Shachi Gosavi

1.8k total citations
45 papers, 1.4k citations indexed

About

Shachi Gosavi is a scholar working on Molecular Biology, Materials Chemistry and Ecology. According to data from OpenAlex, Shachi Gosavi has authored 45 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 24 papers in Materials Chemistry and 5 papers in Ecology. Recurrent topics in Shachi Gosavi's work include Protein Structure and Dynamics (32 papers), Enzyme Structure and Function (23 papers) and RNA and protein synthesis mechanisms (22 papers). Shachi Gosavi is often cited by papers focused on Protein Structure and Dynamics (32 papers), Enzyme Structure and Function (23 papers) and RNA and protein synthesis mechanisms (22 papers). Shachi Gosavi collaborates with scholars based in India, United States and Canada. Shachi Gosavi's co-authors include José N. Onuchic, Paul C. Whitford, R. A. Marcus, Patricia A. Jennings, Jeffrey K. Noel, Kevin Y. Sanbonmatsu, Alexander Schug, L. L. Chavez, Shilpa Yadahalli and Pietro Faccioli and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Shachi Gosavi

43 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shachi Gosavi India 19 1.1k 617 141 136 108 45 1.4k
Rochelle D. Ahmed United Kingdom 22 918 0.8× 273 0.4× 211 1.5× 77 0.6× 89 0.8× 68 1.3k
Thomas Le Saux France 29 1.1k 1.0× 791 1.3× 111 0.8× 36 0.3× 55 0.5× 77 2.5k
Claudia Antoni Chile 14 660 0.6× 258 0.4× 256 1.8× 198 1.5× 44 0.4× 22 1.3k
Takanori Uzawa Japan 20 1.3k 1.1× 339 0.5× 164 1.2× 98 0.7× 79 0.7× 47 1.5k
Gautam Basu India 26 1.3k 1.2× 340 0.6× 66 0.5× 22 0.2× 94 0.9× 81 1.9k
Christophe Danelon Netherlands 24 1.5k 1.3× 204 0.3× 100 0.7× 42 0.3× 121 1.1× 43 2.1k
Hannes Neuweiler Germany 25 1.7k 1.5× 634 1.0× 157 1.1× 34 0.3× 297 2.8× 42 2.3k
Abhishek Singharoy United States 23 1.0k 0.9× 294 0.5× 46 0.3× 20 0.1× 204 1.9× 76 1.5k
Tsutomu Mikawa Japan 22 1.1k 1.0× 222 0.4× 163 1.2× 61 0.4× 19 0.2× 58 1.5k
Zhen Xia United States 19 900 0.8× 405 0.7× 152 1.1× 22 0.2× 288 2.7× 29 1.8k

Countries citing papers authored by Shachi Gosavi

Since Specialization
Citations

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

Fields of papers citing papers by Shachi Gosavi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shachi Gosavi

This figure shows the co-authorship network connecting the top 25 collaborators of Shachi Gosavi. A scholar is included among the top collaborators of Shachi Gosavi 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 Shachi Gosavi. Shachi Gosavi 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.
Gosavi, Shachi, et al.. (2023). Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity. Frontiers in Molecular Biosciences. 10. 1021733–1021733.
2.
Gosavi, Shachi, et al.. (2022). The diversity of protein-protein interaction interfaces within T=3 icosahedral viral capsids. Frontiers in Molecular Biosciences. 9. 967877–967877. 1 indexed citations
3.
Gosavi, Shachi, et al.. (2020). The Molecular Mechanism of Domain Swapping of the C-Terminal Domain of the SARS-Coronavirus Main Protease. Biophysical Journal. 120(3). 504–516. 5 indexed citations
4.
Gosavi, Shachi, et al.. (2020). Structure dictates the mechanism of ligand recognition in the histidine and maltose binding proteins. SHILAP Revista de lepidopterología. 2. 180–190. 1 indexed citations
5.
Gershenson, Anne, Shachi Gosavi, Pietro Faccioli, & Patrick L. Wintrode. (2019). Successes and challenges in simulating the folding of large proteins. Journal of Biological Chemistry. 295(1). 15–33. 55 indexed citations
6.
Udgaonkar, Jayant B., et al.. (2019). A five-residue motif for the design of domain swapping in proteins. Nature Communications. 10(1). 452–452. 44 indexed citations
7.
Gosavi, Shachi, et al.. (2018). The Sensitivity of Computational Protein Folding to Contact Map Perturbations: The Case of Ubiquitin Folding and Function. The Journal of Physical Chemistry B. 122(49). 11497–11507. 7 indexed citations
8.
Gosavi, Shachi, et al.. (2018). On the folding of a structurally complex protein to its metastable active state. Proceedings of the National Academy of Sciences. 115(9). 1998–2003. 18 indexed citations
9.
Gosavi, Shachi, et al.. (2017). Understanding Protein Domain-Swapping in the Cystatin-Monellin Family of Proteins. Biophysical Journal. 112(3). 168a–168a. 1 indexed citations
10.
Yadahalli, Shilpa, Jianguo Li, David P. Lane, Shachi Gosavi, & Chandra Verma. (2017). Characterizing the conformational landscape of MDM2-binding p53 peptides using Molecular Dynamics simulations. Scientific Reports. 7(1). 15600–15600. 14 indexed citations
11.
Yadahalli, Shilpa & Shachi Gosavi. (2017). Packing energetics determine the folding routes of the RNase-H proteins. Physical Chemistry Chemical Physics. 19(13). 9164–9173. 3 indexed citations
12.
Gosavi, Shachi, et al.. (2016). Using the folding landscapes of proteins to understand protein function. Current Opinion in Structural Biology. 36. 67–74. 34 indexed citations
13.
Desikan, Rajat, et al.. (2016). Capturing the Membrane-Triggered Conformational Transition of an α-Helical Pore-Forming Toxin. The Journal of Physical Chemistry B. 120(47). 12064–12078. 27 indexed citations
14.
Gosavi, Shachi, et al.. (2016). Understanding protein domain-swapping using structure-based models of protein folding. Progress in Biophysics and Molecular Biology. 128. 113–120. 43 indexed citations
15.
Broom, Aron, Ke Xia, Kyle Trainor, et al.. (2015). Designed protein reveals structural determinants of extreme kinetic stability. Proceedings of the National Academy of Sciences. 112(47). 14605–14610. 30 indexed citations
16.
Yadahalli, Shilpa & Shachi Gosavi. (2015). Functionally Relevant Specific Packing Can Determine Protein Folding Routes. Journal of Molecular Biology. 428(2). 509–521. 12 indexed citations
17.
Gosavi, Shachi. (2013). Understanding the Folding-Function Tradeoff in Proteins. PLoS ONE. 8(4). e61222–e61222. 27 indexed citations
18.
Whitford, Paul C., Jeffrey K. Noel, Shachi Gosavi, et al.. (2008). An all‐atom structure‐based potential for proteins: Bridging minimal models with all‐atom empirical forcefields. Proteins Structure Function and Bioinformatics. 75(2). 430–441. 297 indexed citations
19.
Whitford, Paul C., Shachi Gosavi, & José N. Onuchic. (2007). Conformational Transitions in Adenylate Kinase. Journal of Biological Chemistry. 283(4). 2042–2048. 97 indexed citations
20.
Gosavi, Shachi, L. L. Chavez, Patricia A. Jennings, & José N. Onuchic. (2005). Topological Frustration and the Folding of Interleukin-1β. Journal of Molecular Biology. 357(3). 986–996. 129 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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