Madhurima Jana

868 total citations
56 papers, 719 citations indexed

About

Madhurima Jana is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Madhurima Jana has authored 56 papers receiving a total of 719 indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 19 papers in Materials Chemistry and 12 papers in Organic Chemistry. Recurrent topics in Madhurima Jana's work include Protein Structure and Dynamics (18 papers), Enzyme Structure and Function (14 papers) and Protein Interaction Studies and Fluorescence Analysis (13 papers). Madhurima Jana is often cited by papers focused on Protein Structure and Dynamics (18 papers), Enzyme Structure and Function (14 papers) and Protein Interaction Studies and Fluorescence Analysis (13 papers). Madhurima Jana collaborates with scholars based in India, Chile and United States. Madhurima Jana's co-authors include Sanjoy Bandyopadhyay, Atanu Singha Roy, Sharat Sarmah, Alexander D. MacKerell, Sourav Das, Mostofa Ataur Rohman, Rakesh Parida, Santanab Giri, Sankar N. Maity and G. Naaresh Reddy and has published in prestigious journals such as The Journal of Chemical Physics, The Journal of Physical Chemistry B and Journal of Power Sources.

In The Last Decade

Madhurima Jana

53 papers receiving 711 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Madhurima Jana India	16	420	162	132	108	95	56	719
Upendra Kumar Singh India	16	504 1.2×	72 0.4×	318 2.4×	80 0.7×	56 0.6×	19	845
Kshatresh Dutta Dubey India	22	549 1.3×	201 1.2×	257 1.9×	79 0.7×	39 0.4×	79	1.3k
Thomas J. Thamann United States	16	458 1.1×	197 1.2×	104 0.8×	130 1.2×	37 0.4×	33	879
Diogo Vila‐Viçosa Portugal	21	475 1.1×	215 1.3×	233 1.8×	81 0.8×	126 1.3×	36	994
Adolfo Lai Italy	15	252 0.6×	150 0.9×	146 1.1×	198 1.8×	75 0.8×	63	824
Yuko Ito Japan	20	492 1.2×	119 0.7×	114 0.9×	148 1.4×	46 0.5×	63	1.0k
Elżbieta Bednarek Poland	21	416 1.0×	132 0.8×	292 2.2×	278 2.6×	29 0.3×	91	1.1k
Daquan Gao United States	19	651 1.6×	91 0.6×	219 1.7×	102 0.9×	31 0.3×	34	1.2k
Yoshiko Moriyama Japan	14	800 1.9×	182 1.1×	357 2.7×	128 1.2×	113 1.2×	32	1.1k
Wojciech Bocian Poland	19	340 0.8×	95 0.6×	281 2.1×	203 1.9×	18 0.2×	72	836

Countries citing papers authored by Madhurima Jana

Since Specialization

Citations

This map shows the geographic impact of Madhurima Jana's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Madhurima Jana with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Madhurima Jana more than expected).

Fields of papers citing papers by Madhurima Jana

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Madhurima Jana. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Madhurima Jana. The network helps show where Madhurima Jana may publish in the future.

Co-authorship network of co-authors of Madhurima Jana

This figure shows the co-authorship network connecting the top 25 collaborators of Madhurima Jana. A scholar is included among the top collaborators of Madhurima Jana based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Madhurima Jana. Madhurima Jana is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Jana, Madhurima, et al.. (2025). Spectroscopic and computational insights into binding of daphnetin with pepsin: Inhibition of pepsin fibrillation and identification of amyloidogenic core region. International Journal of Biological Macromolecules. 321(Pt 2). 146232–146232.

Kumar, Sonu, et al.. (2025). Proline concentration driven thermostability and hydration properties of ubiquitin. Journal of Molecular Liquids. 424. 127108–127108. 3 indexed citations

Maity, Sankar N., et al.. (2024). Comparative Bindings of Glycosaminoglycans with CXCL8 Monomer and Dimer: Insights from Conformational Dynamics and Kinetics of Hydrogen Bonds. The Journal of Physical Chemistry B. 128(42). 10348–10362.

Lyndem, Sona, et al.. (2024). Inhibition of amyloid formation of bovine hemoglobin by bioactive phenolic acids: an elaborate investigation into their binding properties with the protein using multi-spectroscopic and computational techniques. New Journal of Chemistry. 48(27). 12362–12386. 3 indexed citations

Das, Sourav, et al.. (2024). Isoflavones and lysozyme interplay: Molecular insights into binding mechanisms and inhibitory efficacies of isoflavones against protein modification. Chemical Physics Impact. 8. 100643–100643. 5 indexed citations

Jana, Madhurima, et al.. (2024). Binding Interaction of Coumarin Derivative Daphnetin with Ovalbumin: Molecular Insights into the Complexation Process and Effects of Metal Ions and pH in the Binding and Antifibrillation Studies. Molecular Pharmaceutics. 21(9). 4708–4725. 3 indexed citations

Maity, Sankar N., et al.. (2024). Interfacial Glucose to Regulate Hydrated Lipid Bilayer Properties: Influence of Concentrations. Journal of Chemical Information and Modeling. 64(9). 3841–3854. 1 indexed citations

Jana, Madhurima, et al.. (2024). Boron-containing fullerene-based salts with cyclic carbonate solvents as electrolytes for Li-ion batteries and beyond. Physical Chemistry Chemical Physics. 26(12). 9317–9328. 2 indexed citations

Maity, Sankar N., et al.. (2023). Construing the Interactions of Coumarin Derivatives with the Main Protease of Stomach Pepsin Using Spectroscopic and Computational Analyses: Insights into the Binding Thermodynamics, Antifibrillation Studies, and Enzymatic Assay. ACS Food Science & Technology. 4(1). 245–262. 5 indexed citations

10.

Jana, Madhurima, et al.. (2023). Analysis of the Binding Mechanism of Bioactive Coumarins with Ovalbumin: Further Investigation into the Inhibitory Effects toward Protein Fibrillation. ACS Food Science & Technology. 3(5). 866–880. 8 indexed citations

11.

Jana, Madhurima, et al.. (2022). Understanding Conformational Properties and Role of Hydrogen Bonds in Glycosaminoglycans‐Interleukin8 Complexes in Aqueous Medium by Molecular Dynamics Simulation. ChemPhysChem. 24(4). e202200440–e202200440. 4 indexed citations

12.

Mitra, Amit, et al.. (2022). Solid state synthesis of bispyridyl-ferrocene conjugates with unusual site selective 1,4-Michael addition, as potential inhibitor and electrochemical probe for fibrillation in amyloidogenic protein. Journal of Molecular Structure. 1273. 134362–134362. 6 indexed citations

13.

Satish, Lakkoji, et al.. (2021). Conformational changes of GDNF-derived peptide induced by heparin, heparan sulfate, and sulfated hyaluronic acid – Analysis by circular dichroism spectroscopy and molecular dynamics simulation. International Journal of Biological Macromolecules. 182. 2144–2150. 12 indexed citations

14.

Parida, Rakesh, et al.. (2021). In-silico investigation of the conformational properties of the disaccharide units of chondroitin, dermatan and heparan sulphate in aqueous medium. Journal of the Indian Chemical Society. 98(5). 100064–100064. 2 indexed citations

15.

Sarmah, Sharat, et al.. (2020). Elucidation of molecular interaction of bioactive flavonoid luteolin with human serum albumin and its glycated analogue using multi-spectroscopic and computational studies. Journal of Molecular Liquids. 318. 114147–114147. 54 indexed citations

16.

Jana, Madhurima, et al.. (2020). Insights into the Sensitivity of Arginine Concentration to Preserve the Folded Form of Insulin Monomer under Thermal Stress. Journal of Chemical Information and Modeling. 60(6). 3105–3119. 14 indexed citations

17.

Das, Sourav, et al.. (2019). Lysozyme–luteolin binding: molecular insights into the complexation process and the inhibitory effects of luteolin towards protein modification. Physical Chemistry Chemical Physics. 21(23). 12649–12666. 71 indexed citations

18.

Reddy, G. Naaresh, Rakesh Parida, Puru Jena, Madhurima Jana, & Santanab Giri. (2019). Superhalogens as Building Blocks of Super Lewis Acids. ChemPhysChem. 20(12). 1607–1612. 11 indexed citations

19.

Jana, Madhurima & Sanjoy Bandyopadhyay. (2012). Restricted dynamics of water around a protein–carbohydrate complex: Computer simulation studies. The Journal of Chemical Physics. 137(5). 55102–55102. 14 indexed citations

20.

Jana, Madhurima & Sanjoy Bandyopadhyay. (2012). Conformational flexibility of a protein–carbohydrate complex and the structure and ordering of surrounding water. Physical Chemistry Chemical Physics. 14(18). 6628–6628. 30 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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