Soojay Banerjee

4.9k total citations · 1 hit paper
24 papers, 3.7k citations indexed

About

Soojay Banerjee is a scholar working on Molecular Biology, Materials Chemistry and Structural Biology. According to data from OpenAlex, Soojay Banerjee has authored 24 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 10 papers in Materials Chemistry and 7 papers in Structural Biology. Recurrent topics in Soojay Banerjee's work include Enzyme Structure and Function (10 papers), Advanced Electron Microscopy Techniques and Applications (7 papers) and Mitochondrial Function and Pathology (3 papers). Soojay Banerjee is often cited by papers focused on Enzyme Structure and Function (10 papers), Advanced Electron Microscopy Techniques and Applications (7 papers) and Mitochondrial Function and Pathology (3 papers). Soojay Banerjee collaborates with scholars based in United States, Switzerland and United Kingdom. Soojay Banerjee's co-authors include Richard J. Youle, Michael Lazarou, Sriram Subramaniam, Alberto Bartesaghi, Alan Merk, Adam I. Fogel, Shireen A. Sarraf, Yan Li, Koji Yamano and Lesley A. Kane and has published in prestigious journals such as Science, Cell and Chemical Reviews.

In The Last Decade

Soojay Banerjee

23 papers receiving 3.7k citations

Hit Papers

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiq... 2014 2026 2018 2022 2014 250 500 750

Peers

Soojay Banerjee
Terrence Frey United States
Neil A. Farrow United States
Wayne A. Fenton United States
M.G. Iadanza United Kingdom
Prashant Rao United States
Till Rudack Germany
Johnny Habchi United Kingdom
Terrence Frey United States
Soojay Banerjee
Citations per year, relative to Soojay Banerjee Soojay Banerjee (= 1×) peers Terrence Frey

Countries citing papers authored by Soojay Banerjee

Since Specialization
Citations

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

Fields of papers citing papers by Soojay Banerjee

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Soojay Banerjee

This figure shows the co-authorship network connecting the top 25 collaborators of Soojay Banerjee. A scholar is included among the top collaborators of Soojay Banerjee 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 Soojay Banerjee. Soojay Banerjee 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.
Bartesaghi, Alberto, Cecilia Aguerrebere, V. Falconieri, et al.. (2018). Atomic Resolution Cryo-EM Structure of β-Galactosidase. Structure. 26(6). 848–856.e3. 96 indexed citations
2.
Banerjee, Soojay, Alberto Bartesaghi, Alan Merk, et al.. (2016). 2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition. Science. 351(6275). 871–875. 269 indexed citations
3.
Merk, Alan, Alberto Bartesaghi, Soojay Banerjee, et al.. (2016). Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery. Cell. 165(7). 1698–1707. 349 indexed citations
4.
Borgnia, Mario J., Soojay Banerjee, Alan Merk, et al.. (2016). Using Cryo-EM to Map Small Ligands on Dynamic Metabolic Enzymes: Studies with Glutamate Dehydrogenase. Molecular Pharmacology. 89(6). 645–651. 34 indexed citations
5.
Matthies, Doreen, Alberto Bartesaghi, Alan Merk, Soojay Banerjee, & Sriram Subramaniam. (2015). Residue Specific Radiation Damage of Protein Structures using High-Resolution Cryo-Electron Microscopy. Biophysical Journal. 108(2). 190a–190a. 2 indexed citations
6.
Bartesaghi, Alberto, Alan Merk, Soojay Banerjee, et al.. (2015). 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. Science. 348(6239). 1147–1151. 340 indexed citations
7.
Kane, Lesley A., Michael Lazarou, Adam I. Fogel, et al.. (2014). PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. The Journal of Cell Biology. 205(2). 143–153. 991 indexed citations breakdown →
8.
Meyerson, Joel R., Prashant Rao, Janesh Kumar, et al.. (2014). Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports. Scientific Reports. 4(1). 7084–7084. 71 indexed citations
9.
Lin, Xiaoyan, Soojay Banerjee, Joshua D. Kaufman, et al.. (2014). Z-disc-associated, Alternatively Spliced, PDZ Motif-containing Protein (ZASP) Mutations in the Actin-binding Domain Cause Disruption of Skeletal Muscle Actin Filaments in Myofibrillar Myopathy. Journal of Biological Chemistry. 289(19). 13615–13626. 40 indexed citations
10.
Bartesaghi, Alberto, Doreen Matthies, Soojay Banerjee, Alan Merk, & Sriram Subramaniam. (2014). Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy. Proceedings of the National Academy of Sciences. 111(32). 11709–11714. 160 indexed citations
11.
Lazarou, Michael, Derek P. Narendra, Seok Min Jin, et al.. (2013). PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. The Journal of Cell Biology. 200(2). 163–172. 203 indexed citations
13.
Robertson, Joseph W. F., John J. Kasianowicz, & Soojay Banerjee. (2012). Analytical Approaches for Studying Transporters, Channels and Porins. Chemical Reviews. 112(12). 6227–6249. 41 indexed citations
14.
Hoppins, Suzanne, Frank Edlich, Megan M. Cleland, et al.. (2011). The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes. Molecular Cell. 41(2). 150–160. 186 indexed citations
15.
Edlich, Frank, Soojay Banerjee, Motoshi Suzuki, et al.. (2011). Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol. Cell. 145(1). 104–116. 480 indexed citations
16.
Rostovtseva, Tatiana K., Hacène Boukari, Antonella Antignani, et al.. (2009). Bax Activates Endophilin B1 Oligomerization and Lipid Membrane Vesiculation. Journal of Biological Chemistry. 284(49). 34390–34399. 37 indexed citations
17.
Banerjee, Soojay, Baoxian Wei, Maitrayee Bhattacharyya‐Pakrasi, Himadri B. Pakrasi, & Thomas J. Smith. (2003). Structural Determinants of Metal Specificity in the Zinc Transport Protein ZnuA from Synechocystis 6803. Journal of Molecular Biology. 333(5). 1061–1069. 88 indexed citations
18.
Yennawar, Hemant P., et al.. (1997). The effect of denaturants on protein structure. Protein Science. 6(8). 1727–1733. 86 indexed citations
19.
Banerjee, Soojay, Nobuharu Shigematsu, Lewis K. Pannell, et al.. (1997). Probing the Non-Proline Cis Peptide Bond in β-Lactamase from Staphylococcus aureus PC1 by the Replacement Asn136 → Ala,. Biochemistry. 36(36). 10857–10866. 8 indexed citations
20.
Banerjee, Soojay, et al.. (1995). The evolution of sugar isomerases. Protein Engineering Design and Selection. 8(12). 1189–1195. 26 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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