Sriram Subramaniam

19.9k total citations · 6 hit papers
200 papers, 14.2k citations indexed

About

Sriram Subramaniam is a scholar working on Molecular Biology, Structural Biology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Sriram Subramaniam has authored 200 papers receiving a total of 14.2k indexed citations (citations by other indexed papers that have themselves been cited), including 118 papers in Molecular Biology, 57 papers in Structural Biology and 38 papers in Cellular and Molecular Neuroscience. Recurrent topics in Sriram Subramaniam's work include Advanced Electron Microscopy Techniques and Applications (57 papers), Photoreceptor and optogenetics research (32 papers) and Neuroscience and Neuropharmacology Research (28 papers). Sriram Subramaniam is often cited by papers focused on Advanced Electron Microscopy Techniques and Applications (57 papers), Photoreceptor and optogenetics research (32 papers) and Neuroscience and Neuropharmacology Research (28 papers). Sriram Subramaniam collaborates with scholars based in United States, Canada and United Kingdom. Sriram Subramaniam's co-authors include Alberto Bartesaghi, Mario J. Borgnia, Guillermo Sapiro, Jacqueline L.S. Milne, Richard A. Henderson, Oleg Kuybeda, Gabriel A. Frank, Alan Merk, Teruhisa Hirai and Kedar Narayan and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Sriram Subramaniam

198 papers receiving 14.0k citations

Hit Papers

A collaborative framework... 1993 2026 2004 2015 2012 2008 2022 2000 1993 500 1000 1.5k
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. A collaborative framework for 3D alignment and classification of heterogeneous subvolumes in cryo-electron tomography
    2012 1.6k citations Oleg Kuybeda, Gabriel A. Frank et al. Journal of Structural Biology profile →
  2. Molecular architecture of native HIV-1 gp120 trimers
    2008 622 citations Alberto Bartesaghi, Mario J. Borgnia et al. Nature profile →
  3. SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex
    2022 408 citations Dhiraj Mannar, James W. Saville et al. Science profile →
  4. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    2000 379 citations Sriram Subramaniam, Richard A. Henderson Nature profile →
  5. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.
    1993 377 citations Sriram Subramaniam, Richard A. Henderson et al. profile →
  6. Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation
    2022 134 citations Dhiraj Mannar, Karoline Leopold et al. profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Sriram Subramaniam United States 63 7.0k 2.4k 2.2k 1.8k 1.6k 200 14.2k
Xiaowei Zhuang United States 95 21.2k 3.0× 5.3k 2.2× 2.3k 1.1× 1.1k 0.6× 640 0.4× 196 41.2k
David A. Agard United States 90 24.7k 3.5× 3.5k 1.5× 1.4k 0.7× 1.2k 0.7× 329 0.2× 326 37.3k
Wah Chiu United States 88 16.8k 2.4× 5.3k 2.2× 1.1k 0.5× 3.4k 1.9× 425 0.3× 470 29.2k
Alberto Bartesaghi United States 31 2.3k 0.3× 1.3k 0.5× 243 0.1× 687 0.4× 1.2k 0.7× 71 6.2k
Bridget Carragher United States 61 7.9k 1.1× 3.3k 1.4× 534 0.2× 943 0.5× 866 0.6× 195 13.4k
Jennifer Lippincott‐Schwartz United States 118 30.2k 4.3× 3.6k 1.5× 3.7k 1.7× 681 0.4× 690 0.4× 289 51.8k
Thomas D. Goddard United States 13 30.2k 4.3× 1.6k 0.7× 2.2k 1.0× 4.2k 2.4× 992 0.6× 13 47.2k
Mario J. Borgnia United States 37 3.3k 0.5× 455 0.2× 287 0.1× 952 0.5× 1.0k 0.7× 103 7.4k
Juan S. Bonifacino United States 103 23.2k 3.3× 1.6k 0.7× 2.7k 1.3× 1.2k 0.7× 2.1k 1.3× 301 42.7k
David J. Fleet Canada 53 5.1k 0.7× 906 0.4× 660 0.3× 720 0.4× 157 0.1× 128 20.4k

Countries citing papers authored by Sriram Subramaniam

Since Specialization
Citations

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

Fields of papers citing papers by Sriram Subramaniam

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sriram Subramaniam

This figure shows the co-authorship network connecting the top 25 collaborators of Sriram Subramaniam. A scholar is included among the top collaborators of Sriram Subramaniam 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 Sriram Subramaniam. Sriram Subramaniam 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.
Huang, Yongjian, Subu Subramanian, Christine L. Gee, et al.. (2024). Autoinhibition of a clamp-loader ATPase revealed by deep mutagenesis and cryo-EM. Nature Structural & Molecular Biology. 31(3). 424–435. 1 indexed citations
2.
Mannar, Dhiraj, James W. Saville, Xing Zhu, et al.. (2024). Altered receptor binding, antibody evasion and retention of T cell recognition by the SARS-CoV-2 XBB.1.5 spike protein. Nature Communications. 15(1). 1854–1854. 8 indexed citations
3.
Ivison, Sabine, Qing Huang, Dhiraj Mannar, et al.. (2023). SARS-CoV-2 Variants Omicron BA.4/5 and XBB.1.5 Significantly Escape T Cell Recognition in Solid-organ Transplant Recipients Vaccinated Against the Ancestral Strain. Transplantation. 108(4). e49–e62. 1 indexed citations
4.
Castells‐Graells, Roger, Mark A. Arbing, M.R. Sawaya, et al.. (2023). Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold. Proceedings of the National Academy of Sciences. 120(37). e2305494120–e2305494120. 21 indexed citations
5.
Saville, James W., Xing Zhu, Alison Berezuk, et al.. (2023). Allosteric modulation of ryanodine receptor RyR1 by nucleotide derivatives. Structure. 31(7). 790–800.e4. 12 indexed citations
6.
Zhu, Xing, Dhiraj Mannar, Shanti Swaroop Srivastava, et al.. (2021). Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies. PLoS Biology. 19(4). e3001237–e3001237. 135 indexed citations
7.
Lin, Mingqun, Giovanna Grandinetti, Lisa M. Hartnell, et al.. (2020). Host membrane lipids are trafficked to membranes of intravacuolar bacteriumEhrlichia chaffeensis. Proceedings of the National Academy of Sciences. 117(14). 8032–8043. 23 indexed citations
8.
Chittori, Sagar, Jingjun Hong, Hanqiao Feng, et al.. (2017). Structural mechanisms of centromeric nucleosome recognition by the kinetochore protein CENP-N. Science. 359(6373). 339–343. 91 indexed citations
9.
Earl, Lesley A., V. Falconieri, Jacqueline L.S. Milne, & Sriram Subramaniam. (2017). Cryo-EM: beyond the microscope. Current Opinion in Structural Biology. 46. 71–78. 77 indexed citations
10.
Wohlbold, Teddy John, Kira A. Podolsky, Veronika Chromikova, et al.. (2017). Broadly protective murine monoclonal antibodies against influenza B virus target highly conserved neuraminidase epitopes. Nature Microbiology. 2(10). 1415–1424. 99 indexed citations
11.
Banerjee, Soojay, Alberto Bartesaghi, Alan Merk, et al.. (2016). 2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition. Science. 351(6275). 871–875. 269 indexed citations
12.
Meyerson, Joel R., Sagar Chittori, Alan Merk, et al.. (2016). Structural basis of kainate subtype glutamate receptor desensitization. Nature. 537(7621). 567–571. 76 indexed citations
13.
Murphy, Gavin E., Lesley A. Earl, Gregory Q. Del Prete, et al.. (2014). Three-Dimensional Imaging of HIV-1 Virological Synapses Reveals Membrane Architectures Involved in Virus Transmission. Journal of Virology. 88(18). 10327–10339. 62 indexed citations
14.
Frank, Gabriel A., Alberto Bartesaghi, Oleg Kuybeda, et al.. (2012). Computational separation of conformational heterogeneity using cryo-electron tomography and 3D sub-volume averaging. Journal of Structural Biology. 178(2). 165–176. 19 indexed citations
15.
Kuybeda, Oleg, Gabriel A. Frank, Alberto Bartesaghi, et al.. (2012). A collaborative framework for 3D alignment and classification of heterogeneous subvolumes in cryo-electron tomography. Journal of Structural Biology. 181(2). 116–127. 1561 indexed citations breakdown →
16.
Bartesaghi, Alberto & Sriram Subramaniam. (2009). Membrane protein structure determination using cryo-electron tomography and 3D image averaging. Current Opinion in Structural Biology. 19(4). 402–407. 51 indexed citations
17.
Hirai, Teruhisa, Sriram Subramaniam, & Janos Κ. Lanyi. (2009). Structural snapshots of conformational changes in a seven-helix membrane protein: lessons from bacteriorhodopsin. Current Opinion in Structural Biology. 19(4). 433–439. 51 indexed citations
18.
Khursigara, Cezar M., et al.. (2008). Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors. Proceedings of the National Academy of Sciences. 105(43). 16555–16560. 67 indexed citations
19.
Zhang, Peijun, Cezar M. Khursigara, Lisa M. Hartnell, & Sriram Subramaniam. (2007). Direct visualization of Escherichia coli chemotaxis receptor arrays using cryo-electron microscopy. Proceedings of the National Academy of Sciences. 104(10). 3777–3781. 140 indexed citations
20.
Subramaniam, Sriram & Richard A. Henderson. (2000). Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature. 406(6796). 653–657. 379 indexed citations breakdown →

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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