Shruti Arya

704 total citations · 1 hit paper
19 papers, 541 citations indexed

About

Shruti Arya is a scholar working on Molecular Biology, Physiology and Food Science. According to data from OpenAlex, Shruti Arya has authored 19 papers receiving a total of 541 indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 9 papers in Physiology and 4 papers in Food Science. Recurrent topics in Shruti Arya's work include Protein Structure and Dynamics (9 papers), Alzheimer's disease research and treatments (8 papers) and Prion Diseases and Protein Misfolding (4 papers). Shruti Arya is often cited by papers focused on Protein Structure and Dynamics (9 papers), Alzheimer's disease research and treatments (8 papers) and Prion Diseases and Protein Misfolding (4 papers). Shruti Arya collaborates with scholars based in India, United States and Canada. Shruti Arya's co-authors include Aimee W. Kao, Carolina Alquézar, Samrat Mukhopadhyay, Mily Bhattacharya, Anindya Datta, Karishma Bhasne, Michael W. Quick, Michael T. Bowers, Avinash Kumar Singh and Arpana Kumari and has published in prestigious journals such as Journal of Neuroscience, The Journal of Physical Chemistry B and Biochemistry.

In The Last Decade

Shruti Arya

16 papers receiving 539 citations

Hit Papers

Tau Post-translational Modifications: Dynamic Transformer... 2021 2026 2022 2024 2021 50 100 150 200

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shruti Arya India 12 349 278 81 72 55 19 541
Anjli Venkateswaran United States 7 305 0.9× 162 0.6× 59 0.7× 84 1.2× 35 0.6× 7 609
Devkee M. Vadukul United Kingdom 13 289 0.8× 297 1.1× 74 0.9× 41 0.6× 60 1.1× 29 555
Dailu Chen United States 7 248 0.7× 283 1.0× 75 0.9× 31 0.4× 25 0.5× 10 389
Sean R. Kundinger United States 6 310 0.9× 284 1.0× 59 0.7× 40 0.6× 16 0.3× 6 468
Clément Despres France 8 263 0.8× 236 0.8× 57 0.7× 50 0.7× 22 0.4× 10 408
Silvia Torrassa Italy 12 463 1.3× 458 1.6× 44 0.5× 94 1.3× 51 0.9× 12 664
Omar M. Kashmer United States 7 197 0.6× 220 0.8× 71 0.9× 50 0.7× 27 0.5× 9 321
Kim Bruggink Netherlands 6 179 0.5× 212 0.8× 35 0.4× 64 0.9× 29 0.5× 8 340
Jason C. Sang United Kingdom 10 196 0.6× 200 0.7× 47 0.6× 48 0.7× 24 0.4× 13 384
Jennifer A. Macdonald United Kingdom 11 332 1.0× 354 1.3× 63 0.8× 47 0.7× 28 0.5× 13 625

Countries citing papers authored by Shruti Arya

Since Specialization
Citations

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

Fields of papers citing papers by Shruti Arya

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shruti Arya

This figure shows the co-authorship network connecting the top 25 collaborators of Shruti Arya. A scholar is included among the top collaborators of Shruti Arya 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 Shruti Arya. Shruti Arya 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
2.
Singh, Navneet, Shruti Arya, & Abhishek Jain. (2024). LEVERAGING eBPF FOR RUNTIME SECURITY. XVIII(1). 397–406.
3.
Arya, Shruti, Giselle M. Knudsen, Kathryn R. Bowles, et al.. (2023). Mutations in α-synuclein, TDP-43 and tau prolong protein half-life through diminished degradation by lysosomal proteases. Molecular Neurodegeneration. 18(1). 29–29. 15 indexed citations
4.
Dogra, Priyanka, Shruti Arya, Avinash Kumar Singh, Anindya Datta, & Samrat Mukhopadhyay. (2022). Conformational and Solvation Dynamics of an Amyloidogenic Intrinsically Disordered Domain of a Melanosomal Protein. The Journal of Physical Chemistry B. 126(2). 443–452. 3 indexed citations
5.
Alquézar, Carolina, Shruti Arya, & Aimee W. Kao. (2021). Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation. Frontiers in Neurology. 11. 595532–595532. 246 indexed citations breakdown →
6.
Bhasne, Karishma, et al.. (2020). Discerning Dynamic Signatures of Membrane-Bound α-Synuclein Using Site-Specific Fluorescence Depolarization Kinetics. The Journal of Physical Chemistry B. 124(5). 708–717. 9 indexed citations
7.
Arya, Shruti, et al.. (2020). Terminal Capping of an Amyloidogenic Tau Fragment Modulates Its Fibrillation Propensity. The Journal of Physical Chemistry B. 124(40). 8772–8783. 22 indexed citations
8.
Arya, Shruti, et al.. (2019). Catalytic Prion-Like Cross-Talk between a Key Alzheimer’s Disease Tau-Fragment R3 and the Type 2 Diabetes Peptide IAPP. ACS Chemical Neuroscience. 10(11). 4757–4765. 23 indexed citations
9.
Arya, Shruti, Karishma Bhasne, Priyanka Dogra, et al.. (2018). Femtosecond Hydration Map of Intrinsically Disordered α-Synuclein. Biophysical Journal. 114(11). 2540–2551. 32 indexed citations
10.
Arya, Shruti, Priyanka Dogra, Neha Jain, & Samrat Mukhopadhyay. (2017). Detergent-induced aggregation of an amyloidogenic intrinsically disordered protein. Journal of Chemical Sciences. 129(12). 1817–1827.
11.
Arya, Shruti & Samrat Mukhopadhyay. (2016). Water in Amyloidogenic Intrinsically Disordered Proteins: Interplay of Conformational Preference and Amyloid Aggregation. Biophysical Journal. 110(3). 398a–398a. 1 indexed citations
12.
Jain, Neha, et al.. (2016). Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins. Biophysical Journal. 111(4). 768–774. 27 indexed citations
13.
Arya, Shruti, et al.. (2016). Water Rearrangements upon Disorder-to-Order Amyloid Transition. The Journal of Physical Chemistry Letters. 7(20). 4105–4110. 33 indexed citations
14.
Arya, Shruti, Nancy Gupta, Rahul Gupta, & Arun Aggarwal. (2016). Constipation and Outcomes of Cecostomy. American Journal of Therapeutics. 23(6). e1867–e1875. 3 indexed citations
15.
Arya, Shruti, et al.. (2016). Confined Water in Amyloid‐Competent Oligomers of the Prion Protein. ChemPhysChem. 17(18). 2804–2807. 13 indexed citations
16.
Arya, Shruti, et al.. (2015). Conformational Switching and Nanoscale Assembly of Human Prion Protein into Polymorphic Amyloids via Structurally Labile Oligomers. Biochemistry. 54(51). 7505–7513. 19 indexed citations
17.
Arya, Shruti, et al.. (2015). Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin. Physical Chemistry Chemical Physics. 17(35). 22862–22871. 29 indexed citations
18.
Arya, Shruti & Samrat Mukhopadhyay. (2014). Ordered Water within the Collapsed Globules of an Amyloidogenic Intrinsically Disordered Protein. The Journal of Physical Chemistry B. 118(31). 9191–9198. 37 indexed citations
19.
Arya, Shruti, et al.. (2004). Intracellular Domains of a Rat Brain GABA Transporter That Govern Transport. Journal of Neuroscience. 24(16). 4082–4087. 29 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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