Moorthy Krishnan

1.6k total citations
20 papers, 1.2k citations indexed

About

Moorthy Krishnan is a scholar working on Molecular Biology, Neurology and Surgery. According to data from OpenAlex, Moorthy Krishnan has authored 20 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 9 papers in Neurology and 8 papers in Surgery. Recurrent topics in Moorthy Krishnan's work include Barrier Structure and Function Studies (9 papers), Helicobacter pylori-related gastroenterology studies (8 papers) and Protein Tyrosine Phosphatases (5 papers). Moorthy Krishnan is often cited by papers focused on Barrier Structure and Function Studies (9 papers), Helicobacter pylori-related gastroenterology studies (8 papers) and Protein Tyrosine Phosphatases (5 papers). Moorthy Krishnan collaborates with scholars based in United States, Switzerland and India. Moorthy Krishnan's co-authors include Punita Dhawan, Amar B. Singh, R. Daniel Beauchamp, M. Kay Washington, Ashok Sharma, Declan F. McCole, Ajaz A. Bhat, J. Joshua Smith, Steven A. Eschrich and Jillian L. Pope and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Clinical Investigation and Gastroenterology.

In The Last Decade

Moorthy Krishnan

20 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Moorthy Krishnan United States 17 656 381 236 206 193 20 1.2k
Ruchika Gangwar India 26 867 1.3× 122 0.3× 263 1.1× 107 0.5× 372 1.9× 36 1.4k
Susana Lechuga United States 14 441 0.7× 186 0.5× 92 0.4× 103 0.5× 72 0.4× 25 796
Shida Tavalali Germany 8 484 0.7× 478 1.3× 90 0.4× 102 0.5× 67 0.3× 8 875
Takayuki Kohno Japan 22 737 1.1× 221 0.6× 100 0.4× 42 0.2× 181 0.9× 78 1.3k
Ju Ho Youn South Korea 12 555 0.8× 98 0.3× 294 1.2× 82 0.4× 143 0.7× 15 1.3k
Jiajie Tu China 24 846 1.3× 88 0.2× 293 1.2× 87 0.4× 464 2.4× 61 1.8k
Hamda A. Al‐Naemi Qatar 11 368 0.6× 147 0.4× 120 0.5× 44 0.2× 103 0.5× 25 798
Do Kim United States 14 572 0.9× 91 0.2× 259 1.1× 42 0.2× 133 0.7× 24 1.1k
Ha Young Lee South Korea 23 1.1k 1.6× 61 0.2× 211 0.9× 97 0.5× 180 0.9× 63 1.7k
Shariq Madha United States 12 559 0.9× 48 0.1× 334 1.4× 255 1.2× 104 0.5× 17 1.0k

Countries citing papers authored by Moorthy Krishnan

Since Specialization
Citations

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

Fields of papers citing papers by Moorthy Krishnan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Moorthy Krishnan

This figure shows the co-authorship network connecting the top 25 collaborators of Moorthy Krishnan. A scholar is included among the top collaborators of Moorthy Krishnan 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 Moorthy Krishnan. Moorthy Krishnan 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
2.
Marchelletta, Ronald R., Moorthy Krishnan, Marianne R. Spalinger, et al.. (2021). T cell protein tyrosine phosphatase protects intestinal barrier function by restricting epithelial tight junction remodeling. Journal of Clinical Investigation. 131(17). 29 indexed citations
3.
Spalinger, Marianne R., Anica Sayoc-Becerra, Ali Shawki, et al.. (2020). PTPN2 Regulates Interactions Between Macrophages and Intestinal Epithelial Cells to Promote Intestinal Barrier Function. Gastroenterology. 159(5). 1763–1777.e14. 108 indexed citations
4.
Spalinger, Marianne R., Anica Sayoc-Becerra, Stephanie King, et al.. (2020). The JAK Inhibitor Tofacitinib Rescues Intestinal Barrier Defects Caused by Disrupted Epithelial-macrophage Interactions. Journal of Crohn s and Colitis. 15(3). 471–484. 56 indexed citations
5.
Sayoc-Becerra, Anica, et al.. (2019). The JAK-Inhibitor Tofacitinib Rescues Human Intestinal Epithelial Cells and Colonoids from Cytokine-Induced Barrier Dysfunction. Inflammatory Bowel Diseases. 26(3). 407–422. 82 indexed citations
6.
7.
Krishnan, Moorthy & Declan F. McCole. (2017). T cell protein tyrosine phosphatase prevents STAT1 induction of claudin‐2 expression in intestinal epithelial cells. Annals of the New York Academy of Sciences. 1405(1). 116–130. 22 indexed citations
8.
Krishnan, Moorthy, et al.. (2016). VSL#3 Probiotic Stimulates T-cell Protein Tyrosine Phosphatase–mediated Recovery of IFN-γ–induced Intestinal Epithelial Barrier Defects. Inflammatory Bowel Diseases. 22(12). 2811–2823. 30 indexed citations
9.
Krishnan, Moorthy, et al.. (2015). PTPN2 Gene Deficiency Leads to Increased Epithelial Permeability and Promotes STAT‐1‐dependent Claudin‐2 Expression. The FASEB Journal. 29(S1). 1 indexed citations
10.
11.
Knowles, Byron C., Joseph T. Roland, Moorthy Krishnan, et al.. (2014). Myosin Vb uncoupling from RAB8A and RAB11A elicits microvillus inclusion disease. Journal of Clinical Investigation. 124(7). 2947–2962. 83 indexed citations
12.
Pope, Jillian L., Ajaz A. Bhat, Ashok Sharma, et al.. (2013). Claudin-1 regulates intestinal epithelial homeostasis through the modulation of Notch-signalling. Gut. 63(4). 622–634. 202 indexed citations
13.
Krishnan, Moorthy, Lynne A. Lapierre, Byron C. Knowles, & James R. Goldenring. (2013). Rab25 regulates integrin expression in polarized colonic epithelial cells. Molecular Biology of the Cell. 24(6). 818–831. 33 indexed citations
14.
Sharma, Ashok, Ajaz A. Bhat, Moorthy Krishnan, Amar B. Singh, & Punita Dhawan. (2013). Trichostatin-A modulates claudin-1 mRNA stability through the modulation of Hu antigen R and tristetraprolin in colon cancer cells. Carcinogenesis. 34(11). 2610–2621. 31 indexed citations
15.
Penrose, Harrison M., Ronald R. Marchelletta, Moorthy Krishnan, & Declan F. McCole. (2013). Spermidine Stimulates T Cell Protein-tyrosine Phosphatase-mediated Protection of Intestinal Epithelial Barrier Function. Journal of Biological Chemistry. 288(45). 32651–32662. 25 indexed citations
16.
Bhat, Ajaz A., Ashok Sharma, Jillian L. Pope, et al.. (2012). Caudal Homeobox Protein Cdx-2 Cooperates with Wnt Pathway to Regulate Claudin-1 Expression in Colon Cancer Cells. PLoS ONE. 7(6). e37174–e37174. 58 indexed citations
17.
Singh, Amar B., Ashok Sharma, J. Joshua Smith, et al.. (2011). Claudin-1 Up-regulates the Repressor ZEB-1 to Inhibit E-Cadherin Expression in Colon Cancer Cells. Gastroenterology. 141(6). 2140–2153. 145 indexed citations
18.
Dhawan, Punita, Rizwan Ahmad, Rupesh Chaturvedi, et al.. (2011). Claudin-2 expression increases tumorigenicity of colon cancer cells: role of epidermal growth factor receptor activation. Oncogene. 30(29). 3234–3247. 130 indexed citations
19.
Krishnan, Moorthy, Amar B. Singh, J. Joshua Smith, et al.. (2009). HDAC inhibitors regulate claudin-1 expression in colon cancer cells through modulation of mRNA stability. Oncogene. 29(2). 305–312. 84 indexed citations
20.
Singh, Amar B., Moorthy Krishnan, Pran K. Datta, et al.. (2007). Smad4 Regulates Claudin-1 Expression in a Transforming Growth Factor-β–Independent Manner in Colon Cancer Cells. Cancer Research. 67(4). 1571–1579. 63 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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