researcher at University of Massachusetts Medical School
Publications - 8
Citations - 375
Himani Nailwal is an academic researcher from University of Massachusetts Medical School. The author has contributed to research in topics: Viral replication & Virus. The author has an hindex of 6, co-authored 8 publications receiving 245 citations. Previous affiliations of Himani Nailwal include Monash University Malaysia Campus & Monash University.
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Journal ArticleDOI
Necroptosis in anti-viral inflammation
TL;DR: Recent advances on how viruses counteract this host defense mechanism and the effect of necroptosis on the anti-viral inflammatory reaction are discussed.
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Peptidoglycan-Sensing Receptors Trigger the Formation of Functional Amyloids of the Adaptor Protein Imd to Initiate Drosophila NF-κB Signaling
Anni Kleino,Nancy F. Ramia,Gunes Bozkurt,Yanfang Shen,Himani Nailwal,Jing Huang,Johanna Napetschnig,Monique Gangloff,Francis Ka-Ming Chan,Hao Wu,Hao Wu,Jixi Li,Neal S. Silverman +12 more
TL;DR: Amyloid formation involves a motif resembling one found in necroptosis‐associated mammalian proteins and can be negatively regulated, suggesting that amyloidal signaling platforms may present a regulatory point in multiple biological processes.
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The nucleoprotein of influenza A virus induces p53 signaling and apoptosis via attenuation of host ubiquitin ligase RNF43.
TL;DR: This study unravels a novel strategy adopted by IAV for utilizing the much conserved ubiquitin proteasomal pathway and targets RNF43 to modulate p53 ubiquitination levels and hence causes p53 stabilization which is conducive to an enhanced apoptosis level in the host cells.
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A class of viral inducer of degradation of the necroptosis adaptor RIPK3 regulates virus-induced inflammation.
Zhijun Liu,Himani Nailwal,Jonah Rector,Masmudur M. Rahman,Richard Sam,Grant McFadden,Francis Ka-Ming Chan,Francis Ka-Ming Chan +7 more
TL;DR: In this article, a targeted small interfering RNA (siRNA) screen was used to identify a viral inhibitor found in cowpox virus (CPXV) and other orthopoxviruses that bound to the host SKP1-Cullin1-F-box (SCF) machinery and the essential necroptosis kinase receptor interacting protein kinase 3 (RIPK3).
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Nucleoprotein of influenza A virus negatively impacts antiapoptotic protein API5 to enhance E2F1-dependent apoptosis and virus replication.
TL;DR: A proapoptotic role for NP is proposed in IAV pathogenesis, whereby it suppresses expression of antiapoptosis factor API5, thus potentiating the E2F1-dependent apoptotic pathway and ensuring viral replication.