U. Sen

998 total citations
45 papers, 830 citations indexed

About

U. Sen is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, U. Sen has authored 45 papers receiving a total of 830 indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 15 papers in Materials Chemistry and 9 papers in Genetics. Recurrent topics in U. Sen's work include Enzyme Structure and Function (15 papers), Protein Structure and Dynamics (10 papers) and Biochemical and Structural Characterization (8 papers). U. Sen is often cited by papers focused on Enzyme Structure and Function (15 papers), Protein Structure and Dynamics (10 papers) and Biochemical and Structural Characterization (8 papers). U. Sen collaborates with scholars based in India and United States. U. Sen's co-authors include Kottayil I. Varughese, J. Dasgupta, James Zapf, M. D. Madhusudan, James A. Hoch, Xiaojiang S. Chen, Ronda Bransteitter, Raymond C. Stevens, Courtney Prochnow and Myron F. Goodman and has published in prestigious journals such as Nature, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

U. Sen

44 papers receiving 817 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
U. Sen India 16 591 239 133 120 97 45 830
Peter Frank United States 18 1.2k 2.1× 153 0.6× 81 0.6× 63 0.5× 74 0.8× 36 1.4k
Kazuyuki Takai Japan 21 1.3k 2.2× 204 0.9× 62 0.5× 110 0.9× 128 1.3× 103 1.6k
Marta del Álamo Spain 11 506 0.9× 85 0.4× 164 1.2× 61 0.5× 140 1.4× 15 684
Malcolm Buckle France 20 845 1.4× 421 1.8× 72 0.5× 82 0.7× 189 1.9× 43 1.1k
Daniel W. Celander United States 15 970 1.6× 240 1.0× 155 1.2× 316 2.6× 151 1.6× 24 1.4k
Ludovic Renault United Kingdom 20 1.2k 2.1× 245 1.0× 63 0.5× 29 0.2× 53 0.5× 29 1.4k
Stuart W. Hicks United States 18 553 0.9× 108 0.5× 60 0.5× 247 2.1× 44 0.5× 28 1.1k
Natàlia Jiménez Spain 19 386 0.7× 157 0.7× 58 0.4× 190 1.6× 108 1.1× 47 906
Lance M. Hellman United States 20 1.1k 1.9× 235 1.0× 36 0.3× 426 3.5× 80 0.8× 31 1.7k
Hwai‐Chen Guo United States 19 831 1.4× 174 0.7× 45 0.3× 615 5.1× 77 0.8× 33 1.4k

Countries citing papers authored by U. Sen

Since Specialization
Citations

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

Fields of papers citing papers by U. Sen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of U. Sen

This figure shows the co-authorship network connecting the top 25 collaborators of U. Sen. A scholar is included among the top collaborators of U. Sen 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 U. Sen. U. Sen 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.
Ghosh, Shrestha, et al.. (2024). Crystal structure of the complex between cyclic-di-inosine monophosphate and the Vibrio cholerae standalone phosphodiesterase (VcEAL) at 2.2 Å. Biochemical and Biophysical Research Communications. 737. 150535–150535. 1 indexed citations
2.
3.
Sen, U., et al.. (2019). High resolution structure of Vibrio cholerae acylphosphatase (VcAcP) cage: Identification of drugs, location of its binding site and engineering to facilitate cage formation. Biochemical and Biophysical Research Communications. 523(2). 348–353. 2 indexed citations
4.
Ghosh, Biplab, et al.. (2019). Vibrio cholerae YaeO is a Structural Homologue of RNA Chaperone Hfq that Inhibits Rho-dependent Transcription Termination by Dissociating its Hexameric State. Journal of Molecular Biology. 431(24). 4749–4766. 9 indexed citations
6.
Sen, U., et al.. (2015). Crystal structure of phosphoglucomutase from Leishmania major at 3.5 Å resolution. Biochimie. 121. 102–111. 3 indexed citations
8.
Banerjee, Ramanuj, et al.. (2014). Crystallization and preliminary X-ray analysis of a ribokinase fromVibrio choleraeO395. Acta Crystallographica Section F Structural Biology Communications. 70(8). 1098–1102. 2 indexed citations
9.
Banerjee, Ramanuj, et al.. (2014). Atomic resolution crystal structure of VcLMWPTP-1 from Vibrio cholerae O395: Insights into a novel mode of dimerization in the low molecular weight protein tyrosine phosphatase family. Biochemical and Biophysical Research Communications. 450(1). 390–395. 10 indexed citations
10.
Banerjee, Ramanuj, et al.. (2013). A Novel 8-nm Protein Cage Formed by Vibrio cholerae Acylphosphatase. Journal of Molecular Biology. 426(1). 36–38. 5 indexed citations
11.
Dasgupta, J. & U. Sen. (2013). STRUCTURAL ASPECTS OF STRONG INHIBITION AND ROLE OF SCAFFOLD FOR SERINE PROTEASE INHIBITORS. Journal of Proteins and Proteomics. 2(2).
12.
Dey, Sanjay Kumar, et al.. (2013). Conformational Barrier of CheY3 and Inability of CheY4 to Bind FliM Control the Flagellar Motor Action in Vibrio cholerae. PLoS ONE. 8(9). e73923–e73923. 15 indexed citations
13.
Sen, U., et al.. (2012). Cloning, expression, purification, crystallization and preliminary X-ray analysis of a fructokinase fromVibrio choleraeO395. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(12). 1564–1567. 3 indexed citations
14.
Majumder, Sudip, et al.. (2012). Role of remote scaffolding residues in the inhibitory loop pre-organization, flexibility, rigidification and enzyme inhibition of serine protease inhibitors. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824(7). 882–890. 7 indexed citations
15.
Das, Samir, et al.. (2011). Cloning, expression, purification, crystallization and preliminary X-ray analysis of the 31 kDaVibrio choleraeheat-shock protein VcHsp31. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(11). 1382–1385. 1 indexed citations
16.
Sen, U., et al.. (2010). Cloning, overexpression, purification, crystallization and preliminary X-ray analysis of CheY3, a response regulator that directly interacts with the flagellar `switch complex' inVibrio cholerae. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(8). 944–947. 1 indexed citations
17.
Majumder, Sudip, et al.. (2010). Identification of a novel set of scaffolding residues that are instrumental for the inhibitory property of Kunitz (STI) inhibitors. Protein Science. 19(3). 593–602. 9 indexed citations
18.
Holden, Lauren G., Courtney Prochnow, Ronda Bransteitter, et al.. (2008). Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications. Nature. 456(7218). 121–124. 186 indexed citations
19.
Dasgupta, J., U. Sen, Poppy Datta, et al.. (2003). Crystallization and preliminary X-ray structural studies of hemoglobin A2 and hemoglobin E, isolated from the blood samples of β-thalassemic patients. Biochemical and Biophysical Research Communications. 303(2). 619–623. 13 indexed citations
20.
Ravichandran, S., U. Sen, Chandana Chakrabarti, & J. Κ. Dattagupta. (1999). Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 Å resolution. Acta Crystallographica Section D Biological Crystallography. 55(11). 1814–1821. 21 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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