Robert A. Grassucci

12.0k total citations · 7 hit papers
78 papers, 8.7k citations indexed

About

Robert A. Grassucci is a scholar working on Molecular Biology, Structural Biology and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, Robert A. Grassucci has authored 78 papers receiving a total of 8.7k indexed citations (citations by other indexed papers that have themselves been cited), including 67 papers in Molecular Biology, 16 papers in Structural Biology and 8 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in Robert A. Grassucci's work include RNA and protein synthesis mechanisms (46 papers), RNA modifications and cancer (37 papers) and RNA Research and Splicing (17 papers). Robert A. Grassucci is often cited by papers focused on RNA and protein synthesis mechanisms (46 papers), RNA modifications and cancer (37 papers) and RNA Research and Splicing (17 papers). Robert A. Grassucci collaborates with scholars based in United States, Germany and Sweden. Robert A. Grassucci's co-authors include Joachim Frank, Pawel A. Penczek, Rajendra K. Agrawal, C.M.T. Spahn, Terence Wagenknecht, Sidney Fleischer, Amédée des Georges, Roland Beckmann, Maria V. Yelshanskaya and Edward C. Twomey and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Robert A. Grassucci

78 papers receiving 8.6k citations

Hit Papers

Hepatitis C Virus IRES RNA-Induced Changes in the Conform... 1994 2026 2004 2015 2001 1994 2004 2000 2014 100 200 300
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. Hepatitis C Virus IRES RNA-Induced Changes in the Conformation of the 40 S Ribosomal Subunit
    2001 384 citations Robert A. Grassucci, Pawel A. Penczek et al. profile →
  2. The ribosome at improved resolution: New techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles
    1994 344 citations Pawel A. Penczek, Robert A. Grassucci et al. profile →
  3. Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    2004 333 citations C.M.T. Spahn, Robert A. Grassucci et al. Nature profile →
  4. Solution Structure of the E. coli 70S Ribosome at 11.5 Å Resolution
    2000 329 citations Irene S. Gabashvili, Rajendra K. Agrawal et al. Cell profile →
  5. Structure of a mammalian ryanodine receptor
    2014 329 citations Ran Zalk, Oliver B. Clarke et al. Nature profile →
  6. Structural Basis for Gating and Activation of RyR1
    2016 286 citations Amédée des Georges, Oliver B. Clarke et al. Cell profile →
  7. Channel opening and gating mechanism in AMPA-subtype glutamate receptors
    2017 183 citations Edward C. Twomey, Maria V. Yelshanskaya et al. Nature profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert A. Grassucci United States 52 7.3k 1.4k 1.3k 1.1k 795 78 8.7k
Shawn Zheng United States 14 5.2k 0.7× 466 0.3× 1.7k 1.3× 856 0.8× 460 0.6× 19 8.0k
Xiao‐chen Bai United States 47 7.7k 1.1× 435 0.3× 1.2k 0.9× 436 0.4× 672 0.8× 93 10.9k
Jean‐Paul Armache United States 23 6.5k 0.9× 400 0.3× 869 0.7× 1.1k 1.0× 645 0.8× 41 8.7k
Stefan Raunser Germany 52 5.7k 0.8× 1.1k 0.8× 859 0.7× 917 0.9× 832 1.0× 154 9.6k
C.M.T. Spahn Germany 48 6.4k 0.9× 729 0.5× 756 0.6× 1.3k 1.2× 159 0.2× 103 7.6k
Jianlin Lei China 51 6.4k 0.9× 838 0.6× 391 0.3× 846 0.8× 916 1.2× 96 8.6k
Holger Stark Germany 68 12.5k 1.7× 385 0.3× 1.6k 1.2× 1.0k 1.0× 583 0.7× 152 14.9k
Takanori Nakane Japan 32 6.1k 0.8× 293 0.2× 1.1k 0.9× 720 0.7× 506 0.6× 57 8.7k
Michael Radermacher United States 41 3.8k 0.5× 464 0.3× 1.2k 0.9× 298 0.3× 311 0.4× 114 5.2k
Terence Wagenknecht United States 42 3.2k 0.4× 1.2k 0.9× 908 0.7× 234 0.2× 551 0.7× 86 4.1k

Countries citing papers authored by Robert A. Grassucci

Since Specialization
Citations

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

Fields of papers citing papers by Robert A. Grassucci

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert A. Grassucci. 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 Robert A. Grassucci. The network helps show where Robert A. Grassucci may publish in the future.

Co-authorship network of co-authors of Robert A. Grassucci

This figure shows the co-authorship network connecting the top 25 collaborators of Robert A. Grassucci. A scholar is included among the top collaborators of Robert A. Grassucci 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 Robert A. Grassucci. Robert A. Grassucci 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.
Zuo, Hao, Jinseo Park, Wesley B. Asher, et al.. (2024). Promiscuous G-protein activation by the calcium-sensing receptor. Nature. 629(8011). 481–488. 15 indexed citations
2.
Zheng, Xiangdong, Ziao Fu, Deyuan Su, et al.. (2020). Mechanism of ligand activation of a eukaryotic cyclic nucleotide−gated channel. Nature Structural & Molecular Biology. 27(7). 625–634. 39 indexed citations
3.
Fu, Ziao, Guo‐Yan Xu, Robert A. Grassucci, et al.. (2018). Structure and activity of lipid bilayer within a membrane-protein transporter. Proceedings of the National Academy of Sciences. 115(51). 12985–12990. 123 indexed citations
4.
Feng, Xiangsong, Ziao Fu, Sandip Kaledhonkar, et al.. (2017). A Fast and Effective Microfluidic Spraying-Plunging Method for High-Resolution Single-Particle Cryo-EM. Structure. 25(4). 663–670.e3. 83 indexed citations
5.
Twomey, Edward C., Maria V. Yelshanskaya, Robert A. Grassucci, Joachim Frank, & Alexander I. Sobolevsky. (2017). Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes. Neuron. 94(3). 569–580.e5. 92 indexed citations
6.
Georges, Amédée des, Oliver B. Clarke, Ran Zalk, et al.. (2016). Structural Basis for Gating and Activation of RyR1. Cell. 167(1). 145–157.e17. 286 indexed citations breakdown →
7.
Fu, Ziao, Sandip Kaledhonkar, Ming Sun, et al.. (2016). Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy. Structure. 24(12). 2092–2101. 52 indexed citations
8.
Zalk, Ran, Oliver B. Clarke, Amédée des Georges, et al.. (2014). Structure of a mammalian ryanodine receptor. Nature. 517(7532). 44–49. 329 indexed citations breakdown →
9.
Georges, Amédée des, Yaser Hashem, Anett Unbehaun, et al.. (2013). Structure of the mammalian ribosomal pre-termination complex associated with eRF1•eRF3•GDPNP. Nucleic Acids Research. 42(5). 3409–3418. 63 indexed citations
10.
Huang, Tao, Tanvir R. Shaikh, Kushol Gupta, et al.. (2010). The group II intron ribonucleoprotein precursor is a large, loosely packed structure. Nucleic Acids Research. 39(7). 2845–2854. 9 indexed citations
11.
Sorci, Mirco, et al.. (2009). Time‐dependent insulin oligomer reaction pathway prior to fibril formation: Cooling and seeding. Proteins Structure Function and Bioinformatics. 77(1). 62–73. 37 indexed citations
12.
Grassucci, Robert A., Derek J. Taylor, & Joachim Frank. (2008). Visualization of macromolecular complexes using cryo-electron microscopy with FEI Tecnai transmission electron microscopes. Nature Protocols. 3(2). 330–339. 36 indexed citations
13.
Grassucci, Robert A., Derek J. Taylor, & Joachim Frank. (2007). Preparation of macromolecular complexes for cryo-electron microscopy. Nature Protocols. 2(12). 3239–3246. 160 indexed citations
14.
Spahn, C.M.T., Marı́a G. Gómez-Lorenzo, Robert A. Grassucci, et al.. (2004). Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. The EMBO Journal. 23(5). 1008–1019. 326 indexed citations
15.
Spahn, C.M.T., Gregor Blaha, Pawel A. Penczek, et al.. (2001). Localization of the Ribosomal Protection Protein Tet(O) on the Ribosome and the Mechanism of Tetracycline Resistance. Molecular Cell. 7(5). 1037–1045. 53 indexed citations
16.
Gabashvili, Irene S., Rajendra K. Agrawal, C.M.T. Spahn, et al.. (2000). Solution Structure of the E. coli 70S Ribosome at 11.5 Å Resolution. Cell. 100(5). 537–549. 329 indexed citations breakdown →
17.
Frank, Joachim, et al.. (2000). [18] Three-dimensional cryoelectron microscopy of ribosomes. Methods in enzymology on CD-ROM/Methods in enzymology. 317. 276–291. 61 indexed citations
18.
Spahn, C.M.T., Robert A. Grassucci, Pawel A. Penczek, & Joachim Frank. (1999). Direct three-dimensional localization and positive identification of RNA helices within the ribosome by means of genetic tagging and cyro-electron microscopy. Structure. 7(12). 1567–1573. 27 indexed citations
19.
Ban, Nenad, Betty Freeborn, Poul Nissen, et al.. (1998). A 9 Å Resolution X-Ray Crystallographic Map of the Large Ribosomal Subunit. Cell. 93(7). 1105–1115. 192 indexed citations
20.
Boisset, Nicolas, Michael Radermacher, Robert A. Grassucci, et al.. (1993). Three-Dimensional Immunoelectron Microscopy of Scorpion Hemocyanin Labeled with a Monoclonal Fab Fragment. Journal of Structural Biology. 111(3). 234–244. 20 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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