Dhirendra K. Simanshu

5.9k total citations · 1 hit paper
65 papers, 3.8k citations indexed

About

Dhirendra K. Simanshu is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Dhirendra K. Simanshu has authored 65 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 59 papers in Molecular Biology, 18 papers in Materials Chemistry and 16 papers in Cell Biology. Recurrent topics in Dhirendra K. Simanshu's work include Enzyme Structure and Function (18 papers), Protein Kinase Regulation and GTPase Signaling (17 papers) and Lipid Membrane Structure and Behavior (11 papers). Dhirendra K. Simanshu is often cited by papers focused on Enzyme Structure and Function (18 papers), Protein Kinase Regulation and GTPase Signaling (17 papers) and Lipid Membrane Structure and Behavior (11 papers). Dhirendra K. Simanshu collaborates with scholars based in United States, Russia and India. Dhirendra K. Simanshu's co-authors include Frank McCormick, Dwight V. Nissley, Dinshaw J. Patel, Hyeshik Chang, Yuan Tian, Jong‐Eun Park, Inha Heo, Srisathiyanarayanan Dharmaiah, David Jee and V. Narry Kim and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Dhirendra K. Simanshu

64 papers receiving 3.7k citations

Hit Papers

RAS Proteins and Their Regulators in Human Disease 2017 2026 2020 2023 2017 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dhirendra K. Simanshu United States 25 3.1k 603 526 440 341 65 3.8k
Georges Mer United States 32 4.4k 1.4× 403 0.7× 1.1k 2.0× 396 0.9× 205 0.6× 73 4.8k
Alessandro Vindigni United States 33 3.0k 1.0× 590 1.0× 831 1.6× 296 0.7× 322 0.9× 71 3.8k
Haijuan Yang United States 13 4.5k 1.5× 444 0.7× 692 1.3× 451 1.0× 221 0.6× 20 5.1k
Zhenming Zhao United States 13 3.0k 1.0× 490 0.8× 1.1k 2.0× 444 1.0× 174 0.5× 16 3.7k
Andrei Chabes Sweden 37 3.9k 1.3× 566 0.9× 478 0.9× 304 0.7× 308 0.9× 79 4.3k
Amanda Nourse United States 29 3.5k 1.1× 220 0.4× 423 0.8× 497 1.1× 143 0.4× 53 4.0k
Kim Arndt United States 32 3.6k 1.2× 192 0.3× 646 1.2× 617 1.4× 413 1.2× 58 4.6k
James P. Carney United States 20 4.3k 1.4× 794 1.3× 1.3k 2.4× 308 0.7× 386 1.1× 30 4.8k
Jessica S. Williams United States 26 3.0k 1.0× 461 0.8× 510 1.0× 264 0.6× 362 1.1× 46 3.2k
Pavel Janščák Switzerland 36 3.5k 1.1× 717 1.2× 762 1.4× 331 0.8× 484 1.4× 63 3.7k

Countries citing papers authored by Dhirendra K. Simanshu

Since Specialization
Citations

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

Fields of papers citing papers by Dhirendra K. Simanshu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Dhirendra K. Simanshu

This figure shows the co-authorship network connecting the top 25 collaborators of Dhirendra K. Simanshu. A scholar is included among the top collaborators of Dhirendra K. Simanshu 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 Dhirendra K. Simanshu. Dhirendra K. Simanshu 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.
Messing, Simon, Takashi Tsuji, Mitsuhiro Yamaguchi, et al.. (2025). Structural insights into isoform-specific RAS-PI3Kα interactions and the role of RAS in PI3Kα activation. Nature Communications. 16(1). 525–525. 8 indexed citations
2.
Dharmaiah, Srisathiyanarayanan, Daniel A. Bonsor, Albert H. Chan, et al.. (2025). Structural basis for LZTR1 recognition of RAS GTPases for degradation. Science. 389(6765). 1112–1117.
3.
Alexander, Patrick, Albert H. Chan, Monalisa Swain, et al.. (2025). Biophysical and structural analysis of KRAS switch-II pocket inhibitors reveals allele-specific binding constraints. Journal of Biological Chemistry. 301(7). 110331–110331. 1 indexed citations
4.
Whitley, Matthew J., Timothy H. Tran, Ming Yi, et al.. (2024). Comparative analysis of KRAS4a and KRAS4b splice variants reveals distinctive structural and functional properties. Science Advances. 10(7). eadj4137–eadj4137. 14 indexed citations
5.
Finci, Lorenzo I., Mayukh Chakrabarti, Gülçin Gülten, et al.. (2024). Structural dynamics of RAF1-HSP90-CDC37 and HSP90 complexes reveal asymmetric client interactions and key structural elements. Communications Biology. 7(1). 260–260. 8 indexed citations
6.
Yang, Moon Hee, Timothy H. Tran, Christian W. Johnson, et al.. (2023). Allosteric Regulation of Switch-II Domain Controls KRAS Oncogenicity. Cancer Research. 83(19). 3176–3183. 7 indexed citations
7.
Bonsor, Daniel A. & Dhirendra K. Simanshu. (2023). RAS and SHOC2 Roles in RAF Activation and Therapeutic Considerations. PubMed. 8(1). 97–113. 3 indexed citations
8.
Cuevas-Navarro, Antonio, Monalisa Swain, John Columbus, et al.. (2023). RAS-dependent RAF-MAPK hyperactivation by pathogenic RIT1 is a therapeutic target in Noonan syndrome–associated cardiac hypertrophy. Science Advances. 9(28). eadf4766–eadf4766. 12 indexed citations
9.
Chao, Fa-An, Albert H. Chan, Srisathiyanarayanan Dharmaiah, et al.. (2023). Reduced dynamic complexity allows structure elucidation of an excited state of KRASG13D. Communications Biology. 6(1). 594–594. 11 indexed citations
10.
Chao, Fa-An, Srisathiyanarayanan Dharmaiah, Troy Taylor, et al.. (2022). Insights into the Cross Talk between Effector and Allosteric Lobes of KRAS from Methyl Conformational Dynamics. Journal of the American Chemical Society. 144(9). 4196–4205. 17 indexed citations
11.
Bonsor, Daniel A., Patrick Alexander, Kelly Snead, et al.. (2022). Structure of the SHOC2–MRAS–PP1C complex provides insights into RAF activation and Noonan syndrome. Nature Structural & Molecular Biology. 29(10). 966–977. 27 indexed citations
12.
Simanshu, Dhirendra K. & Deborah K. Morrison. (2022). A Structure is Worth a Thousand Words: New Insights for RAS and RAF Regulation. Cancer Discovery. 12(4). 899–912. 41 indexed citations
13.
Dharmaiah, Srisathiyanarayanan, Anatoly Urisman, Matthew Drew, et al.. (2020). Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR. Cell Reports. 32(3). 107909–107909. 43 indexed citations
14.
Goswami, Debanjan, De Chen, Yue Yang, et al.. (2020). Membrane interactions of the globular domain and the hypervariable region of KRAS4b define its unique diffusion behavior. eLife. 9. 21 indexed citations
15.
Nelson, Andrew C., Thomas J. Turbyville, Srisathiyanarayanan Dharmaiah, et al.. (2020). RAS internal tandem duplication disrupts GTPase-activating protein (GAP) binding to activate oncogenic signaling. Journal of Biological Chemistry. 295(28). 9335–9348. 10 indexed citations
16.
Castel, Pau, Alice Cheng, Antonio Cuevas-Navarro, et al.. (2019). RIT1 oncoproteins escape LZTR1-mediated proteolysis. Science. 363(6432). 1226–1230. 57 indexed citations
17.
Hirano, Yoshinori, Yong‐Guang Gao, Daniel Stephenson, et al.. (2019). Structural basis of phosphatidylcholine recognition by the C2–domain of cytosolic phospholipase A2α. eLife. 8. 33 indexed citations
18.
Kim, Boseon, Minju Ha, Luuk Loeff, et al.. (2015). TUT 7 controls the fate of precursor micro RNA s by using three different uridylation mechanisms. The EMBO Journal. 34(13). 1801–1815. 85 indexed citations
19.
Malinina, Lucy, Dhirendra K. Simanshu, Xiuhong Zhai, et al.. (2015). Sphingolipid transfer proteins defined by the GLTP-fold. Quarterly Reviews of Biophysics. 48(3). 281–322. 30 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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