David Fushman

9.8k total citations · 1 hit paper
149 papers, 8.1k citations indexed

About

David Fushman is a scholar working on Molecular Biology, Spectroscopy and Oncology. According to data from OpenAlex, David Fushman has authored 149 papers receiving a total of 8.1k indexed citations (citations by other indexed papers that have themselves been cited), including 133 papers in Molecular Biology, 35 papers in Spectroscopy and 33 papers in Oncology. Recurrent topics in David Fushman's work include Ubiquitin and proteasome pathways (71 papers), Protein Structure and Dynamics (46 papers) and Glycosylation and Glycoproteins Research (29 papers). David Fushman is often cited by papers focused on Ubiquitin and proteasome pathways (71 papers), Protein Structure and Dynamics (46 papers) and Glycosylation and Glycoproteins Research (29 papers). David Fushman collaborates with scholars based in United States, Israel and Germany. David Fushman's co-authors include Cecile M. Pickart, David Cowburn, Ranjani Varadan, Shahri Raasi, Olivier Walker, Sean M. Cahill, Michael Assfalg, Yaroslav Ryabov, Jennifer B. Hall and Daoning Zhang and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David Fushman

145 papers receiving 8.0k citations

Hit Papers

Polyubiquitin chains: polymeric protein signals 2004 2026 2011 2018 2004 250 500 750
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. Polyubiquitin chains: polymeric protein signals
    2004 866 citations Cecile M. Pickart, David Fushman Current Opinion in Chemical Biology profile →

Peers

David Fushman
Edward T. Olejniczak United States
Richard W. Kriwacki United States
David Cowburn United States
Paul C. Driscoll United Kingdom
Stefan M.V. Freund United Kingdom
Kevin H. Gardner United States
James J. Chou United States
Rodolfo Ghirlando United States
John H. Bushweller United States
Mark Bycroft United Kingdom
Edward T. Olejniczak United States
David Fushman
Citations per year, relative to David Fushman David Fushman (= 1×) peers Edward T. Olejniczak

Countries citing papers authored by David Fushman

Since Specialization
Citations

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

Fields of papers citing papers by David Fushman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Fushman

This figure shows the co-authorship network connecting the top 25 collaborators of David Fushman. A scholar is included among the top collaborators of David Fushman 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 David Fushman. David Fushman 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.
Osipiuk, J., C. Tesar, M. Endres, et al.. (2023). Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin. Nature Communications. 14(1). 2366–2366. 36 indexed citations
2.
Strickland, Madeleine, Susan M. Watanabe, Mary R. Starich, et al.. (2022). Tsg101/ESCRT-I recruitment regulated by the dual binding modes of K63-linked diubiquitin. Structure. 30(2). 289–299.e6. 12 indexed citations
3.
Rogers, Joseph M., Ganga B. Vamisetti, Ido Livneh, et al.. (2020). In vivo modulation of ubiquitin chains by N -methylated non-proteinogenic cyclic peptides. RSC Chemical Biology. 2(2). 513–522. 22 indexed citations
4.
Ahmed, Syed Feroj, Gary Sibbet, Ventzislava A. Hristova, et al.. (2020). Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain. Nature Communications. 11(1). 2094–2094. 28 indexed citations
5.
Gomes, Fábio Pereira, et al.. (2018). Top‐down analysis of novel synthetic branched proteins. Journal of Mass Spectrometry. 54(1). 19–25. 6 indexed citations
6.
Singh, Raj, et al.. (2018). Impact of different ionization states of phosphorylated Serine-65 on ubiquitin structure and interactions. Scientific Reports. 8(1). 2651–2651. 8 indexed citations
7.
Zhang, Daoning, Monika Talarowska, Piotr Gałecki, et al.. (2016). Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB+1. FEBS Letters. 590(24). 4573–4585. 6 indexed citations
8.
Castañeda, Carlos A., Olivier Walker, Apurva Chaturvedi, et al.. (2016). Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins. Structure. 24(3). 423–436. 51 indexed citations
9.
Haj‐Yahya, Mahmood, Carlos A. Castañeda, Liat Spasser, et al.. (2013). Modifying the Vicinity of the Isopeptide Bond To Reveal Differential Behavior of Ubiquitin Chains with Interacting Proteins: Organic Chemistry Applied to Synthetic Proteins. Angewandte Chemie International Edition. 52(42). 11149–11153. 27 indexed citations
10.
Bornet, Aurélien, Puneet Ahuja, Riddhiman Sarkar, et al.. (2011). Long‐Lived States to Monitor Protein Unfolding by Proton NMR. ChemPhysChem. 12(15). 2729–2734. 37 indexed citations
11.
Berlin, Konstantin, Dianne P. O’Leary, & David Fushman. (2011). Fast approximations of the rotational diffusion tensor and their application to structural assembly of molecular complexes. Proteins Structure Function and Bioinformatics. 79(7). 2268–2281. 7 indexed citations
12.
Shang, Fu, Edward J. Dudek, Aleš Cvekl, et al.. (2010). Lens Cell Proliferation, Differentiation and Development Require K6 on Ubiquitin. Investigative Ophthalmology & Visual Science. 51(13). 1212–1212. 1 indexed citations
13.
Zhang, Naixia, Qinghua Wang, Aaron Ehlinger, et al.. (2009). Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13. Molecular Cell. 35(3). 280–290. 118 indexed citations
14.
Zhang, Daoning, Tony Chen, Inbal Ziv, et al.. (2009). Together, Rpn10 and Dsk2 Can Serve as a Polyubiquitin Chain-Length Sensor. Molecular Cell. 36(6). 1018–1033. 99 indexed citations
15.
Varadan, Ranjani, Michael Assfalg, & David Fushman. (2005). Using NMR Spectroscopy to Monitor Ubiquitin Chain Conformation and Interactions with Ubiquitin‐Binding Domains. Methods in enzymology on CD-ROM/Methods in enzymology. 399. 177–192. 33 indexed citations
16.
Verma, Rati, Noël R. Peters, Mariapina D’Onofrio, et al.. (2004). Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain. Science. 306(5693). 117–120. 154 indexed citations
17.
Varadan, Ranjani, Michael Assfalg, Aydin Haririnia, et al.. (2004). Solution Conformation of Lys63-linked Di-ubiquitin Chain Provides Clues to Functional Diversity of Polyubiquitin Signaling. Journal of Biological Chemistry. 279(8). 7055–7063. 284 indexed citations
18.
Pickart, Cecile M. & David Fushman. (2004). Polyubiquitin chains: polymeric protein signals. Current Opinion in Chemical Biology. 8(6). 610–616. 866 indexed citations breakdown →
19.
Fushman, David, et al.. (1999). Impact of Cl and Na ions on simulated structure and dynamics of βARK1 PH domain. Proteins Structure Function and Bioinformatics. 35(2). 206–217.
20.
Fushman, David, et al.. (1999). Impact of Cl? and Na+ ions on simulated structure and dynamics of ?ARK1 PH domain. Proteins Structure Function and Bioinformatics. 35(2). 206–217. 23 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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