Srikanth Dakoji

1.7k total citations
16 papers, 1.4k citations indexed

About

Srikanth Dakoji is a scholar working on Molecular Biology, Clinical Biochemistry and Cell Biology. According to data from OpenAlex, Srikanth Dakoji has authored 16 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 4 papers in Clinical Biochemistry and 4 papers in Cell Biology. Recurrent topics in Srikanth Dakoji's work include Metabolism and Genetic Disorders (4 papers), Enzyme Structure and Function (4 papers) and Neuroscience and Neuropharmacology Research (3 papers). Srikanth Dakoji is often cited by papers focused on Metabolism and Genetic Disorders (4 papers), Enzyme Structure and Function (4 papers) and Neuroscience and Neuropharmacology Research (3 papers). Srikanth Dakoji collaborates with scholars based in United States, Canada and Singapore. Srikanth Dakoji's co-authors include David S. Bredt, Roger A. Nicoll, Eric Schnell, Neal Sweeney, Qiang Zhou, Oliver Prange, Olav Olsen, Wendell A. Lim, Aaron W. McGee and Kenneth E. Prehoda and has published in prestigious journals such as Cell, Journal of the American Chemical Society and Annual Review of Biochemistry.

In The Last Decade

Srikanth Dakoji

16 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Srikanth Dakoji United States 13 903 599 442 109 94 16 1.4k
Tetsuya Takano Japan 18 788 0.9× 544 0.9× 391 0.9× 88 0.8× 146 1.6× 31 1.6k
Pamela Arstikaitis Canada 11 1.1k 1.2× 638 1.1× 515 1.2× 64 0.6× 128 1.4× 12 1.5k
Renaldo C. Drisdel United States 18 1.6k 1.8× 680 1.1× 485 1.1× 69 0.6× 217 2.3× 19 2.0k
Gabby Rudenko United States 22 771 0.9× 449 0.7× 271 0.6× 67 0.6× 149 1.6× 35 1.4k
Pascal Kessler France 21 924 1.0× 368 0.6× 279 0.6× 39 0.4× 165 1.8× 32 1.6k
Roman Urfer United States 22 1.1k 1.3× 726 1.2× 201 0.5× 176 1.6× 187 2.0× 28 1.8k
Debra A. Brickey United States 12 1.6k 1.8× 886 1.5× 317 0.7× 98 0.9× 179 1.9× 18 2.1k
Elise F. Stanley Canada 18 965 1.1× 656 1.1× 373 0.8× 96 0.9× 234 2.5× 34 1.6k
Beatriz Alvarez‐Castelao Spain 18 767 0.8× 271 0.5× 305 0.7× 68 0.6× 121 1.3× 30 1.1k
Brian J. Hillier United States 10 881 1.0× 401 0.7× 274 0.6× 80 0.7× 271 2.9× 15 1.3k

Countries citing papers authored by Srikanth Dakoji

Since Specialization
Citations

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

Fields of papers citing papers by Srikanth Dakoji

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Srikanth Dakoji

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

All Works

16 of 16 papers shown
1.
Kennedy, Bruce C., et al.. (2016). Deletion of novel protein TMEM35 alters stress-related functions and impairs long-term memory in mice. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 311(1). R166–R178. 13 indexed citations
2.
Tran, Phu V., et al.. (2013). Fetal iron deficiency alters the proteome of adult rat hippocampal synaptosomes. American Journal of Physiology-Regulatory, Integrative and Comparative Physiology. 305(11). R1297–R1306. 26 indexed citations
3.
Santarius, Thomas, Srikanth Dakoji, Fardad T. Afshari, et al.. (2012). Isolated hypoglossal schwannoma in a 9-year-old child. Journal of Neurosurgery Pediatrics. 10(2). 130–133. 12 indexed citations
4.
Reese, Michael L., Srikanth Dakoji, David S. Bredt, & Volker Dötsch. (2007). The guanylate kinase domain of the MAGUK PSD-95 binds dynamically to a conserved motif in MAP1a. Nature Structural & Molecular Biology. 14(2). 155–163. 39 indexed citations
5.
Dakoji, Srikanth, et al.. (2005). MEMBRANE-ASSOCIATED GUANYLATE KINASES REGULATE ADHESION AND PLASTICITY AT CELL JUNCTIONS. Annual Review of Biochemistry. 74(1). 219–245. 379 indexed citations
6.
Dakoji, Srikanth, Susumu Tomita, Siavash Karimzadegan, Roger A. Nicoll, & David S. Bredt. (2003). Interaction of transmembrane AMPA receptor regulatory proteins with multiple membrane associated guanylate kinases. Neuropharmacology. 45(6). 849–856. 82 indexed citations
7.
Schnell, Eric, Srikanth Dakoji, Neal Sweeney, et al.. (2002). Synaptic Strength Regulated by Palmitate Cycling on PSD-95. Cell. 108(6). 849–863. 471 indexed citations
8.
Agnihotri, Gautam, Shouming He, Lin Hong, et al.. (2002). A Revised Mechanism for the Inactivation of Bovine Liver Enoyl-CoA Hydratase by (Methylenecyclopropyl)formyl-CoA Based on Unexpected Results with the C114A Mutant. Biochemistry. 41(6). 1843–1852. 12 indexed citations
9.
McGee, Aaron W., Srikanth Dakoji, Olav Olsen, et al.. (2001). Structure of the SH3-Guanylate Kinase Module from PSD-95 Suggests a Mechanism for Regulated Assembly of MAGUK Scaffolding Proteins. Molecular Cell. 8(6). 1291–1301. 196 indexed citations
10.
Dakoji, Srikanth, Ding Li, Gautam Agnihotri, Huiqiang Zhou, & Hung‐wen Liu. (2001). Studies on the Inactivation of Bovine Liver Enoyl-CoA Hydratase by (Methylenecyclopropyl)formyl-CoA:  Elucidation of the Inactivation Mechanism and Identification of Cysteine-114 as the Entrapped Nucleophile. Journal of the American Chemical Society. 123(40). 9749–9759. 21 indexed citations
12.
Li, Ding, et al.. (1998). Spiropentylacetyl-CoA, A Mechanism-Based Inactivator of Acyl-CoA Dehydrogenases. Journal of the American Chemical Society. 120(9). 2008–2017. 26 indexed citations
13.
Dakoji, Srikanth, Injae Shin, K.P. Battaile, Jerry Vockley, & Hung‐wen Liu. (1997). Redesigning the active-site of an acyl-CoA dehydrogenase: new evidence supporting a one-base mechanism. Bioorganic & Medicinal Chemistry. 5(12). 2157–2164. 6 indexed citations
14.
Ghosh, Soumitra S., et al.. (1996). Properties of analogues of an intermediate in the process of mechanism-based inactivation of carboxypeptidase A. Bioorganic & Medicinal Chemistry. 4(9). 1487–1492. 3 indexed citations
15.
Dakoji, Srikanth, Injae Shin, Donald Becker, Marian T. Stankovich, & Hung‐wen Liu. (1996). Studies of Acyl-CoA Dehydrogenase Catalyzed Allylic Isomerization:  A One-Base or Two-Base Mechanism?. Journal of the American Chemical Society. 118(45). 10971–10979. 15 indexed citations
16.
Tanaka, Yasuhiro, et al.. (1994). Conscripting the Active-Site Zinc Ion in Carboxypeptidase A in Inactivation Chemistry by a New Type of Irreversible Enzyme Inactivator. Journal of the American Chemical Society. 116(17). 7475–7480. 22 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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