Boopathy Ramakrishnan

2.7k total citations
44 papers, 2.0k citations indexed

About

Boopathy Ramakrishnan is a scholar working on Molecular Biology, Organic Chemistry and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Boopathy Ramakrishnan has authored 44 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 18 papers in Organic Chemistry and 14 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Boopathy Ramakrishnan's work include Glycosylation and Glycoproteins Research (34 papers), Carbohydrate Chemistry and Synthesis (18 papers) and Monoclonal and Polyclonal Antibodies Research (14 papers). Boopathy Ramakrishnan is often cited by papers focused on Glycosylation and Glycoproteins Research (34 papers), Carbohydrate Chemistry and Synthesis (18 papers) and Monoclonal and Polyclonal Antibodies Research (14 papers). Boopathy Ramakrishnan collaborates with scholars based in United States, Japan and Switzerland. Boopathy Ramakrishnan's co-authors include Pradman K. Qasba, Elizabeth Boeggeman, V. Ramasamy, M. Sundaralingam, Linda C. Hsieh‐Wilson, Nelly Khidekel, Xin Chen, Alexander R. Lippert, Sabine Arndt and Marta Pasek and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Boopathy Ramakrishnan

44 papers receiving 2.0k citations

Peers

Boopathy Ramakrishnan
Jennifer J. Kohler United States
Shawn DeFrees United States
R.B. Parekh United Kingdom
Timothy A. Fritz United States
Stacy A. Malaker United States
Jason E. Hudak United States
Jennifer J. Kohler United States
Boopathy Ramakrishnan
Citations per year, relative to Boopathy Ramakrishnan Boopathy Ramakrishnan (= 1×) peers Jennifer J. Kohler

Countries citing papers authored by Boopathy Ramakrishnan

Since Specialization
Citations

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

Fields of papers citing papers by Boopathy Ramakrishnan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Boopathy Ramakrishnan

This figure shows the co-authorship network connecting the top 25 collaborators of Boopathy Ramakrishnan. A scholar is included among the top collaborators of Boopathy Ramakrishnan 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 Boopathy Ramakrishnan. Boopathy Ramakrishnan 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.
Myette, James R., Toshiki Kano, Hitoshi Suzuki, et al.. (2019). A Proliferation Inducing Ligand (APRIL) targeted antibody is a safe and effective treatment of murine IgA nephropathy. Kidney International. 96(1). 104–116. 62 indexed citations
2.
Ramakrishnan, Boopathy, Kristin Narayan, Andrew M. Wollacott, et al.. (2018). Extending human IgG half-life using structure-guided design. mAbs. 10(7). 1–13. 76 indexed citations
3.
Zhu, Zhongyu, Boopathy Ramakrishnan, Jinyu Li, et al.. (2014). Site-specific antibody-drug conjugation through an engineered glycotransferase and a chemically reactive sugar. mAbs. 6(5). 1190–1200. 80 indexed citations
4.
Ramakrishnan, Boopathy & Pradman K. Qasba. (2013). In Vitro Folding of β-1,4Galactosyltransferase and Polypeptide-α-N-Acetylgalactosaminyltransferase from the Inclusion Bodies. Methods in molecular biology. 1022. 321–333. 3 indexed citations
5.
Ramakrishnan, Boopathy, Elizabeth Boeggeman, & Pradman K. Qasba. (2012). Binding of N-Acetylglucosamine (GlcNAc) β1–6-branched Oligosaccharide Acceptors to β4-Galactosyltransferase I Reveals a New Ligand Binding Mode. Journal of Biological Chemistry. 287(34). 28666–28674. 14 indexed citations
6.
Ramakrishnan, Boopathy & Pradman K. Qasba. (2010). Crystal Structure of the Catalytic Domain of Drosophila β1,4-Galactosyltransferase-7. Journal of Biological Chemistry. 285(20). 15619–15626. 18 indexed citations
7.
Boeggeman, Elizabeth, Boopathy Ramakrishnan, Marta Pasek, et al.. (2009). Site Specific Conjugation of Fluoroprobes to the Remodeled Fc N-Glycans of Monoclonal Antibodies Using Mutant Glycosyltransferases: Application for Cell Surface Antigen Detection. Bioconjugate Chemistry. 20(6). 1228–1236. 83 indexed citations
8.
Brown, Jillian R., Feng Yang, Anjana Sinha, et al.. (2008). Deoxygenated Disaccharide Analogs as Specific Inhibitors of β1–4-Galactosyltransferase 1 and Selectin-mediated Tumor Metastasis. Journal of Biological Chemistry. 284(8). 4952–4959. 35 indexed citations
9.
Qasba, Pradman K., Boopathy Ramakrishnan, & Elizabeth Boeggeman. (2008). Structure and Function of β -1,4-Galactosyltransferase. Current Drug Targets. 9(4). 292–309. 102 indexed citations
10.
Qasba, Pradman K., Boopathy Ramakrishnan, & Elizabeth Boeggeman. (2006). Mutant glycosyltransferases assist in the development of a targeted drug delivery system and contrast agents for MRI. The AAPS Journal. 8(1). E190–5. 9 indexed citations
11.
Ramakrishnan, Boopathy & Pradman K. Qasba. (2006). Role of a Single Amino Acid in the Evolution of Glycans of Invertebrates and Vertebrates. Journal of Molecular Biology. 365(3). 570–576. 23 indexed citations
12.
Ramakrishnan, Boopathy, Elizabeth Boeggeman, & Pradman K. Qasba. (2004). Effect of the Met344His Mutation on the Conformational Dynamics of Bovine β-1,4-Galactosyltransferase:  Crystal Structure of the Met344His Mutant in Complex with Chitobiose,,. Biochemistry. 43(39). 12513–12522. 33 indexed citations
13.
Ramakrishnan, Boopathy, Elizabeth Boeggeman, V. Ramasamy, & Pradman K. Qasba. (2004). Structure and catalytic cycle of β-1,4-galactosyltransferase. Current Opinion in Structural Biology. 14(5). 593–600. 84 indexed citations
14.
Khidekel, Nelly, Sabine Arndt, Alexander R. Lippert, et al.. (2003). A Chemoenzymatic Approach toward the Rapid and Sensitive Detection of O -GlcNAc Posttranslational Modifications. Journal of the American Chemical Society. 125(52). 16162–16163. 229 indexed citations
15.
Boeggeman, Elizabeth, Boopathy Ramakrishnan, & Pradman K. Qasba. (2003). The N-terminal stem region of bovine and human β1,4-galactosyltransferase I increases the in vitro folding efficiency of their catalytic domain from inclusion bodies. Protein Expression and Purification. 30(2). 219–229. 32 indexed citations
16.
Ramakrishnan, Boopathy, Elizabeth Boeggeman, & Pradman K. Qasba. (2002). β-1,4-Galactosyltransferase and Lactose Synthase: Molecular Mechanical Devices. Biochemical and Biophysical Research Communications. 291(5). 1113–1118. 38 indexed citations
17.
Ramakrishnan, Boopathy & Pradman K. Qasba. (2002). Structure-based Design of β1,4-Galactosyltransferase I (β4Gal-T1) with Equally Efficient N-Acetylgalactosaminyltransferase Activity. Journal of Biological Chemistry. 277(23). 20833–20839. 192 indexed citations
18.
Kumar, Amarendra, et al.. (1994). Structure and function of the catalytic site mutant Asp 99 Asn of phospholipase A2: Absence of the conserved structural water. Protein Science. 3(11). 2082–2088. 21 indexed citations
19.
Chen, Xin, et al.. (1994). Binding of two distamycin A molecules in the minor groove of an alternating B–DNA duplex. Nature Structural Biology. 1(3). 169–175. 117 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026