Publications of NIPGR Scientists

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Author: search.filters.author.Kumari, Kamlesh

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    Global bibliometry on three decades of methyl jasmonate-induced plant defense research reveals growth of a specialty area in biology
    (Open Science Publishers LLP, 2025) Chugh, Vipul; Kumari, Kamlesh; Yamal, Gupta; Checker, Vibha Gulyani; Yadav, Gitanjali; Kathpalia, Renu
    Methyl jasmonate (MeJA), a naturally existing plant hormone, acts as a vital defense and signaling molecule. Although this hormone has been discovered recently, published reports spanning the last several decades have shown the pleiotropic effects of the hormone raising numerous questions about its regulation, biogenesis, and mode of action. In this work, we explore the complete scientific research on MeJa from its discovery in 1992, spanning research conducted over three decades, through a complex network analysis of 2,542 documents authored by about 9,000 individuals. Several indicators of research progress were evaluated, including co-authorship networks, keyword thematic maps, indices of national and international collaboration, annual scientific production, and most productive affiliations. These indices not only enabled us to evaluate the importance of a specialty discipline in literature but also the place of nations in determining research directionality and the significance of quality of work. Overall, this bibliometric analysis identifies current research trends in a specialty area in biology and we hope that our work would pave the way for greater international collaborations among researchers and a better understanding of research gaps and future scope of work in the actively expanding field of MeJA induced plant defense, stress, and developmental processes.
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    Cavity architecture based modulation of ligand binding tunnels in plant START domains
    (Elsevier B.V., 2023) Mahtha, Sanjeet Kumar; Kumari, Kamlesh; Gaur, Vineet; Yadav, Gitanjali
    The Steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain represents an evolutionarily conserved superfamily of lipid transfer proteins widely distributed across the tree of life. Despite significant expansion in plants, knowledge about this domain remains inadequate in plants. In this work, we explore the role of cavity architectural modulations in START protein evolution and functional diversity. We use deep-learning approaches to generate plant START domain models, followed by surface accessibility studies and a comprehensive structural investigation of the rice START family. We validate 28 rice START domain models, delineate binding cavities, measure pocket volumes, and compare these with mammalian counterparts to understand evolution of binding preferences. Overall, plant START domains retain the ancestral α/β helix-grip signature, but we find subtle variation in cavity architectures, resulting in significantly smaller ligand-binding tunnels in the plant kingdom. We identify cavity lining residues (CLRs) responsible for reduction in ancestral tunnel space, and these appear to be class specific, and unique to plants, providing a mechanism for the observed shift in domain function. For instance, mammalian cavity lining residues A135, G181 and A192 have evolved to larger CLRs across the plant kingdom, contributing to smaller sizes, minimal STARTs being the largest, while members of type-IV HD-Zip family show almost complete obliteration of lipid binding cavities, consistent with their present-day DNA binding functions. In summary, this work quantifies plant START structural & functional divergence, bridging current knowledge gaps.