Asim Poddar

779 total citations
21 papers, 706 citations indexed

About

Asim Poddar is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Asim Poddar has authored 21 papers receiving a total of 706 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 8 papers in Cell Biology and 5 papers in Organic Chemistry. Recurrent topics in Asim Poddar's work include Endoplasmic Reticulum Stress and Disease (4 papers), Metal complexes synthesis and properties (4 papers) and Microtubule and mitosis dynamics (4 papers). Asim Poddar is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (4 papers), Metal complexes synthesis and properties (4 papers) and Microtubule and mitosis dynamics (4 papers). Asim Poddar collaborates with scholars based in India, United States and Spain. Asim Poddar's co-authors include Bhabatarak Bhattacharyya, Pinak Chakrabarti, Avadhesha Surolia, Soumyananda Chakraborti, Gopa Mitra, Suvroma Gupta, Mithu Banerjee, Takashi Owa, Surinder P. Singh and Prachi Joshi and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Langmuir.

In The Last Decade

Asim Poddar

21 papers receiving 693 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Asim Poddar India 13 369 243 114 102 98 21 706
Emma J. Murphy United Kingdom 17 438 1.2× 73 0.3× 109 1.0× 20 0.2× 109 1.1× 24 822
Margret Ryan United States 15 545 1.5× 158 0.7× 152 1.3× 16 0.2× 99 1.0× 23 834
Shin Muraoka Japan 12 567 1.5× 124 0.5× 84 0.7× 21 0.2× 215 2.2× 13 761
Konstantin Pervushin Singapore 15 435 1.2× 90 0.4× 71 0.6× 19 0.2× 90 0.9× 26 709
Zhengding Su China 20 610 1.7× 67 0.3× 56 0.5× 24 0.2× 171 1.7× 86 1.0k
Paul N. Sanderson United Kingdom 17 570 1.5× 356 1.5× 287 2.5× 45 0.4× 138 1.4× 29 1.2k
Marco Chino Italy 19 569 1.5× 157 0.6× 64 0.6× 17 0.2× 324 3.3× 49 1.1k
Seung Seo Lee United Kingdom 17 791 2.1× 519 2.1× 41 0.4× 22 0.2× 112 1.1× 32 1.2k
Ira . Indonesia 16 905 2.5× 168 0.7× 267 2.3× 32 0.3× 79 0.8× 48 1.4k
Enguerran Vanquelef France 7 541 1.5× 192 0.8× 31 0.3× 16 0.2× 137 1.4× 9 833

Countries citing papers authored by Asim Poddar

Since Specialization
Citations

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

Fields of papers citing papers by Asim Poddar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Asim Poddar

This figure shows the co-authorship network connecting the top 25 collaborators of Asim Poddar. A scholar is included among the top collaborators of Asim Poddar 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 Asim Poddar. Asim Poddar 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.
Chakraborty, Tushar, et al.. (2021). Alternative Sigma Factor of Staphylococcus aureus Interacts with the Cognate Antisigma Factor Primarily Using Its Domain 3. Biochemistry. 60(2). 135–151. 6 indexed citations
2.
Chakraborty, Tushar, et al.. (2020). Understanding the structure, stability, and anti-sigma factor-binding thermodynamics of an anti-anti-sigma factor from Staphylococcus aureus. Journal of Biomolecular Structure and Dynamics. 39(17). 6539–6552. 2 indexed citations
3.
Agarwal, Shubhangi, et al.. (2018). Structural insights into the nanomolar affinity of RING E3 ligase ZNRF1 for Ube2N and its functional implications. Biochemical Journal. 475(9). 1569–1582. 11 indexed citations
4.
Mitra, Gopa, Suvroma Gupta, Asim Poddar, & Bhabatarak Bhattacharyya. (2015). MAP2c prevents arachidonic acid-induced fibril formation of tau: Role of chaperone activity and phosphorylation. Biophysical Chemistry. 205. 16–23. 9 indexed citations
5.
Mukherjee, Suman, Shamba Chatterjee, Asim Poddar, Bhabatarak Bhattacharyya, & Suvroma Gupta. (2015). Cytotoxic biphenyl-4-carboxylic acid targets the tubulin–microtubule system and inhibits cellular migration in HeLa cells. Journal of Taibah University for Science. 10(6). 839–849. 2 indexed citations
6.
Chakravarty, Devlina, Asim Poddar, Mahadeb Pal, et al.. (2015). Actin–Curcumin Interaction: Insights into the Mechanism of Actin Polymerization Inhibition. Biochemistry. 54(4). 1132–1143. 16 indexed citations
7.
Chakraborti, Soumyananda, Amlan Das, Asim Poddar, et al.. (2013). Stable and Potent Analogues Derived from the Modification of the Dicarbonyl Moiety of Curcumin. Biochemistry. 52(42). 7449–7460. 65 indexed citations
8.
Chakraborti, Soumyananda, Devlina Chakravarty, Suvroma Gupta, et al.. (2012). Discrimination of Ligands with Different Flexibilities Resulting from the Plasticity of the Binding Site in Tubulin. Biochemistry. 51(36). 7138–7148. 26 indexed citations
9.
Chakraborti, Soumyananda, Neha Kapoor, Amlan Das, et al.. (2011). Curcumin Recognizes a Unique Binding Site of Tubulin. Journal of Medicinal Chemistry. 54(18). 6183–6196. 101 indexed citations
10.
Chakraborti, Soumyananda, Tanaya Chatterjee, Prachi Joshi, et al.. (2009). Structure and Activity of Lysozyme on Binding to ZnO Nanoparticles. Langmuir. 26(5). 3506–3513. 158 indexed citations
11.
12.
Mitra, Gopa, et al.. (2007). Chaperone‐mediated inhibition of tubulin self‐assembly. Proteins Structure Function and Bioinformatics. 67(1). 112–120. 11 indexed citations
13.
Gupta, Suvroma, et al.. (2006). Oxalone and Lactone Moieties of Podophyllotoxin Exhibit Properties of Both the B and C Rings of Colchicine in Its Binding with Tubulin. Biochemistry. 45(20). 6467–6475. 29 indexed citations
14.
Gupta, Suvroma, Mithu Banerjee, Asim Poddar, et al.. (2005). Biphasic Kinetics of the Colchicine−Tubulin Interaction: Role of Amino Acids Surrounding the A ring of Bound Colchicine Molecule. Biochemistry. 44(30). 10181–10188. 7 indexed citations
15.
Sarkar, Taradas, Gopa Mitra, Suvroma Gupta, et al.. (2004). MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes. European Journal of Biochemistry. 271(8). 1488–1496. 17 indexed citations
16.
Gupta, Suvroma, Taradas Sarkar, Asim Poddar, et al.. (2004). The B‐ring substituent at C‐7 of colchicine and the α‐C‐terminus of tubulin communicate through the “tail–body” interaction. Proteins Structure Function and Bioinformatics. 57(3). 602–609. 12 indexed citations
17.
Banerjee, Mithu, Asim Poddar, Gopa Mitra, et al.. (2004). Sulfonamide Drugs Binding to the Colchicine Site of Tubulin:  Thermodynamic Analysis of the Drug−Tubulin Interactions by Isothermal Titration Calorimetry. Journal of Medicinal Chemistry. 48(2). 547–555. 124 indexed citations
18.
Gupta, Suvroma, et al.. (2002). BisANS binding to tubulin: Isothermal titration calorimetry and the site‐specific proteolysis reveal the GTP‐induced structural stability of tubulin. Proteins Structure Function and Bioinformatics. 50(2). 283–289. 13 indexed citations
19.
Manna, Tapas, et al.. (2001). Chaperone-like Activity of Tubulin. Journal of Biological Chemistry. 276(43). 39742–39747. 41 indexed citations
20.
Sarkar, Taradas, Tapas Manna, S.P. Bhattacharyya, et al.. (2001). Role of the carboxy‐termini of tubulin on its chaperone‐like activity. Proteins Structure Function and Bioinformatics. 44(3). 262–269. 11 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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