Peter Schuck

31.3k total citations · 8 hit papers
350 papers, 23.4k citations indexed

About

Peter Schuck is a scholar working on Molecular Biology, Nuclear and High Energy Physics and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Peter Schuck has authored 350 papers receiving a total of 23.4k indexed citations (citations by other indexed papers that have themselves been cited), including 176 papers in Molecular Biology, 80 papers in Nuclear and High Energy Physics and 69 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Peter Schuck's work include Protein purification and stability (85 papers), Nuclear physics research studies (73 papers) and Monoclonal and Polyclonal Antibodies Research (46 papers). Peter Schuck is often cited by papers focused on Protein purification and stability (85 papers), Nuclear physics research studies (73 papers) and Monoclonal and Polyclonal Antibodies Research (46 papers). Peter Schuck collaborates with scholars based in United States, France and Germany. Peter Schuck's co-authors include Peter Smith Ring, M. R. Strayer, Huaying Zhao, Patrick H. Brown, Julie Dam, Andrea Balbo, Jacob Lebowitz, Marc S. Lewis, A. Tohsaki and Chad A. Brautigam and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Peter Schuck

339 papers receiving 23.0k citations

Hit Papers

Size-Distribution Analysi... 1983 2026 1997 2011 2000 1983 2002 2002 2003 1000 2.0k 3.0k

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Peter Schuck 12.3k 4.3k 3.7k 2.8k 2.2k 350 23.4k
Akira Hasegawa 9.6k 0.8× 4.9k 1.1× 12.1k 3.3× 7.3k 2.6× 2.0k 0.9× 1.2k 45.0k
Gerhard Wagner 29.7k 2.4× 2.9k 0.7× 1.6k 0.4× 5.6k 2.0× 4.3k 2.0× 535 41.9k
Stefan Becker 8.3k 0.7× 1.5k 0.4× 907 0.2× 3.0k 1.1× 773 0.4× 357 16.3k
John L. Markley 20.1k 1.6× 1.3k 0.3× 859 0.2× 5.2k 1.8× 979 0.4× 507 27.9k
Angela M. Gronenborn 30.7k 2.5× 2.0k 0.5× 1.6k 0.4× 9.1k 3.2× 3.1k 1.4× 550 40.6k
Brian D. Sykes 19.2k 1.6× 809 0.2× 1.2k 0.3× 4.2k 1.5× 1.7k 0.8× 468 28.5k
Stephan Grzesiek 22.5k 1.8× 1.3k 0.3× 1.2k 0.3× 6.0k 2.1× 1.9k 0.8× 171 29.5k
Harden M. McConnell 16.9k 1.4× 1.1k 0.3× 8.1k 2.2× 4.3k 1.5× 2.5k 1.2× 384 33.9k
Gottfried Otting 13.3k 1.1× 1.3k 0.3× 1.3k 0.4× 5.4k 1.9× 668 0.3× 326 19.8k
Robert Kaptein 14.1k 1.1× 1.0k 0.2× 1.6k 0.4× 3.8k 1.3× 922 0.4× 347 20.1k

Countries citing papers authored by Peter Schuck

Since Specialization
Citations

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

Fields of papers citing papers by Peter Schuck

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Peter Schuck

This figure shows the co-authorship network connecting the top 25 collaborators of Peter Schuck. A scholar is included among the top collaborators of Peter Schuck 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 Peter Schuck. Peter Schuck 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.
Schuck, Peter & Huaying Zhao. (2023). Diversity of short linear interaction motifs in SARS-CoV-2 nucleocapsid protein. mBio. 14(6). e0238823–e0238823. 8 indexed citations
2.
Zhao, Huaying, Di Wu, Sergio A. Hassan, et al.. (2023). A conserved oligomerization domain in the disordered linker of coronavirus nucleocapsid proteins. Science Advances. 9(14). eadg6473–eadg6473. 26 indexed citations
3.
Zhao, Huaying, Ai Nguyen, Di Wu, et al.. (2022). Plasticity in structure and assembly of SARS-CoV-2 nucleocapsid protein. PNAS Nexus. 1(2). pgac049–pgac049. 40 indexed citations
4.
Harkness, Robert W., Yuki Toyama, Zev A. Ripstein, et al.. (2021). Competing stress-dependent oligomerization pathways regulate self-assembly of the periplasmic protease-chaperone DegP. Proceedings of the National Academy of Sciences. 118(32). 15 indexed citations
5.
Sousa, Alioscka A., Peter Schuck, & Sergio A. Hassan. (2021). Biomolecular interactions of ultrasmall metallic nanoparticles and nanoclusters. Nanoscale Advances. 3(11). 2995–3027. 41 indexed citations
6.
Juul‐Madsen, Kristian, Anne Troldborg, Thomas R. Wittenborn, et al.. (2021). Characterization of DNA–protein complexes by nanoparticle tracking analysis and their association with systemic lupus erythematosus. Proceedings of the National Academy of Sciences. 118(30). 7 indexed citations
7.
Velázquez‐Campoy, Adrián, Olga Abián, Rafael Claveria‐Gimeno, et al.. (2021). A multi-laboratory benchmark study of isothermal titration calorimetry (ITC) using Ca2+ and Mg2+ binding to EDTA. European Biophysics Journal. 50(3-4). 429–451. 8 indexed citations
8.
Conicella, Alexander E., Rui Huang, Zev A. Ripstein, et al.. (2020). An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase. Proceedings of the National Academy of Sciences. 117(42). 26226–26236. 21 indexed citations
9.
Chen, Zhaochun, Giacomo Diaz, Teresa Pollicino, et al.. (2018). Role of humoral immunity against hepatitis B virus core antigen in the pathogenesis of acute liver failure. Proceedings of the National Academy of Sciences. 115(48). E11369–E11378. 57 indexed citations
10.
Ge, Jingpeng, Johannes Elferich, April Goehring, et al.. (2018). Structure of mouse protocadherin 15 of the stereocilia tip link in complex with LHFPL5. eLife. 7. 57 indexed citations
11.
Ferreira, Rodrigo da Silva, Ricardo J.S. Torquato, Huaying Zhao, et al.. (2018). Binding kinetics of ultrasmall gold nanoparticles with proteins. Nanoscale. 10(7). 3235–3244. 37 indexed citations
12.
Morozov, Giora I., Huaying Zhao, Michael G. Mage, et al.. (2016). Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing. Proceedings of the National Academy of Sciences. 113(8). E1006–15. 68 indexed citations
13.
Schuck, Peter, et al.. (2016). Tubulin Dimer Reversible Dissociation. Journal of Biological Chemistry. 291(17). 9281–9294. 12 indexed citations
14.
Marzahn, Melissa R., Suresh Marada, Jihun Lee, et al.. (2016). Higher‐order oligomerization promotes localization of SPOP to liquid nuclear speckles. The EMBO Journal. 35(12). 1254–1275. 152 indexed citations
15.
Chaudhry, Charu, Andrew J.R. Plested, Peter Schuck, & Mark L. Mayer. (2009). Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions. Proceedings of the National Academy of Sciences. 106(30). 12329–12334. 41 indexed citations
16.
Schuck, Peter, et al.. (2007). Protein Interactions. 8 indexed citations
17.
Boukari, Hacène, Dan L. Sackett, Peter Schuck, & Ralph Nossal. (2007). Single‐walled tubulin ring polymers. Biopolymers. 86(5-6). 424–436. 11 indexed citations
18.
Mans, Janet, Kannan Natarajan, Andrea Balbo, et al.. (2007). Cellular Expression and Crystal Structure of the Murine Cytomegalovirus Major Histocompatibility Complex Class I-like Glycoprotein, m153. Journal of Biological Chemistry. 282(48). 35247–35258. 21 indexed citations
19.
Schuck, Peter, et al.. (2007). Special Issue: The Workshop on the State of the Art in Nuclear Cluster Physics (SOTANCP2008) Strasbourg, France 13-16 May, 2008. HAL (Le Centre pour la Communication Scientifique Directe). 2 indexed citations
20.
Dam, Julie, R. Guan, K. Natarajan, et al.. (2003). VARIABLE MHC CLASS I ENGAGEMENT BY LY49 NATURAL KILLER CELL RECEPTORS DEMONSTRATED BY THE CRYSTAL STRUCTURE OF LY49C BOUND TO H-2K(B). Langmuir. 20.

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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