Harkewal Singh

433 total citations
20 papers, 378 citations indexed

About

Harkewal Singh is a scholar working on Molecular Biology, Materials Chemistry and Immunology. According to data from OpenAlex, Harkewal Singh has authored 20 papers receiving a total of 378 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 11 papers in Materials Chemistry and 3 papers in Immunology. Recurrent topics in Harkewal Singh's work include Enzyme Structure and Function (11 papers), Biochemical and Molecular Research (7 papers) and Protein Structure and Dynamics (3 papers). Harkewal Singh is often cited by papers focused on Enzyme Structure and Function (11 papers), Biochemical and Molecular Research (7 papers) and Protein Structure and Dynamics (3 papers). Harkewal Singh collaborates with scholars based in United States, China and Costa Rica. Harkewal Singh's co-authors include John J. Tanner, Thomas J. Reilly, Donald Becker, Pablo Sobrado, Kent S. Gates, Derrick R. Seiner, Zachary D. Parsons, Jason Labutti, Haiying Zhou and Jonathan P. Schuermann and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Harkewal Singh

20 papers receiving 374 citations

Peers

Harkewal Singh

BIOCH

Zhibing Lu United States

Graeme Thomson United Kingdom

Sophie Rahuel-Clermont France

Christian Frick Switzerland

K. Ida Japan

Chia‐Hui Tai United States

A.E. Oberholzer Switzerland

Ricardo Martí‐Arbona United States

Ivana Leščić Ašler Croatia

Gitte Meriläinen Finland

Zhibing Lu United States

Harkewal Singh

336 ×1.2

150 ×1.3

64 ×1.0

89 ×1.8

BIOCH

66 ×1.7

Citations per year, relative to Harkewal Singh Harkewal Singh (= 1×) peers Zhibing Lu

Countries citing papers authored by Harkewal Singh

Since Specialization

Citations

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

Fields of papers citing papers by Harkewal Singh

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Harkewal Singh

This figure shows the co-authorship network connecting the top 25 collaborators of Harkewal Singh. A scholar is included among the top collaborators of Harkewal 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 Harkewal Singh. Harkewal 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, Harkewal, et al.. (2019). Enzymatic Conversion of RBCs by α-N-Acetylgalactosaminidase from Spirosoma linguale. Enzyme Research. 2019. 1–27. 2 indexed citations

Korasick, David A., et al.. (2017). Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS Journal. 284(18). 3029–3049. 16 indexed citations

Rao, Shubha Gururaja, et al.. (2017). Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein. Scientific Reports. 7(1). 8500–8500. 25 indexed citations

Hillebrand, Roman, et al.. (2017). Covalent Allosteric Inactivation of Protein Tyrosine Phosphatase 1B (PTP1B) by an Inhibitor–Electrophile Conjugate. Biochemistry. 56(14). 2051–2060. 28 indexed citations

Zhu, Weidong, et al.. (2016). Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA. Bioscience Reports. 36(6). 6 indexed citations

Li, Ya, Harkewal Singh, Derrick R. Seiner, et al.. (2015). Inactivation of protein tyrosine phosphatases by dietary isothiocyanates. Bioorganic & Medicinal Chemistry Letters. 25(20). 4549–4552. 15 indexed citations

Singh, Harkewal, et al.. (2015). Crystal structure and tartrate inhibition of Legionella pneumophila histidine acid phosphatase. Archives of Biochemistry and Biophysics. 585. 32–38. 7 indexed citations

Singh, Harkewal, et al.. (2014). Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proceedings of the National Academy of Sciences. 111(9). 3389–3394. 60 indexed citations

Singh, Harkewal, et al.. (2012). Crystal Structures and Small-angle X-ray Scattering Analysis of UDP-galactopyranose Mutase from the Pathogenic Fungus Aspergillus fumigatus. Journal of Biological Chemistry. 287(12). 9041–9051. 33 indexed citations

10.

Singh, Harkewal, et al.. (2012). Identification of the NAD(P)H Binding Site of Eukaryotic UDP-Galactopyranose Mutase. Journal of the American Chemical Society. 134(43). 18132–18138. 24 indexed citations

11.

Singh, Harkewal, et al.. (2012). Proline: Mother Nature's cryoprotectant applied to protein crystallography. Acta Crystallographica Section D Biological Crystallography. 68(8). 1010–1018. 28 indexed citations

12.

Singh, Harkewal, et al.. (2012). Crystal Structures of Trypanosoma cruzi UDP-Galactopyranose Mutase Implicate Flexibility of the Histidine Loop in Enzyme Activation. Biochemistry. 51(24). 4968–4979. 23 indexed citations

13.

Singh, Harkewal, et al.. (2011). Crystal structure and immunogenicity of the class C acid phosphatase from Pasteurella multocida. Archives of Biochemistry and Biophysics. 509(1). 76–81. 5 indexed citations

14.

Singh, Harkewal, Thomas J. Reilly, & John J. Tanner. (2011). Structural basis of the inhibition of class C acid phosphatases by adenosine 5′‐phosphorothioate. FEBS Journal. 278(22). 4374–4381. 3 indexed citations

15.

Singh, Harkewal, Thomas J. Reilly, Michael J. Calcutt, & John J. Tanner. (2011). Expression, purification and crystallization of an atypical class C acid phosphatase fromMycoplasma bovis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(10). 1296–1299. 4 indexed citations

16.

Zhou, Haiying, Harkewal Singh, Zachary D. Parsons, et al.. (2011). The Biological Buffer Bicarbonate/CO₂ Potentiates H₂O₂-Mediated Inactivation of Protein Tyrosine Phosphatases. Journal of the American Chemical Society. 133(40). 15803–15805. 64 indexed citations

17.

Singh, Harkewal, Jonathan P. Schuermann, Thomas J. Reilly, Michael J. Calcutt, & John J. Tanner. (2010). Recognition of Nucleoside Monophosphate Substrates by Haemophilus influenzae Class C Acid Phosphatase. Journal of Molecular Biology. 404(4). 639–649. 13 indexed citations

18.

Singh, Harkewal, Richard L. Felts, Li Ma, et al.. (2009). Expression, purification and crystallization of class C acid phosphatases fromFrancisella tularensisandPasteurella multocida. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(3). 226–231. 3 indexed citations

19.

Singh, Harkewal, Richard L. Felts, Jonathan P. Schuermann, Thomas J. Reilly, & John J. Tanner. (2009). Crystal Structures of the Histidine Acid Phosphatase from Francisella tularensis Provide Insight into Substrate Recognition. Journal of Molecular Biology. 394(5). 893–904. 15 indexed citations

20.

Singh, Harkewal, et al.. (2006). Docking studies of Tau Protein. International MultiConference of Engineers and Computer Scientists. 154–159. 4 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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