Mrinal Shekhar

1.7k total citations
30 papers, 938 citations indexed

About

Mrinal Shekhar is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Mrinal Shekhar has authored 30 papers receiving a total of 938 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 7 papers in Spectroscopy and 6 papers in Materials Chemistry. Recurrent topics in Mrinal Shekhar's work include Protein Structure and Dynamics (9 papers), Lipid Membrane Structure and Behavior (5 papers) and Photosynthetic Processes and Mechanisms (5 papers). Mrinal Shekhar is often cited by papers focused on Protein Structure and Dynamics (9 papers), Lipid Membrane Structure and Behavior (5 papers) and Photosynthetic Processes and Mechanisms (5 papers). Mrinal Shekhar collaborates with scholars based in United States, France and United Kingdom. Mrinal Shekhar's co-authors include Emad Tajkhorshid, Eric Gouaux, Wout Oosterheert, Steven Mansoor, Abhishek Singharoy, Argyris Politis, Andy M. Lau, Chloé Martens, Yuhang Wang and Paula J. Booth and has published in prestigious journals such as Nature, Cell and Journal of the American Chemical Society.

In The Last Decade

Mrinal Shekhar

30 papers receiving 934 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mrinal Shekhar United States 17 639 150 149 136 105 30 938
Mark A. Herzik United States 18 843 1.3× 131 0.9× 76 0.5× 29 0.2× 159 1.5× 30 1.3k
Jonathan J. Ruprecht United Kingdom 22 1.7k 2.6× 328 2.2× 40 0.3× 84 0.6× 61 0.6× 30 2.0k
Montserrat Samsó United States 24 1.5k 2.3× 287 1.9× 90 0.6× 132 1.0× 100 1.0× 56 1.8k
Cristina Paulino Netherlands 18 1.1k 1.8× 302 2.0× 33 0.2× 65 0.5× 95 0.9× 30 1.4k
Alisa Glukhova United States 24 2.1k 3.3× 1.0k 6.8× 242 1.6× 193 1.4× 89 0.8× 36 2.5k
Volodymyr M. Korkhov Switzerland 25 1.1k 1.7× 357 2.4× 112 0.8× 198 1.5× 99 0.9× 47 1.7k
Tung‐Chung Mou United States 19 981 1.5× 203 1.4× 82 0.6× 33 0.2× 75 0.7× 40 1.2k
Eriko Nango Japan 20 602 0.9× 159 1.1× 31 0.2× 67 0.5× 364 3.5× 48 963
Marco G. Casarotto Australia 24 1.3k 2.0× 307 2.0× 77 0.5× 67 0.5× 60 0.6× 87 1.7k
A. Batyuk United States 14 496 0.8× 182 1.2× 17 0.1× 44 0.3× 129 1.2× 21 628

Countries citing papers authored by Mrinal Shekhar

Since Specialization
Citations

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

Fields of papers citing papers by Mrinal Shekhar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mrinal Shekhar

This figure shows the co-authorship network connecting the top 25 collaborators of Mrinal Shekhar. A scholar is included among the top collaborators of Mrinal Shekhar 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 Mrinal Shekhar. Mrinal Shekhar 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.
2.
Lee, Sooncheol, Xiaoyun Wu, Colin W. Garvie, et al.. (2022). Velcrin-induced selective cleavage of tRNALeu(TAA) by SLFN12 causes cancer cell death. Nature Chemical Biology. 19(3). 301–310. 25 indexed citations
3.
Shekhar, Mrinal, Zachary Smith, Markus A. Seeliger, & Pratyush Tiwary. (2022). Protein Flexibility and Dissociation Pathway Differentiation Can Explain Onset of Resistance Mutations in Kinases**. Angewandte Chemie International Edition. 61(28). e202200983–e202200983. 28 indexed citations
4.
Shekhar, Mrinal, Genki Terashi, Chitrak Gupta, et al.. (2021). CryoFold: Determining protein structures and data-guided ensembles from cryo-EM density maps. Matter. 4(10). 3195–3216. 29 indexed citations
5.
Gupta, Chitrak, John Vant, Mrinal Shekhar, et al.. (2021). Poor Person’s pH Simulation of Membrane Proteins. Methods in molecular biology. 2315. 197–217. 2 indexed citations
6.
Martens, Chloé, Mrinal Shekhar, Shashank Pant, et al.. (2020). Hydrogen-deuterium exchange mass spectrometry captures distinct dynamics upon substrate and inhibitor binding to a transporter. Nature Communications. 11(1). 6162–6162. 60 indexed citations
7.
Vant, John, Kalyanashis Jana, Mrinal Shekhar, et al.. (2020). Flexible Fitting of Small Molecules into Electron Microscopy Maps Using Molecular Dynamics Simulations with Neural Network Potentials. Journal of Chemical Information and Modeling. 60(5). 2591–2604. 24 indexed citations
8.
Vant, John, Daipayan Sarkar, Chitrak Gupta, et al.. (2020). Molecular Dynamics Flexible Fitting: All You Want to Know About Resolution Exchange. Methods in molecular biology. 2165. 301–315. 3 indexed citations
9.
Dashti, Ali, Ghoncheh Mashayekhi, Mrinal Shekhar, et al.. (2020). Retrieving functional pathways of biomolecules from single-particle snapshots. Nature Communications. 11(1). 4734–4734. 68 indexed citations
10.
Pérez, Alberto, Mrinal Shekhar, Genki Terashi, et al.. (2019). MAINMAST-MELD-MDFF: Denovo Structure-Determination with Data-Guided Molecular Dynamics. Biophysical Journal. 116(3). 287a–288a. 1 indexed citations
11.
Jiang, Tao, Po‐Chao Wen, Zhiyu Zhao, et al.. (2019). Computational Dissection of Membrane Transport at a Microscopic Level. Trends in Biochemical Sciences. 45(3). 202–216. 18 indexed citations
12.
Martens, Chloé, Mrinal Shekhar, Andy M. Lau, Emad Tajkhorshid, & Argyris Politis. (2019). Integrating hydrogen–deuterium exchange mass spectrometry with molecular dynamics simulations to probe lipid-modulated conformational changes in membrane proteins. Nature Protocols. 14(11). 3183–3204. 44 indexed citations
13.
Shekhar, Mrinal, et al.. (2018). Antibiotic Permeation across the Bacterial Outer Membrane Porin. Biophysical Journal. 114(3). 226a–226a. 1 indexed citations
14.
Wen, Po‐Chao, Paween Mahinthichaichan, Tao Jiang, et al.. (2018). Microscopic view of lipids and their diverse biological functions. Current Opinion in Structural Biology. 51. 177–186. 26 indexed citations
15.
Martens, Chloé, Mrinal Shekhar, Antoni J. Borysik, et al.. (2018). Direct protein-lipid interactions shape the conformational landscape of secondary transporters. Nature Communications. 9(1). 4151–4151. 103 indexed citations
16.
Wang, Yuhang, Mrinal Shekhar, Christopher J. Williams, et al.. (2018). Constructing atomic structural models into cryo-EM densities using molecular dynamics – Pros and cons. Journal of Structural Biology. 204(2). 319–328. 8 indexed citations
17.
Chen, Shanshuang, Yan Zhao, Yuhang Wang, et al.. (2018). Activation and Desensitization Mechanism of AMPA Receptor - TARP Complex by cryo-EM. SSRN Electronic Journal. 1 indexed citations
18.
Zeng, Fuxing, Yanbo Chen, Jonathan Remis, et al.. (2017). Structural basis of co-translational quality control by ArfA and RF2 bound to ribosome. Nature. 541(7638). 554–557. 32 indexed citations
19.
Chen, Shanshuang, Yan Zhao, Yuhang Wang, et al.. (2017). Activation and Desensitization Mechanism of AMPA Receptor-TARP Complex by Cryo-EM. Cell. 170(6). 1234–1246.e14. 109 indexed citations
20.
Mansoor, Steven, et al.. (2016). X-ray structures define human P2X3 receptor gating cycle and antagonist action. Nature. 538(7623). 66–71. 205 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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