Rajeeva Singh

2.9k total citations
43 papers, 2.0k citations indexed

About

Rajeeva Singh is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Oncology. According to data from OpenAlex, Rajeeva Singh has authored 43 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 18 papers in Radiology, Nuclear Medicine and Imaging and 17 papers in Oncology. Recurrent topics in Rajeeva Singh's work include HER2/EGFR in Cancer Research (17 papers), Monoclonal and Polyclonal Antibodies Research (17 papers) and Growth Hormone and Insulin-like Growth Factors (5 papers). Rajeeva Singh is often cited by papers focused on HER2/EGFR in Cancer Research (17 papers), Monoclonal and Polyclonal Antibodies Research (17 papers) and Growth Hormone and Insulin-like Growth Factors (5 papers). Rajeeva Singh collaborates with scholars based in United States, Japan and India. Rajeeva Singh's co-authors include George M. Whitesides, Erin K. Maloney, Wayne C. Widdison, Ravi Chari, Hans K. Erickson, Sharon Wilhelm, Charlene A. Audette, Kathleen R. Whiteman, John M. Lambert and Walter A. Blättler and has published in prestigious journals such as Journal of the American Chemical Society, Cancer Research and Analytical Biochemistry.

In The Last Decade

Rajeeva Singh

41 papers receiving 1.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rajeeva Singh United States 22 940 872 801 247 241 43 2.0k
Rosalyn D. Blumenthal United States 32 810 0.9× 862 1.0× 1.6k 2.0× 145 0.6× 75 0.3× 95 2.9k
Gianfranco De Feo Italy 5 728 0.8× 1.0k 1.2× 207 0.3× 131 0.5× 37 0.2× 9 1.8k
Walter A. Blättler United States 25 2.4k 2.5× 2.1k 2.4× 2.2k 2.8× 306 1.2× 312 1.3× 37 4.5k
Norma O’Donovan Ireland 36 2.3k 2.4× 2.2k 2.6× 561 0.7× 251 1.0× 118 0.5× 116 4.3k
Matilde Olivé United States 13 978 1.0× 1.2k 1.4× 239 0.3× 89 0.4× 68 0.3× 18 2.1k
Steven A. Middleton United States 30 1.2k 1.3× 1.8k 2.1× 308 0.4× 798 3.2× 93 0.4× 63 3.7k
Ana M. Tari United States 31 708 0.8× 1.7k 2.0× 238 0.3× 161 0.7× 29 0.1× 65 2.6k
Katherine R. Kozak United States 24 760 0.8× 965 1.1× 674 0.8× 111 0.4× 22 0.1× 39 2.0k
Frank Loganzo United States 26 1.2k 1.3× 1.2k 1.4× 556 0.7× 425 1.7× 15 0.1× 56 2.4k
D J Chaplin United Kingdom 19 740 0.8× 1.4k 1.6× 495 0.6× 290 1.2× 41 0.2× 33 3.0k

Countries citing papers authored by Rajeeva Singh

Since Specialization
Citations

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

Fields of papers citing papers by Rajeeva Singh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rajeeva Singh

This figure shows the co-authorship network connecting the top 25 collaborators of Rajeeva Singh. A scholar is included among the top collaborators of Rajeeva Singh 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 Rajeeva Singh. Rajeeva Singh 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.
2.
Ali, Amr El‐Hag, Kangwen Deng, Lili Huang, et al.. (2024). Insight Into the Degradation Pathways of an AAV9. Journal of Pharmaceutical Sciences. 113(9). 2967–2973. 4 indexed citations
3.
4.
Miller, Michael L., Nathan Fishkin, Wěi Li, et al.. (2016). A New Class of Antibody–Drug Conjugates with Potent DNA Alkylating Activity. Molecular Cancer Therapeutics. 15(8). 1870–1878. 65 indexed citations
5.
Ab, Olga, Kathleen R. Whiteman, Laura M. Bartle, et al.. (2015). IMGN853, a Folate Receptor-α (FRα)–Targeting Antibody–Drug Conjugate, Exhibits Potent Targeted Antitumor Activity against FRα-Expressing Tumors. Molecular Cancer Therapeutics. 14(7). 1605–1613. 160 indexed citations
6.
Zhao, Robert Y., Sharon Wilhelm, Charlene A. Audette, et al.. (2011). Synthesis and Evaluation of Hydrophilic Linkers for Antibody–Maytansinoid Conjugates. Journal of Medicinal Chemistry. 54(10). 3606–3623. 150 indexed citations
7.
Fishkin, Nathan, Erin K. Maloney, Ravi Chari, & Rajeeva Singh. (2011). A novel pathway for maytansinoid release from thioether linked antibody–drug conjugates (ADCs) under oxidative conditions. Chemical Communications. 47(38). 10752–10752. 38 indexed citations
8.
Kovtun, Yelena, Charlene A. Audette, Michele Mayo, et al.. (2010). Antibody-Maytansinoid Conjugates Designed to Bypass Multidrug Resistance. Cancer Research. 70(6). 2528–2537. 194 indexed citations
9.
Singh, Rajeeva & Hans K. Erickson. (2008). Antibody–Cytotoxic Agent Conjugates: Preparation and Characterization. Methods in molecular biology. 525. 445–467. 30 indexed citations
10.
Bauer, Todd W., Fan Fan, Wenbiao Liu, et al.. (2007). Targeting of Insulin-like Growth Factor-I Receptor with a Monoclonal Antibody Inhibits Growth of Hepatic Metastases from Human Colon Carcinoma in Mice. Annals of Surgical Oncology. 14(10). 2838–2846. 17 indexed citations
11.
Bauer, Todd W., Marya F. McCarty, Jane Wey, et al.. (2004). Therapeutic targeting of the insulin-like growth factor-I receptor (IGF-IR) plus oxaliplatin decreases hepatic growth of human colon cancer. Annals of Surgical Oncology. 11(S2). S65–S65. 1 indexed citations
12.
Singh, Rajeeva, et al.. (2003). Structural stability of human α-thrombin studied by disulfide reduction and scrambling. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1651(1-2). 85–92. 16 indexed citations
13.
Singh, Rajeeva & Erin K. Maloney. (2002). Labeling of Antibodies by in Situ Modification of Thiol Groups Generated from Selenol-Catalyzed Reduction of Native Disulfide Bonds. Analytical Biochemistry. 304(2). 147–156. 18 indexed citations
14.
Singh, Rajeeva & A. G. Appu Rao. (2002). Reductive unfolding and oxidative refolding of a Bowman–Birk inhibitor from horsegram seeds (Dolichos biflorus): evidence for ‘hyperreactive’ disulfide bonds and rate-limiting nature of disulfide isomerization in folding. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1597(2). 280–291. 53 indexed citations
15.
Singh, Rajeeva, L J Kats, Walter A. Blättler, & John M. Lambert. (1996). Formation of N-Substituted 2-Iminothiolanes When Amino Groups in Proteins and Peptides Are Modified by 2-Iminothiolane. Analytical Biochemistry. 236(1). 114–125. 49 indexed citations
16.
Singh, Rajeeva, Walter A. Blättler, & Albert R. Collinson. (1995). [20] Assay for thiols based on reactivation of papain. Methods in enzymology on CD-ROM/Methods in enzymology. 251. 229–237. 23 indexed citations
17.
Singh, Rajeeva & L J Kats. (1995). Catalysis of Reduction of Disulfide by Selenol. Analytical Biochemistry. 232(1). 86–91. 43 indexed citations
18.
Singh, Rajeeva, Guy Lamoureux, Watson J. Lees, & George M. Whitesides. (1995). [14] Reagents for rapid reduction of disulfide bonds. Methods in enzymology on CD-ROM/Methods in enzymology. 251. 167–173. 37 indexed citations
19.
Singh, Rajeeva, W A Blättler, & Albert R. Collinson. (1993). An Amplified Assay for Thiols Based on Reactivation of Papain. Analytical Biochemistry. 213(1). 49–56. 54 indexed citations
20.
Singh, Rajeeva & George M. Whitesides. (1991). A reagent for reduction of disulfide bonds in proteins that reduces disulfide bonds faster than does dithiothreitol. The Journal of Organic Chemistry. 56(7). 2332–2337. 30 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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