Leela Shrestha

1.3k total citations
11 papers, 701 citations indexed

About

Leela Shrestha is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Leela Shrestha has authored 11 papers receiving a total of 701 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 2 papers in Cell Biology and 1 paper in Organic Chemistry. Recurrent topics in Leela Shrestha's work include Glycosylation and Glycoproteins Research (2 papers), Biochemical and Molecular Research (2 papers) and Glycogen Storage Diseases and Myoclonus (1 paper). Leela Shrestha is often cited by papers focused on Glycosylation and Glycoproteins Research (2 papers), Biochemical and Molecular Research (2 papers) and Glycogen Storage Diseases and Myoclonus (1 paper). Leela Shrestha collaborates with scholars based in United Kingdom, Canada and Czechia. Leela Shrestha's co-authors include N. Burgess-Brown, Elisabeth P. Carpenter, A.C.W. Pike, C.A. Shintre, G. Berridge, Shubhashish Mukhopadhyay, C. Bountra, Phillip J. Stansfeld, F. von Delft and Wyatt W. Yue and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Leela Shrestha

11 papers receiving 699 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Leela Shrestha United Kingdom 10 429 146 109 56 56 11 701
C.A. Shintre United Kingdom 6 272 0.6× 169 1.2× 93 0.9× 30 0.5× 66 1.2× 6 456
Paul W. Doetsch United States 15 1.0k 2.4× 113 0.8× 91 0.8× 40 0.7× 27 0.5× 29 1.3k
Ralf‐Jürgen Kuban Germany 12 420 1.0× 91 0.6× 48 0.4× 38 0.7× 13 0.2× 20 646
Shengchen Lin China 13 371 0.9× 150 1.0× 37 0.3× 103 1.8× 19 0.3× 17 678
Carlotta Zamparelli Italy 18 544 1.3× 97 0.7× 35 0.3× 136 2.4× 100 1.8× 30 803
Yoshio Kodera Japan 16 448 1.0× 102 0.7× 64 0.6× 57 1.0× 21 0.4× 33 768
Yifei Zhu China 17 430 1.0× 133 0.9× 25 0.2× 34 0.6× 16 0.3× 46 787
P. Mahajan United Kingdom 13 562 1.3× 103 0.7× 134 1.2× 78 1.4× 13 0.2× 26 775
Luba A. Aleksandrov United States 20 938 2.2× 292 2.0× 149 1.4× 75 1.3× 109 1.9× 29 1.5k
Christina R. Kahl Germany 7 402 0.9× 77 0.5× 29 0.3× 87 1.6× 21 0.4× 11 633

Countries citing papers authored by Leela Shrestha

Since Specialization
Citations

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

Fields of papers citing papers by Leela Shrestha

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Leela Shrestha

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

All Works

11 of 11 papers shown
1.
McCorvie, Thomas J., Paula M. Loria, Meihua Tu, et al.. (2022). Molecular basis for the regulation of human glycogen synthase by phosphorylation and glucose-6-phosphate. Nature Structural & Molecular Biology. 29(7). 628–638. 17 indexed citations
2.
Pike, A.C.W., Simon R. Bushell, Andrew Quigley, et al.. (2021). The structural basis of fatty acid elongation by the ELOVL elongases. Nature Structural & Molecular Biology. 28(6). 512–520. 53 indexed citations
3.
Rödström, Karin E. J., Aytuğ K. Kiper, Wei Zhang, et al.. (2020). A lower X-gate in TASK channels traps inhibitors within the vestibule. Nature. 582(7812). 443–447. 54 indexed citations
4.
McCorvie, Thomas J., J. Kopec, Ángel L. Pey, et al.. (2016). Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase. Human Molecular Genetics. 25(11). 2234–2244. 37 indexed citations
5.
Grieben, Mariana, A.C.W. Pike, C.A. Shintre, et al.. (2016). Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2). Nature Structural & Molecular Biology. 24(2). 114–122. 140 indexed citations
6.
Montgomery, Anna B., J. Kopec, Leela Shrestha, et al.. (2015). Crystal structure of Porphyromonas gingivalis peptidylarginine deiminase: implications for autoimmunity in rheumatoid arthritis. Annals of the Rheumatic Diseases. 75(6). 1255–1261. 65 indexed citations
7.
Guetzoyan, Lucie, Richard J. Ingham, Nikzad Nikbin, et al.. (2014). Machine-assisted synthesis of modulators of the histone reader BRD9 using flow methods of chemistry and frontal affinity chromatography. MedChemComm. 5(4). 540–546. 37 indexed citations
8.
Chalk, R., G. Berridge, Leela Shrestha, et al.. (2014). High-Throughput Mass Spectrometry Applied to Structural Genomics. SHILAP Revista de lepidopterología. 1(4). 159–175. 2 indexed citations
9.
Quigley, Andrew, Yin Yao Dong, A.C.W. Pike, et al.. (2013). The Structural Basis of ZMPSTE24-Dependent Laminopathies. Science. 339(6127). 1604–1607. 79 indexed citations
10.
Shintre, C.A., A.C.W. Pike, Qiuhong Li, et al.. (2013). Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states. Proceedings of the National Academy of Sciences. 110(24). 9710–9715. 195 indexed citations
11.
Elkins, Jonathan M., C. Gileadi, Leela Shrestha, et al.. (2010). Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms. Protein Science. 19(4). 731–741. 22 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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