Puneet Juneja

686 total citations
19 papers, 433 citations indexed

About

Puneet Juneja is a scholar working on Molecular Biology, Pharmacology and Materials Chemistry. According to data from OpenAlex, Puneet Juneja has authored 19 papers receiving a total of 433 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 3 papers in Pharmacology and 3 papers in Materials Chemistry. Recurrent topics in Puneet Juneja's work include Microbial Natural Products and Biosynthesis (2 papers), Neuroblastoma Research and Treatments (2 papers) and RNA modifications and cancer (2 papers). Puneet Juneja is often cited by papers focused on Microbial Natural Products and Biosynthesis (2 papers), Neuroblastoma Research and Treatments (2 papers) and RNA modifications and cancer (2 papers). Puneet Juneja collaborates with scholars based in United States, Germany and Canada. Puneet Juneja's co-authors include Hugh O’Neill, Anne Kuhlee, Eldar Zent, Stefan Raunser, B.U. Klink, Alfred Wittinghofer, Xiaolin Cheng, Utsab R. Shrestha, Jeremy C. Smith and Volker S. Urban and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Puneet Juneja

18 papers receiving 427 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Puneet Juneja United States 11 265 79 62 57 54 19 433
Ana M. Villamil Giraldo Sweden 13 253 1.0× 72 0.9× 56 0.9× 43 0.8× 32 0.6× 23 454
Lipi Thukral India 15 314 1.2× 128 1.6× 28 0.5× 59 1.0× 13 0.2× 37 569
François Berger France 11 204 0.8× 44 0.6× 31 0.5× 27 0.5× 23 0.4× 26 542
Benno Kuropka Germany 13 209 0.8× 29 0.4× 52 0.8× 21 0.4× 13 0.2× 51 477
Jian Kang Singapore 13 451 1.7× 21 0.3× 32 0.5× 40 0.7× 100 1.9× 21 586
Chester J. Provoda United States 10 215 0.8× 53 0.7× 24 0.4× 40 0.7× 10 0.2× 15 378
Nathalie Croteau Canada 8 267 1.0× 124 1.6× 129 2.1× 34 0.6× 87 1.6× 16 466
Guanghui Tang China 11 358 1.4× 37 0.5× 14 0.2× 52 0.9× 27 0.5× 18 524
Igor Tascón Spain 11 271 1.0× 17 0.2× 75 1.2× 21 0.4× 24 0.4× 17 412
Alexander Kolchinsky Russia 18 485 1.8× 30 0.4× 73 1.2× 28 0.5× 43 0.8× 33 771

Countries citing papers authored by Puneet Juneja

Since Specialization
Citations

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

Fields of papers citing papers by Puneet Juneja

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Puneet Juneja

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

All Works

19 of 19 papers shown
1.
Singla, Amika, Ho Yee Joyce Fung, Ran Song, et al.. (2024). Structural basis for Retriever-SNX17 assembly and endosomal sorting. Nature Communications. 15(1). 10193–10193. 5 indexed citations
2.
Peterson, Jake M., et al.. (2024). Structure of the SARS-CoV-2 Frameshift Stimulatory Element with an Upstream Multibranch Loop. Biochemistry. 63(10). 1287–1296. 8 indexed citations
3.
Singla, Amika, Yan Han, Kohei Suzuki, et al.. (2023). Structural organization of the retriever–CCC endosomal recycling complex. Nature Structural & Molecular Biology. 31(6). 910–924. 17 indexed citations
4.
Lin, David Yin-wei, et al.. (2023). Conformational heterogeneity of the BTK PHTH domain drives multiple regulatory states. eLife. 12. 4 indexed citations
5.
Juneja, Puneet, et al.. (2022). PAM binding ensures orientational integration during Cas4-Cas1-Cas2-mediated CRISPR adaptation. Molecular Cell. 82(22). 4353–4367.e6. 9 indexed citations
6.
Blumenthal, Donald, Xiaolin Cheng, Mikolai Fajer, et al.. (2021). Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. Journal of Biological Chemistry. 297(3). 101007–101007. 10 indexed citations
7.
Wang, Fengbin, Leticia C. Beltrán, Chunfu Xu, et al.. (2021). Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials. Nature Communications. 12(1). 407–407. 46 indexed citations
8.
Srinivas, Pooja, et al.. (2021). Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy. Nucleic Acids Research. 49(20). 11800–11809. 9 indexed citations
9.
Imai, Norihiro, C. Denise Okafor, Puneet Juneja, et al.. (2020). Allosteric regulation of thioesterase superfamily member 1 by lipid sensor domain binding fatty acids and lysophosphatidylcholine. Proceedings of the National Academy of Sciences. 117(36). 22080–22089. 15 indexed citations
10.
Cao, Dongdong, et al.. (2020). Cryo-EM structure of the respiratory syncytial virus RNA polymerase. Nature Communications. 11(1). 368–368. 77 indexed citations
11.
Han, Sae‐Won, Rodolfo Ghirlando, Simon Messing, et al.. (2020). Biochemical and structural analyses reveal that the tumor suppressor neurofibromin (NF1) forms a high-affinity dimer. Journal of Biological Chemistry. 295(4). 1105–1119. 27 indexed citations
12.
Venkatakrishnan, Singanallur, Puneet Juneja, & Hugh O’Neill. (2020). Model-based Reconstruction for Single Particle Cryo-Electron Microscopy. arXiv (Cornell University). 1390–1394.
13.
Shrestha, Utsab R., Puneet Juneja, Qiu Zhang, et al.. (2019). Generation of the configurational ensemble of an intrinsically disordered protein from unbiased molecular dynamics simulation. Proceedings of the National Academy of Sciences. 116(41). 20446–20452. 82 indexed citations
14.
Han, Sae‐Won, Rodolfo Ghirlando, Simon Messing, et al.. (2019). Biochemical and structural analyses reveal that the tumor suppressor neurofibromin (NF1) forms a high-affinity dimer. Journal of Biological Chemistry. 295(4). 1105–1119. 32 indexed citations
15.
Klink, B.U., Eldar Zent, Puneet Juneja, et al.. (2017). A recombinant BBSome core complex and how it interacts with ciliary cargo. eLife. 6. 60 indexed citations
16.
Hubrich, Florian, Puneet Juneja, Michael Müller, et al.. (2015). Chorismatase Mechanisms Reveal Fundamentally Different Types of Reaction in a Single Conserved Protein Fold. Journal of the American Chemical Society. 137(34). 11032–11037. 11 indexed citations
17.
Juneja, Puneet, Ashit Rao, Helmut Cölfen, Kay Diederichs, & Wolfram Welte. (2014). Crystallization and preliminary X-ray analysis of the C-type lectin domain of the spicule matrix protein SM50 fromStrongylocentrotus purpuratus. Acta Crystallographica Section F Structural Biology Communications. 70(2). 260–262. 1 indexed citations
18.
Juneja, Puneet, Reinhold Horlacher, Daniel Bertrand, et al.. (2014). An Internally Modulated, Thermostable, pH-sensitive Cys Loop Receptor from the Hydrothermal Vent Worm Alvinella pompejana. Journal of Biological Chemistry. 289(21). 15130–15140. 5 indexed citations
19.
Juneja, Puneet, Florian Hubrich, Kay Diederichs, Wolfram Welte, & Jennifer N. Andexer. (2013). Mechanistic Implications for the Chorismatase FkbO Based on the Crystal Structure. Journal of Molecular Biology. 426(1). 105–115. 15 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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