Subal Bishayee

1.5k total citations
47 papers, 1.3k citations indexed

About

Subal Bishayee is a scholar working on Molecular Biology, Oncology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Subal Bishayee has authored 47 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 17 papers in Oncology and 16 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Subal Bishayee's work include Glycosylation and Glycoproteins Research (16 papers), Monoclonal and Polyclonal Antibodies Research (16 papers) and HER2/EGFR in Cancer Research (13 papers). Subal Bishayee is often cited by papers focused on Glycosylation and Glycoproteins Research (16 papers), Monoclonal and Polyclonal Antibodies Research (16 papers) and HER2/EGFR in Cancer Research (13 papers). Subal Bishayee collaborates with scholars based in United States, India and Italy. Subal Bishayee's co-authors include Manjusri Das, A.S. Balasubramanian, Subrata Majumdar, Helen Fernandes, J. M. Khire, Stanley Cohen, B.K. Bachhawat, Charles D. Scher, Aruna Basu and Manchala Raghunath and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Molecular and Cellular Biology.

In The Last Decade

Subal Bishayee

47 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
Subal Bishayee United States 18 837 302 247 215 125 47 1.3k
Hidesuke Fukazawa Japan 23 882 1.1× 329 1.1× 122 0.5× 235 1.1× 163 1.3× 50 1.6k
Shinzo Nishi Japan 22 868 1.0× 181 0.6× 123 0.5× 429 2.0× 43 0.3× 57 1.7k
S. Aswanikumar United States 10 909 1.1× 270 0.9× 82 0.3× 440 2.0× 66 0.5× 10 1.5k
Eric S. Day United States 16 766 0.9× 202 0.7× 211 0.9× 395 1.8× 94 0.8× 25 1.4k
Svetlana Bergelson United States 18 1.1k 1.3× 352 1.2× 208 0.8× 209 1.0× 86 0.7× 31 1.5k
James R. Zabrecky United States 9 480 0.6× 251 0.8× 160 0.6× 460 2.1× 66 0.5× 10 1.2k
Takuro Ariga Japan 20 770 0.9× 96 0.3× 143 0.6× 229 1.1× 188 1.5× 88 1.6k
C. Kan United States 8 915 1.1× 161 0.5× 151 0.6× 266 1.2× 44 0.4× 11 1.3k
Deepa Nath India 16 592 0.7× 276 0.9× 102 0.4× 284 1.3× 89 0.7× 48 1.3k
Mario I. Vega United States 26 1.0k 1.2× 510 1.7× 190 0.8× 459 2.1× 69 0.6× 84 2.0k

Countries citing papers authored by Subal Bishayee

Since Specialization
Citations

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

Fields of papers citing papers by Subal Bishayee

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Subal Bishayee

This figure shows the co-authorship network connecting the top 25 collaborators of Subal Bishayee. A scholar is included among the top collaborators of Subal Bishayee 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 Subal Bishayee. Subal Bishayee 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.
Luistro, Leopoldo, James Rosinski, Hongjin Bian, et al.. (2012). Development and characterization of a preclinical ovarian carcinoma model to investigate the mechanism of acquired resistance to trastuzumab. International Journal of Oncology. 41(2). 639–651. 7 indexed citations
2.
Chiara, Federica, Subal Bishayee, Carl‐Henrik Heldin, & Jean‐Baptiste Demoulin. (2004). Autoinhibition of the Platelet-derived Growth Factor β-Receptor Tyrosine Kinase by Its C-terminal Tail. Journal of Biological Chemistry. 279(19). 19732–19738. 46 indexed citations
3.
Luistro, Leopoldo, Christian Tovar, Subal Bishayee, et al.. (2004). Development and characterization of a pre-clinical model of ovarian carcinoma to investigate mechanisms of resistance to the anti-HER2/neu antibody Herceptin™. Cancer Research. 64. 276–276. 1 indexed citations
4.
Bishayee, Subal. (2000). Role of conformational alteration in the epidermal growth factor receptor (EGFR) function. Biochemical Pharmacology. 60(8). 1217–1223. 45 indexed citations
5.
Bishayee, Anupam, Laura Beguinot, & Subal Bishayee. (1999). Phosphorylation of Tyrosine 992, 1068, and 1086 Is Required for Conformational Change of the Human Epidermal Growth Factor Receptor C-Terminal Tail. Molecular Biology of the Cell. 10(3). 525–536. 31 indexed citations
6.
Kanakaraj, Palanisamy, et al.. (1995). Characterization of a Novel Epidermal‐Growth‐Factor‐Receptor‐Related 200‐kDa Tyrosine Kinase in Tumor Cells. European Journal of Biochemistry. 230(3). 951–957. 11 indexed citations
7.
8.
9.
Basu, Aruna, Manchala Raghunath, Subal Bishayee, & Manjusri Das. (1989). Inhibition of Tyrosine Kinase Activity of the Epidermal Growth Factor (EGF) Receptor by a Truncated Receptor Form That Binds to EGF: Role for Interreceptor Interaction in Kinase Regulation. Molecular and Cellular Biology. 9(2). 671–677. 110 indexed citations
10.
Bishayee, Subal, Subrata Majumdar, Charles D. Scher, & Samina Y. Khan. (1988). Characterization of a novel anti-peptide antibody that recognizes a specific conformation of the platelet-derived growth factor receptor.. Molecular and Cellular Biology. 8(9). 3696–3702. 42 indexed citations
11.
Abidi, Fatima, Subal Bishayee, Bimal K. Bachhawat, & Ranjan Bhadra. (1987). Lectin-binding assay by polyethylene glycol 8000. Analytical Biochemistry. 166(2). 257–266. 6 indexed citations
12.
Bishayee, Subal, Alonzo H. Ross, Richard B. Womer, & Charles D. Scher. (1986). Purified human platelet-derived growth factor receptor has ligand-stimulated tyrosine kinase activity.. Proceedings of the National Academy of Sciences. 83(18). 6756–6760. 59 indexed citations
13.
Das, Manjusri, et al.. (1984). Mitogenic activity of the epidermal growth factor receptor after transfer from A431 carcinoma cells to receptor-negative fibroblastic cells.. PubMed. 44(8). 3539–45. 5 indexed citations
14.
Das, Manjusri, et al.. (1983). [49] Spontaneous transfer of exogenous epidermal growth factor receptors into receptor-negative mutant cells. Methods in enzymology on CD-ROM/Methods in enzymology. 98. 555–561. 4 indexed citations
15.
Bachhawat, B.K., et al.. (1981). Fractionation of sialoglycoproteins on an immobilized sialic acid-binding lectin. Analytical Biochemistry. 115(1). 130–137. 7 indexed citations
16.
Bishayee, Subal & Manjusri Das. (1981). Aberrant energy metabolism in a variant epidermal growth factor receptor‐negative fibroblastic cell line. FEBS Letters. 127(2). 241–244. 8 indexed citations
17.
Bachhawat, B.K., et al.. (1981). Further characterization of the sialic acid-binding lectin from the horseshoe crab Carcinoscorpius rotunda cauda. Archives of Biochemistry and Biophysics. 209(1). 325–333. 26 indexed citations
18.
Bishayee, Subal, et al.. (1980). Isolation and characterisation of a sialic acid-binding lectin (carcinoscorpin) from indian horseshoe crab Carcinoscorpius rotunda cauda. Biochimica et Biophysica Acta (BBA) - Protein Structure. 623(1). 89–97. 60 indexed citations
19.
Das, Pijush K. & Subal Bishayee. (1980). Differential localisation of phosphorylated and non‐phosphorylated forms of arylsulfatase A in lysosomes. FEBS Letters. 111(1). 43–46. 7 indexed citations
20.
Bishayee, Subal & Umadas Maitra. (1976). Specificity of cleavage by ribonuclease III. Biochemical and Biophysical Research Communications. 73(2). 306–313. 5 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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