Arghya Barman

723 total citations
27 papers, 602 citations indexed

About

Arghya Barman is a scholar working on Molecular Biology, Physiology and Oncology. According to data from OpenAlex, Arghya Barman has authored 27 papers receiving a total of 602 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 8 papers in Physiology and 7 papers in Oncology. Recurrent topics in Arghya Barman's work include Protein Structure and Dynamics (9 papers), Alzheimer's disease research and treatments (8 papers) and Computational Drug Discovery Methods (6 papers). Arghya Barman is often cited by papers focused on Protein Structure and Dynamics (9 papers), Alzheimer's disease research and treatments (8 papers) and Computational Drug Discovery Methods (6 papers). Arghya Barman collaborates with scholars based in United States, United Kingdom and Japan. Arghya Barman's co-authors include Rajeev Prabhakar, Donald Hamelberg, Ram Prasad Bora, Rajiv R. P. Singh, Xiaoxia Zhu, Mehmet Özbil, Stephan C. Schürer, V. Ramamurthy, Rajib Choudhury and Manish Paul and has published in prestigious journals such as Journal of Biological Chemistry, Accounts of Chemical Research and The Journal of Physical Chemistry B.

In The Last Decade

Arghya Barman

27 papers receiving 598 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Arghya Barman United States 15 374 176 129 86 85 27 602
Andy Merritt United Kingdom 15 430 1.1× 161 0.9× 172 1.3× 71 0.8× 56 0.7× 32 816
Anna K. Tickler Australia 10 450 1.2× 426 2.4× 75 0.6× 64 0.7× 68 0.8× 10 848
Dahabada H. J. Lopes United States 13 581 1.6× 564 3.2× 132 1.0× 56 0.7× 83 1.0× 19 1.0k
Risto Cukalevski Sweden 12 508 1.4× 433 2.5× 85 0.7× 37 0.4× 101 1.2× 13 839
Thomas Wiglenda Germany 10 359 1.0× 366 2.1× 95 0.7× 137 1.6× 124 1.5× 15 918
Monica M. Pallitto United States 5 528 1.4× 557 3.2× 124 1.0× 49 0.6× 57 0.7× 5 780
Eleri Hughes United Kingdom 16 524 1.4× 265 1.5× 50 0.4× 33 0.4× 99 1.2× 33 761
Samer Salamekh United States 5 429 1.1× 561 3.2× 85 0.7× 105 1.2× 55 0.6× 8 785
Wei‐Hui Wu China 14 303 0.8× 568 3.2× 126 1.0× 84 1.0× 110 1.3× 19 803
Michael C. Owen Hungary 13 433 1.2× 308 1.8× 70 0.5× 38 0.4× 74 0.9× 35 707

Countries citing papers authored by Arghya Barman

Since Specialization
Citations

This map shows the geographic impact of Arghya Barman'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 Arghya Barman with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Arghya Barman more than expected).

Fields of papers citing papers by Arghya Barman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Arghya Barman. 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 Arghya Barman. The network helps show where Arghya Barman may publish in the future.

Co-authorship network of co-authors of Arghya Barman

This figure shows the co-authorship network connecting the top 25 collaborators of Arghya Barman. A scholar is included among the top collaborators of Arghya Barman 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 Arghya Barman. Arghya Barman is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Barman, Arghya & Donald Hamelberg. (2016). Fe(II)/Fe(III) Redox Process Can Significantly Modulate the Conformational Dynamics and Electrostatics of Pirin in NF-κB Regulation. ACS Omega. 1(5). 837–842. 13 indexed citations
2.
Paul, Thomas J., Arghya Barman, Mehmet Özbil, et al.. (2016). Mechanisms of peptide hydrolysis by aspartyl and metalloproteases. Physical Chemistry Chemical Physics. 18(36). 24790–24801. 14 indexed citations
3.
Liu, Fange, Jiafeng Geng, Ryan H. Gumpper, et al.. (2015). An Iron Reservoir to the Catalytic Metal. Journal of Biological Chemistry. 290(25). 15621–15634. 13 indexed citations
4.
Barman, Arghya, et al.. (2015). Computational perspective and evaluation of plausible catalytic mechanisms of peptidyl-prolyl cis–trans isomerases. Biochimica et Biophysica Acta (BBA) - General Subjects. 1850(10). 1994–2004. 12 indexed citations
5.
Barman, Arghya, et al.. (2015). Conserved Hydration Sites in Pin1 Reveal a Distinctive Water Recognition Motif in Proteins. Journal of Chemical Information and Modeling. 56(1). 139–147. 3 indexed citations
6.
Barman, Arghya, et al.. (2015). Pushing the Limits of a Molecular Mechanics Force Field To Probe Weak CH···π Interactions in Proteins. Journal of Chemical Theory and Computation. 11(4). 1854–1863. 9 indexed citations
7.
8.
Barman, Arghya & Donald Hamelberg. (2014). Loss of intramolecular electrostatic interactions and limited conformational ensemble may promote self-association ofcis-tau peptide. Proteins Structure Function and Bioinformatics. 83(3). 436–444. 2 indexed citations
9.
Barman, Arghya & Rajeev Prabhakar. (2013). Elucidating the catalytic mechanism of β-secretase (BACE1): A quantum mechanics/molecular mechanics (QM/MM) approach. Journal of Molecular Graphics and Modelling. 40. 1–9. 31 indexed citations
10.
Paul, Manish, et al.. (2013). Comparative molecular dynamics simulation studies for determining factors contributing to the thermostability of chemotaxis protein “CheY”. Journal of Biomolecular Structure and Dynamics. 32(6). 928–949. 37 indexed citations
11.
Özbil, Mehmet, Arghya Barman, Ram Prasad Bora, & Rajeev Prabhakar. (2012). Computational Insights into Dynamics of Protein Aggregation and Enzyme–Substrate Interactions. The Journal of Physical Chemistry Letters. 3(23). 3460–3469. 5 indexed citations
12.
Barman, Arghya & Rajeev Prabhakar. (2012). Protonation States of the Catalytic Dyad of β-Secretase (BACE1) in the Presence of Chemically Diverse Inhibitors: A Molecular Docking Study. Journal of Chemical Information and Modeling. 52(5). 1275–1287. 32 indexed citations
13.
Choudhury, Rajib, Arghya Barman, Rajeev Prabhakar, & V. Ramamurthy. (2012). Hydrocarbons Depending on the Chain Length and Head Group Adopt Different Conformations within a Water-Soluble Nanocapsule:1H NMR and Molecular Dynamics Studies. The Journal of Physical Chemistry B. 117(1). 398–407. 48 indexed citations
14.
Echeverrı́a, Valentina, Ross Zeitlin, Sarah Burgess, et al.. (2011). Cotinine Reduces Amyloid-β Aggregation and Improves Memory in Alzheimer's Disease Mice. Journal of Alzheimer s Disease. 24(4). 817–835. 74 indexed citations
15.
Zhu, Xiaoxia, Arghya Barman, Mehmet Özbil, et al.. (2011). Mechanism of peptide hydrolysis by co-catalytic metal centers containing leucine aminopeptidase enzyme: a DFT approach. JBIC Journal of Biological Inorganic Chemistry. 17(2). 209–222. 22 indexed citations
16.
Barman, Arghya, Stephan C. Schürer, & Rajeev Prabhakar. (2011). Computational Modeling of Substrate Specificity and Catalysis of the β-Secretase (BACE1) Enzyme. Biochemistry. 50(20). 4337–4349. 44 indexed citations
17.
Vetrivel, Kulandaivelu S., Arghya Barman, Ying Chen, et al.. (2011). Loss of Cleavage at β′-Site Contributes to Apparent Increase in β-Amyloid Peptide (Aβ) Secretion by β-Secretase (BACE1)-Glycosylphosphatidylinositol (GPI) Processing of Amyloid Precursor Protein. Journal of Biological Chemistry. 286(29). 26166–26177. 32 indexed citations
18.
Bora, Ram Prasad, Arghya Barman, Xiaoxia Zhu, Mehmet Özbil, & Rajeev Prabhakar. (2010). Which One Among Aspartyl Protease, Metallopeptidase, and Artificial Metallopeptidase is the Most Efficient Catalyst in Peptide Hydrolysis?. The Journal of Physical Chemistry B. 114(33). 10860–10875. 19 indexed citations
19.
Singh, Rajiv R. P., et al.. (2009). Modeling the Self-Assembly Dynamics of Macromolecular Protein Aggregates Underlying Neurodegenerative Disorders. Journal of Computational and Theoretical Nanoscience. 6(6). 1338–1351. 3 indexed citations
20.
Barman, Arghya, et al.. (2008). Insights into the mechanism of methionine oxidation catalyzed by metal (Cu2+, Zn2+, and Fe3+)—Amyloid beta (Aβ) peptide complexes: A computational study. Journal of Computational Chemistry. 30(9). 1405–1413. 13 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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