Subha Sundaram

707 total citations
17 papers, 574 citations indexed

About

Subha Sundaram is a scholar working on Molecular Biology, Immunology and Organic Chemistry. According to data from OpenAlex, Subha Sundaram has authored 17 papers receiving a total of 574 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 8 papers in Immunology and 5 papers in Organic Chemistry. Recurrent topics in Subha Sundaram's work include Glycosylation and Glycoproteins Research (14 papers), Galectins and Cancer Biology (6 papers) and Monoclonal and Polyclonal Antibodies Research (5 papers). Subha Sundaram is often cited by papers focused on Glycosylation and Glycoproteins Research (14 papers), Galectins and Cancer Biology (6 papers) and Monoclonal and Polyclonal Antibodies Research (5 papers). Subha Sundaram collaborates with scholars based in United States, China and Hungary. Subha Sundaram's co-authors include Pamela Stanley, A. Etienne, Stuart M. Haslam, Simon J. North, Sara Chalabi, Anne Dell, Jihye Jang‐Lee, Nancy L. Shaper, Jae Hoon Lee and T. Shantha Raju and has published in prestigious journals such as Journal of Biological Chemistry, Angewandte Chemie International Edition and Biochemistry.

In The Last Decade

Subha Sundaram

17 papers receiving 565 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Subha Sundaram United States 13 516 176 166 122 81 17 574
Mary C. Beranek United States 12 443 0.9× 142 0.8× 197 1.2× 81 0.7× 112 1.4× 13 627
Lan‐Yi Chang Taiwan 10 474 0.9× 177 1.0× 203 1.2× 49 0.4× 114 1.4× 16 614
Stephen M. Manzella United States 12 456 0.9× 184 1.0× 135 0.8× 67 0.5× 133 1.6× 17 652
Peter J. Chefalo United States 10 383 0.7× 135 0.8× 202 1.2× 59 0.5× 152 1.9× 12 552
Detlef Grunow Germany 11 575 1.1× 296 1.7× 95 0.6× 116 1.0× 73 0.9× 18 667
Eckart Grabenhorst Germany 12 558 1.1× 105 0.6× 137 0.8× 128 1.0× 79 1.0× 19 645
Mindy Porterfield United States 9 458 0.9× 111 0.6× 138 0.8× 35 0.3× 89 1.1× 9 520
Morten Alder Schulz Denmark 7 353 0.7× 62 0.4× 98 0.6× 140 1.1× 35 0.4× 7 403
M. KISO Japan 10 408 0.8× 162 0.9× 147 0.9× 52 0.4× 105 1.3× 13 523
S Hirani United States 9 308 0.6× 141 0.8× 172 1.0× 76 0.6× 106 1.3× 10 516

Countries citing papers authored by Subha Sundaram

Since Specialization
Citations

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

Fields of papers citing papers by Subha Sundaram

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Subha Sundaram

This figure shows the co-authorship network connecting the top 25 collaborators of Subha Sundaram. A scholar is included among the top collaborators of Subha Sundaram 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 Subha Sundaram. Subha Sundaram is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

17 of 17 papers shown
1.
Lu, Linchao, Shweta Varshney, Youxi Yuan, et al.. (2023). In vivo evidence for GDP-fucose transport in the absence of transporter SLC35C1 and putative transporter SLC35C2. Journal of Biological Chemistry. 299(12). 105406–105406. 6 indexed citations
2.
Liang, Meng, Boris Bartholdy, Frank Batista, et al.. (2020). The Golgi Glycoprotein MGAT4D is an Intrinsic Protector of Testicular Germ Cells From Mild Heat Stress. Scientific Reports. 10(1). 2135–2135. 12 indexed citations
3.
Mayoral, Joshua, et al.. (2020). Point mutations that inactivate MGAT4D-L, an inhibitor of MGAT1 and complex N-glycan synthesis. Journal of Biological Chemistry. 295(41). 14053–14064. 2 indexed citations
4.
Varshney, Shweta, Frank Batista, Subha Sundaram, et al.. (2019). A modifier in the 129S2/SvPasCrl genome is responsible for the viability of Notch1[12f/12f] mice. BMC Developmental Biology. 19(1). 19–19. 15 indexed citations
5.
Batista, Frank, et al.. (2018). MGAT1 and Complex N-Glycans Regulate ERK Signaling During Spermatogenesis. Scientific Reports. 8(1). 2022–2022. 17 indexed citations
6.
Varshney, Shweta, Mitsutaka Ogawa, Yuta Sakaidani, et al.. (2017). O-GlcNAc on NOTCH1 EGF repeats regulates ligand-induced Notch signaling and vascular development in mammals. eLife. 6. 67 indexed citations
7.
Hassinen, Antti, et al.. (2015). GnT1IP-L specifically inhibits MGAT1 in the Golgi via its luminal domain. eLife. 4. 19 indexed citations
8.
Stanley, Pamela & Subha Sundaram. (2014). Rapid Assays for Lectin Toxicity and Binding Changes that Reflect Altered Glycosylation in Mammalian Cells. PubMed. 6(2). 117–133. 6 indexed citations
9.
Zheng, Tianqing, Hao Jiang, David Soriano del Amo, et al.. (2011). Tracking N‐Acetyllactosamine on Cell‐Surface Glycans In Vivo. Angewandte Chemie International Edition. 50(18). 4113–4118. 72 indexed citations
10.
Zheng, Tianqing, Hao Jiang, David Soriano del Amo, et al.. (2011). Tracking N‐Acetyllactosamine on Cell‐Surface Glycans In Vivo. Angewandte Chemie. 123(18). 4199–4204. 17 indexed citations
11.
North, Simon J., Subha Sundaram, Jihye Jang‐Lee, et al.. (2009). Glycomics Profiling of Chinese Hamster Ovary Cell Glycosylation Mutants Reveals N-Glycans of a Novel Size and Complexity. Journal of Biological Chemistry. 285(8). 5759–5775. 173 indexed citations
12.
Aguilan, Jennifer T., Subha Sundaram, Edward Nieves, & Pamela Stanley. (2009). Mutational and functional analysis of Large in a novel CHO glycosylation mutant. Glycobiology. 19(9). 971–986. 34 indexed citations
13.
14.
Lee, Jae Hoon, Sung‐Hye Park, Subha Sundaram, et al.. (2003). A Mutation Causing a Reduced Level of Expression of Six β4-Galactosyltransferase Genes Is the Basis of the Lec19 CHO Glycosylation Mutant. Biochemistry. 42(42). 12349–12357. 7 indexed citations
15.
Lee, Jae Hoon, Subha Sundaram, Nancy L. Shaper, T. Shantha Raju, & Pamela Stanley. (2001). Chinese Hamster Ovary (CHO) Cells May Express Six β4-Galactosyltransferases (β4GalTs). Journal of Biological Chemistry. 276(17). 13924–13934. 57 indexed citations
16.
Weinstein, Jasminder, et al.. (1996). A Point Mutation Causes Mistargeting of Golgi GlcNAc-TV in the Lec4A Chinese Hamster Ovary Glycosylation Mutant. Journal of Biological Chemistry. 271(44). 27462–27469. 28 indexed citations
17.
Stanley, Pamela, Subha Sundaram, & Sandra Sallustio. (1991). A subclass of cell surface carbohydrates revealed by a CHO mutant with two glycosylation mutations. Glycobiology. 1(3). 307–314. 24 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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