Nancy J. Bump

3.3k total citations · 1 hit paper
15 papers, 1.4k citations indexed

About

Nancy J. Bump is a scholar working on Molecular Biology, Oncology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Nancy J. Bump has authored 15 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Molecular Biology, 4 papers in Oncology and 3 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Nancy J. Bump's work include Ubiquitin and proteasome pathways (5 papers), Peptidase Inhibition and Analysis (4 papers) and Chemical Synthesis and Analysis (3 papers). Nancy J. Bump is often cited by papers focused on Ubiquitin and proteasome pathways (5 papers), Peptidase Inhibition and Analysis (4 papers) and Chemical Synthesis and Analysis (3 papers). Nancy J. Bump collaborates with scholars based in United States, Canada and United Kingdom. Nancy J. Bump's co-authors include John A. Mankovich, Tariq Ghayur, Margaret Hugunin, Maria Hackett, Winnie W. Wong, Joanne Kamens, Hamish Allen, Simon Franklin, Kenneth D. Brady and Lois K. Miller and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Nancy J. Bump

15 papers receiving 1.3k citations

Hit Papers

Inhibition of ICE Family Proteases by Baculovirus Antiapo... 1995 2026 2005 2015 1995 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Nancy J. Bump United States 11 1.1k 364 293 156 150 15 1.4k
Elangovan Boobalan United States 9 1.4k 1.2× 275 0.8× 307 1.0× 167 1.1× 209 1.4× 11 1.6k
Emad S. Alnemri United States 7 1.3k 1.2× 395 1.1× 240 0.8× 212 1.4× 244 1.6× 8 1.6k
Maria Hackett United States 7 1.7k 1.5× 420 1.2× 221 0.8× 236 1.5× 214 1.4× 8 2.0k
Michal Štros Czechia 21 1.3k 1.1× 419 1.2× 302 1.0× 157 1.0× 84 0.6× 36 1.9k
Louis P. Deiss United States 14 1.2k 1.1× 372 1.0× 315 1.1× 157 1.0× 435 2.9× 17 1.8k
Carol D. Katayama United States 15 1.0k 0.9× 759 2.1× 309 1.1× 117 0.8× 86 0.6× 20 1.8k
Michelle A. Hughes United Kingdom 17 1.1k 1.0× 500 1.4× 253 0.9× 191 1.2× 344 2.3× 24 1.5k
Alexandre Nesterov United States 15 886 0.8× 210 0.6× 187 0.6× 168 1.1× 76 0.5× 16 1.3k
Christiane Landgraf Germany 22 1.3k 1.1× 351 1.0× 381 1.3× 92 0.6× 97 0.6× 29 1.7k
Jürgen Frey Germany 20 667 0.6× 524 1.4× 173 0.6× 60 0.4× 205 1.4× 30 1.3k

Countries citing papers authored by Nancy J. Bump

Since Specialization
Citations

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

Fields of papers citing papers by Nancy J. Bump

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Nancy J. Bump. 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 Nancy J. Bump. The network helps show where Nancy J. Bump may publish in the future.

Co-authorship network of co-authors of Nancy J. Bump

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

All Works

15 of 15 papers shown
1.
Gavin, James M., Kara M. Hoar, Qing Xu, et al.. (2014). Mechanistic Study of Uba5 Enzyme and the Ufm1 Conjugation Pathway. Journal of Biological Chemistry. 289(33). 22648–22658. 34 indexed citations
2.
Blackburn, Christopher, Jonathan L. Blank, Frank J. Bruzzese, et al.. (2012). Optimization of a series of dipeptides with a P3 β-neopentyl asparagine residue as non-covalent inhibitors of the chymotrypsin-like activity of human 20S proteasome. MedChemComm. 3(6). 710–719. 9 indexed citations
3.
Tsu, Christopher, James M. Gavin, Michael A. Milhollen, et al.. (2011). Mechanistic Studies of Substrate-assisted Inhibition of Ubiquitin-activating Enzyme by Adenosine Sulfamate Analogues. Journal of Biological Chemistry. 286(47). 40867–40877. 66 indexed citations
4.
Blackburn, Christopher, Jonathan L. Blank, Frank J. Bruzzese, et al.. (2010). Optimization of a series of dipeptides with a P3 threonine residue as non-covalent inhibitors of the chymotrypsin-like activity of the human 20S proteasome. Bioorganic & Medicinal Chemistry Letters. 20(22). 6581–6586. 39 indexed citations
5.
Blackburn, Christopher, Kenneth M. Gigstad, Paul Hales, et al.. (2010). Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S β5-subunit. Biochemical Journal. 430(3). 461–476. 129 indexed citations
6.
Jia, Yong, Nancy J. Bump, Anca Clabbers, et al.. (2005). Purification and kinetic characterization of recombinant human mitogen-activated protein kinase kinase kinase COT and the complexes with its cellular partner NF-κB1 p105. Archives of Biochemistry and Biophysics. 441(1). 64–74. 13 indexed citations
7.
Arnold, Lee D., R.A. Dixon, Robert V. Talanian, et al.. (2002). Molecular interactions in crystal structures of potent inhibitors bound to the kinase domain of Tie-2. 43. 848. 2 indexed citations
8.
Salmerón, Andrés, Julia Janzen, Yasmina Soneji, et al.. (2001). Direct Phosphorylation of NF-κB1 p105 by the IκB Kinase Complex on Serine 927 Is Essential for Signal-induced p105 Proteolysis. Journal of Biological Chemistry. 276(25). 22215–22222. 114 indexed citations
9.
Datta, Rakesh, Hiromi Kojima, David Banach, et al.. (1997). Activation of a CrmA-insensitive, p35-sensitive Pathway in Ionizing Radiation-induced Apoptosis. Journal of Biological Chemistry. 272(3). 1965–1969. 117 indexed citations
10.
Kamens, Joanne, Michael Paskind, Margaret Hugunin, et al.. (1995). Identification and Characterization of ICH-2, a Novel Member of the Interleukin-1β-converting Enzyme Family of Cysteine Proteases. Journal of Biological Chemistry. 270(25). 15250–15256. 238 indexed citations
11.
Bump, Nancy J., Maria Hackett, Margaret Hugunin, et al.. (1995). Inhibition of ICE Family Proteases by Baculovirus Antiapoptotic Protein p35. Science. 269(5232). 1885–1888. 555 indexed citations breakdown →
12.
Najjar, Victor A. & Nancy J. Bump. (1989). Covalent peptide transfer to cell membrane proteins (peptidyl transferase). FEBS Letters. 253(1-2). 129–131. 2 indexed citations
13.
Bump, Nancy J. & Victor A. Najjar. (1988). Tuftsin stimulates growth of HL60 cells. FEBS Letters. 226(2). 303–306. 6 indexed citations
14.
Bump, Nancy J., et al.. (1986). Isolation and subunit composition of tuftsin receptor.. Proceedings of the National Academy of Sciences. 83(19). 7187–7191. 30 indexed citations
15.
Chaudhuri, Manas K., Danuta Konopińska, Nancy J. Bump, & Victor A. Najjar. (1983). The Similarity between Tuftsin (Thr‐Lys‐Pro‐Arg) Receptors and Tuftsin Antibody: A Case of Induced Molecular Mimicrya. Annals of the New York Academy of Sciences. 419(1). 135–142. 14 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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