Harsh Ranawat

Mr. Harsh Ranawat

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Research Focus & Metrics

Academic Career Length

8Years (2019-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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13 March 2019 in Molecules
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Journal Article
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AGANKUR GOGOI
ANKUR GOGOI
Nirmal MazumderNirmal Mazumder
Nirmal Mazumder
SKSurajit Konwer
Surajit Konwer
HRHarsh Ranawat
Harsh Ranawat
NCNai-Tzu Chen
Nai-Tzu Chen
GZGuan-Yu Zhuo
Guan-Yu Zhuo
Chiral molecules are stereoselective with regard to specific biological functions. Enantiomers differ considerably in their physiological reactions with the human body. Safeguarding the quality and safety of drugs requires an efficient analytical platform by which to selectively probe chiral compounds to ensure the extraction of single enantiomers. Asymmetric synthesis is a mature approach to the production of single enantiomers; however, it is poorly suited to mass production and allows for only specific enantioselective reactions. Furthermore, it is too expensive and time-consuming for the evaluation of therapeutic drugs in the early stages of development. These limitations have prompted the development of surface-modified nanoparticles using amino acids, chiral organic ligands, or functional groups as chiral selectors applicable to a racemic mixture of chiral molecules. The fact that these combinations can be optimized in terms of sensitivity, specificity, and enantioselectivity makes them ideal for enantiomeric recognition and separation. In chiral resolution, molecules bond selectively to particle surfaces according to homochiral interactions, whereupon an enantiopure compound is extracted from the solution through a simple filtration process. In this review article, we discuss the fabrication of chiral nanoparticles and look at the ways their distinctive surface properties have been adopted in enantiomeric recognition and separation.

1 July 2019 in Biomedical Engineering Letters
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Journal Article
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HRHarsh Ranawat
Harsh Ranawat
SPSagnik Pal
Sagnik Pal
Nirmal MazumderNirmal Mazumder
Nirmal Mazumder

26 May 2025 in bioRxiv
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Preprint
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HRHarsh Ranawat
Harsh Ranawat
MCMarc K.M. Cajili
Marc K.M. Cajili
NLNatalia Lopez-Barbosa
Natalia Lopez-Barbosa
TQThomas Quail
Thomas Quail
Remus DameRemus Dame
Remus Dame
SDSvetlana O. Dodonova
Svetlana O. Dodonova
Summary: Asgards are the closest archaeal relatives of eukaryotes, representing an important step in chromatin evolution. However, their chromatin organization has remained enigmatic until now. In this study, we present the first structures of Asgard chromatin assemblies formed by the Hodarchaeal histone HHoB. Our high-resolution cryo-EM structures reveal that this Asgard histone assembles into compact "closed" and into extended "open" hypernucleosomes. Thus the closed hypernucleosome conformation is conserved across archaeal lineages, while the open conformation resembles a eukaryotic H3-H4 octasome and likely represents an Asgard- specific innovation. Moreover, we show that Mg²⁺ ions influence Asgard chromatin conformation, suggesting a regulatory role. Overall, our study provides the first structure-based model of Asgard chromatin organization, expanding our understanding of chromatin architecture in evolutionary context.

3 July 2026 in bioRxiv
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Preprint
Open access
CCChung Hyun Cho
Chung Hyun Cho
CRColleen S. Russett
Colleen S. Russett
ZHZachary H. Harvey
Zachary H. Harvey
NPNika Pende
Nika Pende
LHLogan H. Hodgskiss
Logan H. Hodgskiss
FBFrédéric BERGER
Frédéric BERGER
The emergence of the eukaryotes coincided with the diversification of histone proteins and their post-translational modifications by enzymes that constitute the core of eukaryotic chromatin. Yet the evolutionary origins of this regulatory machinery are unknown. Here, we show that the key molecular components of histone-based chromatin regulation are present in the Asgard archaea, the closest prokaryotic relatives of eukaryotes. Asgard histones are abundant and have extended N-terminal tails rich in lysine residues that can be post-translationally modified, all of which are features shared with eukaryotic histones. In line with these findings, we identify enzymes from Asgard archaea that deposit or remove lysine acetylation on histone tails in vitro. Moreover, Asgard sirtuin deacetylases (SIR2 proteins) restore chromatin silencing in yeast, demonstrating the functional compatibility of Asgard enzymes with eukaryotic histone substrates. Our findings establish that the foundations of histone-based chromatin predate eukaryogenesis and place Asgard archaea as an evolutionary intermediate in the emergence of eukaryotic chromatin.