Debanjan Bhowmik

725 total citations
26 papers, 601 citations indexed

About

Debanjan Bhowmik is a scholar working on Physiology, Molecular Biology and Biomaterials. According to data from OpenAlex, Debanjan Bhowmik has authored 26 papers receiving a total of 601 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Physiology, 15 papers in Molecular Biology and 11 papers in Biomaterials. Recurrent topics in Debanjan Bhowmik's work include Alzheimer's disease research and treatments (17 papers), Supramolecular Self-Assembly in Materials (10 papers) and Protein Structure and Dynamics (9 papers). Debanjan Bhowmik is often cited by papers focused on Alzheimer's disease research and treatments (17 papers), Supramolecular Self-Assembly in Materials (10 papers) and Protein Structure and Dynamics (9 papers). Debanjan Bhowmik collaborates with scholars based in India, United States and Canada. Debanjan Bhowmik's co-authors include Sudipta Maiti, Perunthiruthy K. Madhu, Muralidharan Chandrakesan, Bidyut Sarkar, Venus Singh Mithu, Bappaditya Chandra, Anand Kant Das, Teri W. Odom, Kaustubh R. Mote and Gilbert C. Walker and has published in prestigious journals such as Journal of Biological Chemistry, Angewandte Chemie International Edition and Nature Communications.

In The Last Decade

Debanjan Bhowmik

26 papers receiving 595 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Debanjan Bhowmik India 15 376 323 136 91 81 26 601
Bappaditya Chandra India 12 214 0.6× 323 1.0× 69 0.5× 33 0.4× 48 0.6× 21 490
Hong Zeng United States 12 431 1.1× 256 0.8× 58 0.4× 23 0.3× 33 0.4× 21 776
Geoffrey W. Platt United Kingdom 16 410 1.1× 685 2.1× 78 0.6× 52 0.6× 63 0.8× 21 888
Lauren E. Buchanan United States 12 325 0.9× 594 1.8× 92 0.7× 29 0.3× 33 0.4× 23 916
Michael Schleeger Germany 10 151 0.4× 265 0.8× 73 0.5× 31 0.3× 40 0.5× 15 514
Samo Curk United Kingdom 6 232 0.6× 233 0.7× 73 0.5× 24 0.3× 17 0.2× 7 378
Bidyut Sarkar India 13 382 1.0× 324 1.0× 111 0.8× 8 0.1× 30 0.4× 22 596
Neelanjana Sengupta India 16 190 0.5× 369 1.1× 99 0.7× 8 0.1× 75 0.9× 46 604
Brian Michael United States 8 536 1.4× 486 1.5× 156 1.1× 9 0.1× 26 0.3× 9 803
Juliane Adler Germany 15 234 0.6× 229 0.7× 99 0.7× 8 0.1× 34 0.4× 19 391

Countries citing papers authored by Debanjan Bhowmik

Since Specialization
Citations

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

Fields of papers citing papers by Debanjan Bhowmik

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Debanjan Bhowmik

This figure shows the co-authorship network connecting the top 25 collaborators of Debanjan Bhowmik. A scholar is included among the top collaborators of Debanjan Bhowmik 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 Debanjan Bhowmik. Debanjan Bhowmik 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.
Bhowmik, Debanjan, Christiane Gläser, Matthew C. Childers, et al.. (2025). Hypertrophic cardiomyopathy mutations Y115H and E497D disrupt the folded-back state of human β-cardiac myosin allosterically. Nature Communications. 16(1). 8751–8751. 1 indexed citations
2.
Bonizzi, Arianna, Maria Grimaldi, Marta Truffi, et al.. (2025). Exploring breast cancer-related biochemical changes in circulating extracellular vesicles using Raman spectroscopy. Biosensors and Bioelectronics. 278. 117287–117287. 2 indexed citations
3.
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Bhowmik, Debanjan, et al.. (2019). Resolving Single-Nanoconstruct Dynamics during Targeting and Nontargeting Live-Cell Membrane Interactions. ACS Nano. 13(12). 13637–13644. 18 indexed citations
6.
Hu, Jingtian, Danqing Wang, Debanjan Bhowmik, et al.. (2019). Lattice-Resonance Metalenses for Fully Reconfigurable Imaging. ACS Nano. 13(4). 4613–4620. 49 indexed citations
7.
Choo, Priscilla, Alexander J. Hryn, Kayla S. B. Culver, et al.. (2018). Wavelength-Dependent Differential Interference Contrast Inversion of Anisotropic Gold Nanoparticles. The Journal of Physical Chemistry C. 122(47). 27024–27031. 18 indexed citations
8.
Chandra, Bappaditya, Venus Singh Mithu, Debanjan Bhowmik, et al.. (2017). Curcumin Dictates Divergent Fates for the Central Salt Bridges in Amyloid- β 40 and Amyloid- β 42. Biophysical Journal. 112(8). 1597–1608. 16 indexed citations
9.
Chandra, Bappaditya, Debanjan Bhowmik, Kaustubh R. Mote, et al.. (2017). Secondary Structure Flipping Connected to Salt-Bridge Formation Converts Toxic Amyloid-β 40 Oligomers to Fibrils. Biophysical Journal. 112(3). 362a–363a. 3 indexed citations
10.
Das, Anand Kant, Anoop Rawat, Debanjan Bhowmik, et al.. (2015). An Early Folding Contact between Phe19 and Leu34 is Critical for Amyloid-β Oligomer Toxicity. ACS Chemical Neuroscience. 6(8). 1290–1295. 51 indexed citations
11.
Chandrakesan, Muralidharan, Debanjan Bhowmik, Bidyut Sarkar, et al.. (2015). Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18–35 and Makes It Soluble. Journal of Biological Chemistry. 290(50). 30099–30107. 13 indexed citations
12.
Bhowmik, Debanjan, Kaustubh R. Mote, Christina M. MacLaughlin, et al.. (2015). Cell-Membrane-Mimicking Lipid-Coated Nanoparticles Confer Raman Enhancement to Membrane Proteins and Reveal Membrane-Attached Amyloid-β Conformation. ACS Nano. 9(9). 9070–9077. 81 indexed citations
13.
Mithu, Venus Singh, Bidyut Sarkar, Debanjan Bhowmik, et al.. (2014). Curcumin Alters the Salt Bridge-containing Turn Region in Amyloid β(1–42) Aggregates. Journal of Biological Chemistry. 289(16). 11122–11131. 49 indexed citations
14.
Sarkar, Bidyut, Venus Singh Mithu, Bappaditya Chandra, et al.. (2014). Significant Structural Differences between Transient Amyloid‐β Oligomers and Less‐Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations. Angewandte Chemie International Edition. 53(27). 6888–6892. 83 indexed citations
15.
Bhowmik, Debanjan, Anand Kant Das, & Sudipta Maiti. (2014). Rapid, Cell-Free Assay for Membrane-Active Forms of Amyloid-β. Langmuir. 31(14). 4049–4053. 20 indexed citations
16.
Sarkar, Bidyut, Venus Singh Mithu, Bappaditya Chandra, et al.. (2014). Significant Structural Differences between Transient Amyloid‐β Oligomers and Less‐Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations. Angewandte Chemie. 126(27). 7008–7012. 4 indexed citations
17.
Bhowmik, Debanjan, Christina M. MacLaughlin, Muralidharan Chandrakesan, et al.. (2013). pH changes the aggregation propensity of amyloid-β without altering the monomer conformation. Physical Chemistry Chemical Physics. 16(3). 885–889. 25 indexed citations
18.
Nag, Suman, Bidyut Sarkar, Muralidharan Chandrakesan, et al.. (2013). A folding transition underlies the emergence of membrane affinity in amyloid-β. Physical Chemistry Chemical Physics. 15(44). 19129–19129. 31 indexed citations
19.
Sarkar, Bidyut, et al.. (2011). アミロイドが凝集するAβ 42 のヘアピン形のクロスβ構造を変えることなしに,Asp 23 -Lys 28 塩橋を破壊するZn ++ 結合. Biophysical Journal. 101(11). 2825–2832. 1 indexed citations
20.
Mithu, Venus Singh, Bidyut Sarkar, Debanjan Bhowmik, et al.. (2011). Zn++ Binding Disrupts the Asp23-Lys28 Salt Bridge without Altering the Hairpin-Shaped Cross-β Structure of Aβ42 Amyloid Aggregates. Biophysical Journal. 101(11). 2825–2832. 54 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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