Rajaraman Krishnan

2.0k total citations
17 papers, 1.7k citations indexed

About

Rajaraman Krishnan is a scholar working on Molecular Biology, Physiology and Neurology. According to data from OpenAlex, Rajaraman Krishnan has authored 17 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 8 papers in Physiology and 5 papers in Neurology. Recurrent topics in Rajaraman Krishnan's work include Prion Diseases and Protein Misfolding (10 papers), Alzheimer's disease research and treatments (8 papers) and Neurological diseases and metabolism (5 papers). Rajaraman Krishnan is often cited by papers focused on Prion Diseases and Protein Misfolding (10 papers), Alzheimer's disease research and treatments (8 papers) and Neurological diseases and metabolism (5 papers). Rajaraman Krishnan collaborates with scholars based in United States, India and Israel. Rajaraman Krishnan's co-authors include Susan Lindquist, Ashok A. Deniz, Samrat Mukhopadhyay, Edward A. Lemke, Bakthisaran Raman, Ch. Mohan Rao, T. Ramakrishna, Jessica L. Goodman, Susan W. Liebman and Tiago F. Outeiro and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Rajaraman Krishnan

17 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rajaraman Krishnan United States 13 1.5k 582 361 255 253 17 1.7k
Tricia R. Serio United States 20 1.7k 1.1× 654 1.1× 458 1.3× 207 0.8× 302 1.2× 36 2.0k
David W. Colby United States 21 2.2k 1.5× 672 1.2× 636 1.8× 73 0.3× 392 1.5× 23 2.6k
Thomas R. Jahn United Kingdom 21 1.6k 1.1× 1.1k 2.0× 158 0.4× 288 1.1× 101 0.4× 31 2.2k
Olga V. Bocharova Russia 25 1.9k 1.3× 648 1.1× 631 1.7× 105 0.4× 586 2.3× 59 2.2k
Rubén Díaz-Avalos United States 15 1.1k 0.8× 277 0.5× 256 0.7× 101 0.4× 223 0.9× 20 1.4k
Shilpa Sambashivan United States 11 1.9k 1.3× 1.4k 2.3× 380 1.1× 390 1.5× 129 0.5× 14 2.7k
Shaoda He United Kingdom 8 1.3k 0.9× 1.1k 1.9× 216 0.6× 177 0.7× 48 0.2× 10 2.0k
Peter Friedhoff Germany 30 2.7k 1.8× 1.5k 2.6× 246 0.7× 222 0.9× 86 0.3× 69 3.6k
Frank Shewmaker United States 33 3.3k 2.3× 841 1.4× 666 1.8× 241 0.9× 462 1.8× 60 3.8k
Douglas M. Fowler United States 7 1.6k 1.1× 1.0k 1.8× 133 0.4× 208 0.8× 96 0.4× 10 2.3k

Countries citing papers authored by Rajaraman Krishnan

Since Specialization
Citations

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

Fields of papers citing papers by Rajaraman Krishnan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Rajaraman Krishnan

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

All Works

17 of 17 papers shown
1.
Kolitz, Sarah, Jason Z. Kim, Jenny Zhang, et al.. (2020). 477 Deep learning to drive COVID-19 rapid drug repurposing. SHILAP Revista de lepidopterología. A293.1–A293. 2 indexed citations
2.
Tsubery, Haim, et al.. (2019). Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif. Journal of Molecular Biology. 431(10). 1920–1939. 3 indexed citations
3.
Levenson, Jonathan M., Jennifer E. Ward, Charlotte Hiu-Yan Chung, et al.. (2019). GAIM fusions are therapeutic candidates for peripheral amyloidosis. Amyloid. 26(sup1). 85–86. 2 indexed citations
4.
Krishnan, Rajaraman, et al.. (2017). Conformation as the Therapeutic Target for Neurodegenerative Diseases. Current Alzheimer Research. 14(4). 393–402. 8 indexed citations
5.
Levenson, Jonathan M., Sally Schroeter, Jenna C. Carroll, et al.. (2016). NPT088 reduces both amyloid‐β and tau pathologies in transgenic mice. Alzheimer s & Dementia Translational Research & Clinical Interventions. 2(3). 141–155. 36 indexed citations
6.
Krishnan, Rajaraman, Haim Tsubery, Sharon Gilead, et al.. (2014). A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies. Journal of Molecular Biology. 426(13). 2500–2519. 44 indexed citations
7.
Krishnan, Rajaraman, Jessica L. Goodman, Samrat Mukhopadhyay, et al.. (2012). Conserved features of intermediates in amyloid assembly determine their benign or toxic states. Proceedings of the National Academy of Sciences. 109(28). 11172–11177. 113 indexed citations
8.
Halfmann, Randal, Simon Alberti, Rajaraman Krishnan, et al.. (2011). Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins. Molecular Cell. 43(1). 72–84. 150 indexed citations
9.
Harmeier, Anja, Andreas C. Woerner, Jessica L. Goodman, et al.. (2011). The cellular prion protein mediates neurotoxic signalling of β‐sheet‐rich conformers independent of prion replication. The EMBO Journal. 30(10). 2057–2070. 195 indexed citations
10.
Wang, Huan, Martin L. Duennwald, Andrew D. Steele, et al.. (2008). Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proceedings of the National Academy of Sciences. 105(20). 7159–7164. 48 indexed citations
11.
Mukhopadhyay, Samrat, Rajaraman Krishnan, Edward A. Lemke, Susan Lindquist, & Ashok A. Deniz. (2007). A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. Proceedings of the National Academy of Sciences. 104(8). 2649–2654. 261 indexed citations
12.
Krishnan, Rajaraman & Susan Lindquist. (2005). Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature. 435(7043). 765–772. 399 indexed citations
13.
Derkatch, Irina L., Susan M. Uptain, Tiago F. Outeiro, et al.. (2004). Effects of Q/N-rich, polyQ, and non-polyQ amyloids on thede novoformation of the [PSI+] prion in yeast and aggregation of Sup35in vitro. Proceedings of the National Academy of Sciences. 101(35). 12934–12939. 182 indexed citations
14.
Krishnan, Rajaraman, Bakthisaran Raman, T. Ramakrishna, & Ch. Mohan Rao. (2001). Interaction of human recombinant αA‐ and αB‐crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation. FEBS Letters. 497(2-3). 118–123. 68 indexed citations
15.
Rao, Ch. Mohan, Bakthisaran Raman, T. Ramakrishna, et al.. (1998). Structural perturbation of α-crystallin and its chaperone-like activity. International Journal of Biological Macromolecules. 22(3-4). 271–281. 51 indexed citations
16.
Krishnan, Rajaraman, Bakthisaran Raman, T. Ramakrishna, & Ch. Mohan Rao. (1998). The Chaperone-like α-Crystallin Forms a Complex Only with the Aggregation-Prone Molten Globule State of α-Lactalbumin. Biochemical and Biophysical Research Communications. 249(3). 917–921. 42 indexed citations
17.
Krishnan, Rajaraman, Bakthisaran Raman, & Ch. Mohan Rao. (1996). Molten-Globule State of Carbonic Anhydrase Binds to the Chaperone-like α-Crystallin. Journal of Biological Chemistry. 271(44). 27595–27600. 98 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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