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Rajnikant Dixit

Researcher at National Institute of Malaria Research

Publications -  69
Citations -  1400

Rajnikant Dixit is an academic researcher from National Institute of Malaria Research. The author has contributed to research in topics: Anopheles stephensi & Proteases. The author has an hindex of 14, co-authored 60 publications receiving 1139 citations. Previous affiliations of Rajnikant Dixit include Maharshi Dayanand University & National Institutes of Health.

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Hemocyte differentiation mediates innate immune memory in Anopheles gambiae mosquitoes.

TL;DR: The immune system of mosquitoes is primed early-on when the malaria parasite (Plasmodium spp.) first crosses the mosquito gut epithelial barrier, and a substantial increase in a single type of hemocyte (macrophage-like insect immune cells) is implicated in long-lived antiplasmodial immunity.
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Cysteine Proteases: Modes of Activation and Future Prospects as Pharmacological Targets.

TL;DR: This review specifically highlights the modes of activation (processing) of papain family enzymes, which involve auto-activation, trans-activation and also clarifies the future aspects of targeting PPIs to prevent the activation of cysteine proteases.
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The STAT Pathway Mediates Late-Phase Immunity against Plasmodium in the Mosquito Anopheles gambiae

TL;DR: The AgSTAT-A pathway mediates a late-phase antiplasmodial response that reduces oocyst survival in A. gambiae, and silencing of SOCS, a STAT suppressor, has the opposite effect, reducing Plasmodium infection by increasing NOS expression.
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Salivary glands harbor more diverse microbial communities than gut in Anopheles culicifacies.

TL;DR: The salivary gland microbial community structure is more diverse than gut of the mosquito, probably due to differential feeding associated engagements such as food acquisition, ingestion and digestion processes.
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Structure-function of falcipains: malarial cysteine proteases.

TL;DR: Structural and functional analysis of falcipains showed that they have unique domains including a refolding domain and a hemoglobin binding domain that provide structural insight to facilitate the design or modification of effective drug treatment against malaria.