Tej P. Singh

434 total citations
23 papers, 370 citations indexed

About

Tej P. Singh is a scholar working on Molecular Biology, Nutrition and Dietetics and Immunology. According to data from OpenAlex, Tej P. Singh has authored 23 papers receiving a total of 370 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 11 papers in Nutrition and Dietetics and 6 papers in Immunology. Recurrent topics in Tej P. Singh's work include Infant Nutrition and Health (6 papers), Neutrophil, Myeloperoxidase and Oxidative Mechanisms (5 papers) and Vitamin C and Antioxidants Research (5 papers). Tej P. Singh is often cited by papers focused on Infant Nutrition and Health (6 papers), Neutrophil, Myeloperoxidase and Oxidative Mechanisms (5 papers) and Vitamin C and Antioxidants Research (5 papers). Tej P. Singh collaborates with scholars based in India, Germany and United States. Tej P. Singh's co-authors include Sujata Sharma, Punit Kaur, Sujata Sharma, Christian Betzel, Pravindra Kumar, N. Singh, M. Sinha, Alagiri Srinivasan, Ramasamy P. Kumar and Janesh Kumar and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Tej P. Singh

21 papers receiving 368 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Tej P. Singh India	12	210	84	77	43	39	23	370
Johanna Kallio Finland	8	240 1.1×	62 0.7×	24 0.3×	36 0.8×	66 1.7×	14	544
Yihu Yang China	11	184 0.9×	49 0.6×	32 0.4×	29 0.7×	20 0.5×	15	351
Maddalena Catalano Italy	9	247 1.2×	43 0.5×	37 0.5×	15 0.3×	94 2.4×	10	383
Serena Monaco United Kingdom	12	386 1.8×	66 0.8×	36 0.5×	40 0.9×	74 1.9×	23	498
Andrey Fabricio Ziem Nascimento Brazil	10	206 1.0×	24 0.3×	41 0.5×	43 1.0×	21 0.5×	24	357
Yeon-Ran Kim South Korea	14	278 1.3×	21 0.3×	25 0.3×	75 1.7×	38 1.0×	22	476
Moon Hee Sung South Korea	12	193 0.9×	13 0.2×	59 0.8×	21 0.5×	14 0.4×	20	352
R. Fortin Italy	7	300 1.4×	39 0.5×	13 0.2×	67 1.6×	47 1.2×	10	512
Dominic A. Colosimo United States	7	263 1.3×	15 0.2×	74 1.0×	17 0.4×	56 1.4×	8	452
Tao Cui United States	11	424 2.0×	17 0.2×	26 0.3×	54 1.3×	30 0.8×	19	639

Countries citing papers authored by Tej P. Singh

Since Specialization

Citations

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

Fields of papers citing papers by Tej P. Singh

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tej P. Singh

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

All Works

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20 of 20 papers shown

Singh, Tej P., et al.. (2025). Unveiling Natural Power: Morin and Myricetin as Potent Inhibitors of Histidinol-Phosphate Aminotransferase in Drug-Resistant Acinetobacter baumannii. ACS Omega. 10(8). 7920–7936.

Singh, Tej P., et al.. (2025). Disruption of histidine biosynthesis in Acinetobacter baumannii by Tubuloside B from Cistanche tubulosa. Computers in Biology and Medicine. 198(Pt A). 111174–111174.

Viswanathan, V., et al.. (2021). Structure of Yak Lactoperoxidase at 1.55 Å Resolution. The Protein Journal. 40(1). 8–18. 5 indexed citations

Viswanathan, V., et al.. (2021). A Peptide Bond from the Inter-lobe Segment in the Bilobal Lactoferrin Acts as a Preferred Site for Cleavage for Serine Proteases to Generate the Perfect C-lobe: Structure of the Pepsin Hydrolyzed Lactoferrin C-lobe at 2.28 Å Resolution. The Protein Journal. 40(6). 857–866. 6 indexed citations

Sharma, Pradeep, et al.. (2021). Structure of a ternary complex of lactoperoxidase with iodide and hydrogen peroxide at 1.77 Å resolution. Journal of Inorganic Biochemistry. 220. 111461–111461. 10 indexed citations

Kaur, Punit, et al.. (2017). Structural basis of activation of mammalian heme peroxidases. Progress in Biophysics and Molecular Biology. 133. 49–55. 22 indexed citations

Kaur, Punit, et al.. (2016). Structure of bovine lactoperoxidase with a partially linked heme moiety at 1.98Å resolution. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865(3). 329–335. 16 indexed citations

Kaushik, Sanket, N. Singh, Avinash Singh, et al.. (2013). The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii. PLoS ONE. 8(7). e67547–e67547. 25 indexed citations

Kaushik, Sanket, Avinash Singh, M. Sinha, et al.. (2013). Cloning, expression, crystallization and preliminary structural studies of dihydrodipicolinate reductase fromAcinetobacter baumannii. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(6). 653–656. 2 indexed citations

10.

Kushwaha, G.S., et al.. (2012). Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824(4). 679–691. 18 indexed citations

11.

Kumar, Sanjit, N. Singh, M. Sinha, et al.. (2010). Crystal structure determination and inhibition studies of a novel xylanase and α‐amylase inhibitor protein (XAIP) from Scadoxus multiflorus. FEBS Journal. 277(13). 2868–2882. 14 indexed citations

12.

Singh, Amit Kumar, Ramasamy P. Kumar, N. Singh, et al.. (2009). Mode of Binding of the Tuberculosis Prodrug Isoniazid to Heme Peroxidases. Journal of Biological Chemistry. 285(2). 1569–1576. 41 indexed citations

13.

Singh, N., Ramasamy P. Kumar, Sanjit Kumar, et al.. (2009). Simultaneous inhibition of anti‐coagulation and inflammation: crystal structure of phospholipase A₂ complexed with indomethacin at 1.4 Å resolution reveals the presence of the new common ligand‐binding site. Journal of Molecular Recognition. 22(6). 437–445. 28 indexed citations

14.

Kumar, Janesh, A.S. Ethayathulla, Devendra B. Srivastava, et al.. (2007). Carbohydrate-binding properties of goat secretory glycoprotein (SPG-40) and its functional implications: structures of the native glycoprotein and its four complexes with chitin-like oligosaccharides. Acta Crystallographica Section D Biological Crystallography. 63(4). 437–446. 11 indexed citations

15.

Kumar, Janesh, A.S. Ethayathulla, Devendra B. Srivastava, et al.. (2006). Structure of a bovine secretory signalling glycoprotein (SPC-40) at 2.1 Å resolution. Acta Crystallographica Section D Biological Crystallography. 62(9). 953–963. 16 indexed citations

16.

Sharma, Sujata, J. Jasti, Janesh Kumar, Ashok Kumar Mohanty, & Tej P. Singh. (2003). Crystal Structure of a Proteolytically Generated Functional Monoferric C-lobe of Bovine Lactoferrin at 1.9Å Resolution. Journal of Molecular Biology. 331(2). 485–496. 18 indexed citations

17.

Sharma, Sujata, Pravindra Kumar, Christian Betzel, & Tej P. Singh. (2001). Structure and function of proteins involved in milk allergies. Journal of Chromatography B Biomedical Sciences and Applications. 756(1-2). 183–187. 72 indexed citations

18.

Sharma, Sujata, Subramanian Karthikeyan, Ch. Betzel, & Tej P. Singh. (1999). Isolation, purification, crystallization and preliminary X-ray analysis of β₁-bungarotoxin fromBungarus caeruleus(Indian common krait). Acta Crystallographica Section D Biological Crystallography. 55(5). 1093–1094. 10 indexed citations

19.

Dey, Sharmistha, Shome Nath Mitra, & Tej P. Singh. (1996). Design of peptides: synthesis, crystal structure and molecular conformation of N‐Boc‐L‐Val‐δPhe‐L‐Ile‐OCH₃. International journal of peptide & protein research. 48(2). 123–128. 20 indexed citations

20.

Saxena, Ajay K., Tej P. Singh, Κ. Peters, S. Fittkau, & Christian Betzel. (1996). Strategy to design peptide inhibitors: Structure of a complex of proteinase K with a designed octapeptide inhibitor N‐Ac‐Pro‐Ala‐Pro‐Phe‐DAla‐Ala‐Ala‐Ala‐NH₂ at 2.5 Å resolution. Protein Science. 5(12). 2453–2458. 16 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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