Krishnananda Chattopadhyay

2.9k total citations
99 papers, 2.4k citations indexed

About

Krishnananda Chattopadhyay is a scholar working on Molecular Biology, Materials Chemistry and Neurology. According to data from OpenAlex, Krishnananda Chattopadhyay has authored 99 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 24 papers in Materials Chemistry and 16 papers in Neurology. Recurrent topics in Krishnananda Chattopadhyay's work include Protein Structure and Dynamics (23 papers), Enzyme Structure and Function (13 papers) and Alzheimer's disease research and treatments (13 papers). Krishnananda Chattopadhyay is often cited by papers focused on Protein Structure and Dynamics (23 papers), Enzyme Structure and Function (13 papers) and Alzheimer's disease research and treatments (13 papers). Krishnananda Chattopadhyay collaborates with scholars based in India, United States and France. Krishnananda Chattopadhyay's co-authors include Shyamalava Mazumdar, Carl Frieden, Elliot L. Elson, Goutam De, Anindita Mukhopadhyay, Shubhasis Haldar, Nidhi Joshi, Saveez Saffarian, Sourav Chowdhury and Sunny Sharma and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

Krishnananda Chattopadhyay

94 papers receiving 2.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Krishnananda Chattopadhyay India 24 1.2k 647 308 282 243 99 2.4k
Nakul C. Maiti India 27 1.5k 1.2× 1.2k 1.9× 204 0.7× 330 1.2× 315 1.3× 91 3.6k
Pramit K. Chowdhury India 27 1.1k 0.9× 524 0.8× 134 0.4× 185 0.7× 217 0.9× 96 2.2k
Takashi Sakamoto Japan 29 1.0k 0.9× 624 1.0× 162 0.5× 287 1.0× 127 0.5× 120 2.7k
Morten J. Bjerrum Denmark 29 1.3k 1.1× 525 0.8× 304 1.0× 337 1.2× 88 0.4× 98 2.4k
Barry B. Muhoberac United States 28 774 0.6× 533 0.8× 323 1.0× 314 1.1× 82 0.3× 62 2.1k
Surajit Ghosh India 29 1.3k 1.0× 619 1.0× 69 0.2× 398 1.4× 972 4.0× 165 3.2k
S. M. Yarmoluk Ukraine 29 1.6k 1.3× 623 1.0× 77 0.3× 252 0.9× 96 0.4× 189 2.8k
Toshinori Shimanouchi Japan 26 1.1k 0.9× 208 0.3× 167 0.5× 500 1.8× 303 1.2× 140 1.9k
Nikos S. Hatzakis Denmark 32 2.5k 2.1× 502 0.8× 265 0.9× 600 2.1× 433 1.8× 89 3.7k
Sue A. Carter United States 24 924 0.8× 637 1.0× 717 2.3× 128 0.5× 326 1.3× 46 2.5k

Countries citing papers authored by Krishnananda Chattopadhyay

Since Specialization
Citations

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

Fields of papers citing papers by Krishnananda Chattopadhyay

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Krishnananda Chattopadhyay

This figure shows the co-authorship network connecting the top 25 collaborators of Krishnananda Chattopadhyay. A scholar is included among the top collaborators of Krishnananda Chattopadhyay 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 Krishnananda Chattopadhyay. Krishnananda Chattopadhyay 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.
Jain, Rajeev, et al.. (2025). Influence of Magnesium Ions and Crowding Agents on Structure and Stability of RNA Aptamers. Biochemistry. 64(6). 1233–1243.
2.
Bera, Biswajit, et al.. (2025). An Investigation into Substitution‐Kinetics, Biomolecular Responses and Multimodal Anticancer Potential of a Dihalide Pd(II) Complex. Chemistry - An Asian Journal. 20(10). e202401832–e202401832. 1 indexed citations
3.
Sarkar, Debabrata, et al.. (2025). Small Molecule Modulators of α-Synuclein Phase Separation. ACS Chemical Neuroscience. 16(16). 3174–3183. 1 indexed citations
4.
5.
Jawed, Junaid Jibran, Subrata Majumdar, Syamal Roy, et al.. (2024). Leishmania protein KMP-11 modulates cholesterol transport and membrane fluidity to facilitate host cell invasion. EMBO Reports. 25(12). 5561–5598. 2 indexed citations
6.
Kundu, Sudip, et al.. (2024). Curcumin-based Nanoformulation for the Pyroptotic Death of MDA-MB-231 Cells. ACS Applied Nano Materials. 7(5). 4895–4912. 4 indexed citations
7.
Mohanty, Priyesh, et al.. (2022). A Zn‐dependent structural transition of SOD1 modulates its ability to undergo phase separation. The EMBO Journal. 42(2). e111185–e111185. 33 indexed citations
8.
Manna, Bharat, et al.. (2021). Role of Conformational Change and Glucose Binding Sites in the Enhanced Glucose Tolerance of Agrobacterium tumefaciens 5A GH1 β-Glucosidase Mutants. The Journal of Physical Chemistry B. 125(33). 9402–9416. 11 indexed citations
9.
Dey, Sandip, et al.. (2021). Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects. Communications Biology. 4(1). 518–518. 13 indexed citations
10.
Mukherjee, Kamalika, Saikat Chakrabarti, Syamal Roy, et al.. (2020). MicroRNA exporter HuR clears the internalized pathogens by promoting pro‐inflammatory response in infected macrophages. EMBO Molecular Medicine. 12(3). e11011–e11011. 17 indexed citations
11.
Mishra, Snehasis, et al.. (2019). Efficient Detection of Early Events of α-Synuclein Aggregation Using a Cysteine Specific Hybrid Scaffold. Biochemistry. 58(8). 1109–1119. 13 indexed citations
12.
Chattopadhyay, Krishnananda, et al.. (2019). Cryo-Electron Microscopy Uncovers Key Residues within the Core of Alpha-Synuclein Fibrils. ACS Chemical Neuroscience. 10(3). 1135–1136. 12 indexed citations
13.
Chowdhury, Sourav, et al.. (2018). Comparative Study of Toluidine Blue O and Methylene Blue Binding to Lysozyme and Their Inhibitory Effects on Protein Aggregation. ACS Omega. 3(3). 2588–2601. 52 indexed citations
14.
Tripathi, Timir & Krishnananda Chattopadhyay. (2018). Interaction of α-Synuclein with ATP Synthase: Switching Role from Physiological to Pathological. ACS Chemical Neuroscience. 10(1). 16–17. 16 indexed citations
15.
Prasad, G. V. R., et al.. (2014). Early Sodium Dodecyl Sulfate Induced Collapse of α-Synuclein Correlates with Its Amyloid Formation. ACS Chemical Neuroscience. 6(2). 239–246. 16 indexed citations
16.
Lahiri, Sagar, et al.. (2014). Enzymatic and Regulatory Attributes of Trehalose‐6‐Phosphate Phosphatase from Candida utilis and its Role During Thermal Stress. Journal of Cellular Physiology. 229(9). 1245–1255. 6 indexed citations
17.
Sharma, Sunny, et al.. (2013). OSMOLYTE INDUCED STABILIZATION OF PROTEIN MOLECULES: A BRIEF REVIEW. Journal of Proteins and Proteomics. 3(2). 12 indexed citations
18.
Sharma, Sunny, et al.. (2013). A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties. Scientific Reports. 3(1). 3525–3525. 23 indexed citations
19.
Chattopadhyay, Krishnananda, Elliot L. Elson, & Carl Frieden. (2005). The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods. Proceedings of the National Academy of Sciences. 102(7). 2385–2389. 114 indexed citations
20.
Chattopadhyay, Krishnananda, Saveez Saffarian, Elliot L. Elson, & Carl Frieden. (2002). Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proceedings of the National Academy of Sciences. 99(22). 14171–14176. 99 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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