Appu K. Singh

1.7k total citations
22 papers, 1.1k citations indexed

About

Appu K. Singh is a scholar working on Molecular Biology, Sensory Systems and Cellular and Molecular Neuroscience. According to data from OpenAlex, Appu K. Singh has authored 22 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 11 papers in Sensory Systems and 9 papers in Cellular and Molecular Neuroscience. Recurrent topics in Appu K. Singh's work include Ion Channels and Receptors (11 papers), Ion channel regulation and function (8 papers) and Plant Stress Responses and Tolerance (5 papers). Appu K. Singh is often cited by papers focused on Ion Channels and Receptors (11 papers), Ion channel regulation and function (8 papers) and Plant Stress Responses and Tolerance (5 papers). Appu K. Singh collaborates with scholars based in United States, India and United Kingdom. Appu K. Singh's co-authors include Alexander I. Sobolevsky, Luke L. McGoldrick, Kei Saotome, Maria V. Yelshanskaya, Edward C. Twomey, Robert A. Grassucci, Eleonora Zakharian, Lusine Demirkhanyan, Maria G. Kurnikova and Jared M. Sampson and has published in prestigious journals such as Nature, Science and Nature Communications.

In The Last Decade

Appu K. Singh

22 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Appu K. Singh United States 15 624 618 321 203 168 22 1.1k
Amrita Samanta United States 7 413 0.7× 517 0.8× 179 0.6× 127 0.6× 139 0.8× 10 845
Luke L. McGoldrick United States 11 426 0.7× 430 0.7× 147 0.5× 146 0.7× 119 0.7× 14 880
Kevin W. Huynh United States 9 378 0.6× 450 0.7× 132 0.4× 131 0.6× 118 0.7× 16 708
Kirill D. Nadezhdin Russia 22 879 1.4× 370 0.6× 182 0.6× 179 0.9× 103 0.6× 50 1.4k
William F. Borschel United States 11 405 0.6× 378 0.6× 216 0.7× 101 0.5× 104 0.6× 13 714
Maria V. Yelshanskaya United States 16 923 1.5× 319 0.5× 802 2.5× 150 0.7× 106 0.6× 33 1.4k
Vera Y. Moiseenkova‐Bell United States 25 1.1k 1.7× 1.2k 2.0× 482 1.5× 301 1.5× 305 1.8× 58 2.2k
Melinda M. Diver United States 7 340 0.5× 450 0.7× 256 0.8× 78 0.4× 64 0.4× 8 711
Christina L. Takanishi United States 9 461 0.7× 383 0.6× 183 0.6× 100 0.5× 132 0.8× 10 938

Countries citing papers authored by Appu K. Singh

Since Specialization
Citations

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

Fields of papers citing papers by Appu K. Singh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Appu K. Singh

This figure shows the co-authorship network connecting the top 25 collaborators of Appu K. Singh. A scholar is included among the top collaborators of Appu K. 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 Appu K. Singh. Appu K. 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.
Patil, Dipak N., Serena Pantalone, Yan Cao, et al.. (2023). Structure of the photoreceptor synaptic assembly of the extracellular matrix protein pikachurin with the orphan receptor GPR179. Science Signaling. 16(795). eadd9539–eadd9539. 4 indexed citations
2.
Patil, Dipak N., Shikha Singh, Timothy S. Strutzenberg, et al.. (2022). Cryo-EM structure of human GPR158 receptor coupled to the RGS7-Gβ5 signaling complex. Science. 375(6576). 86–91. 37 indexed citations
3.
Bhardwaj, Rajesh, Arthur Neuberger, Kirill D. Nadezhdin, et al.. (2020). Inactivation-mimicking block of the epithelial calcium channel TRPV6. Science Advances. 6(48). 33 indexed citations
4.
Singh, Appu K., et al.. (2020). Structural Basis of Temperature Sensation by the TRP Channel TRPV3. Biophysical Journal. 118(3). 22a–22a. 16 indexed citations
5.
Singh, Appu K., Luke L. McGoldrick, & Alexander I. Sobolevsky. (2019). Expression, Purification, and Crystallization of the Transient Receptor Potential Channel TRPV6. Methods in molecular biology. 1987. 23–37. 4 indexed citations
6.
McGoldrick, Luke L., Appu K. Singh, Lusine Demirkhanyan, et al.. (2019). Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii. Nature Communications. 10(1). 4180–4180. 25 indexed citations
7.
Singh, Appu K., et al.. (2019). Structural basis of temperature sensation by the TRP channel TRPV3. Nature Structural & Molecular Biology. 26(11). 994–998. 87 indexed citations
8.
Singh, Appu K., Kei Saotome, Luke L. McGoldrick, & Alexander I. Sobolevsky. (2018). Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB. Nature Communications. 9(1). 2465–2465. 87 indexed citations
9.
Singh, Appu K., Luke L. McGoldrick, Edward C. Twomey, & Alexander I. Sobolevsky. (2018). Mechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6. Science Advances. 4(8). eaau6088–eaau6088. 81 indexed citations
10.
Singh, Appu K., Luke L. McGoldrick, & Alexander I. Sobolevsky. (2018). Structure and gating mechanism of the transient receptor potential channel TRPV3. Nature Structural & Molecular Biology. 25(9). 805–813. 148 indexed citations
11.
Singh, Appu K., Luke L. McGoldrick, Kei Saotome, & Alexander I. Sobolevsky. (2018). X-ray crystallography of TRP channels. Channels. 12(1). 137–152. 4 indexed citations
12.
McGoldrick, Luke L., Appu K. Singh, Kei Saotome, et al.. (2017). Opening of the human epithelial calcium channel TRPV6. Nature. 553(7687). 233–237. 157 indexed citations
13.
Singh, Appu K., et al.. (2017). Structural and biochemical characterization of ligand recognition by CysB, the master regulator of sulfate metabolism. Biochimie. 142. 112–124. 18 indexed citations
14.
Singh, Appu K., Kei Saotome, & Alexander I. Sobolevsky. (2017). Swapping of transmembrane domains in the epithelial calcium channel TRPV6. Scientific Reports. 7(1). 10669–10669. 49 indexed citations
15.
Saotome, Kei, Appu K. Singh, Maria V. Yelshanskaya, & Alexander I. Sobolevsky. (2016). Crystal structure of the epithelial calcium channel TRPV6. Nature. 534(7608). 506–511. 177 indexed citations
16.
Yelshanskaya, Maria V., et al.. (2016). Structural Bases of Noncompetitive Inhibition of AMPA-Subtype Ionotropic Glutamate Receptors by Antiepileptic Drugs. Neuron. 91(6). 1305–1315. 102 indexed citations
17.
Yelshanskaya, Maria V., Kei Saotome, Appu K. Singh, & Alexander I. Sobolevsky. (2016). Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors. Scientific Reports. 6(1). 19082–19082. 14 indexed citations
18.
Singh, Appu K., et al.. (2015). Crystal Structure of Fad35R from Mycobacterium tuberculosis H37Rv in the Apo-State. PLoS ONE. 10(5). e0124333–e0124333. 4 indexed citations
19.
Singh, Appu K., et al.. (2014). Molecular Basis of Peptide Recognition in Metallopeptidase Dug1p from Saccharomyces cerevisiae. Biochemistry. 53(50). 7870–7883. 5 indexed citations
20.
Pandya, Vaibhav Kumar, et al.. (2012). Co-Factor Binding Confers Substrate Specificity to Xylose Reductase from Debaryomyces hansenii. PLoS ONE. 7(9). e45525–e45525. 13 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Amrita Samanta Breakdown of academic impact, for papers by Luke L. McGoldrick Breakdown of academic impact, for papers by Kevin W. Huynh Breakdown of academic impact, for papers by Kirill D. Nadezhdin Breakdown of academic impact, for papers by William F. Borschel Breakdown of academic impact, for papers by Maria V. Yelshanskaya Breakdown of academic impact, for papers by Vera Y. Moiseenkova‐Bell Breakdown of academic impact, for papers by Melinda M. Diver Breakdown of academic impact, for papers by Christina L. Takanishi
Rankless by CCL
2026