Christopher Tsu

2.3k total citations
34 papers, 1.8k citations indexed

About

Christopher Tsu is a scholar working on Molecular Biology, Oncology and Cancer Research. According to data from OpenAlex, Christopher Tsu has authored 34 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 14 papers in Oncology and 11 papers in Cancer Research. Recurrent topics in Christopher Tsu's work include Ubiquitin and proteasome pathways (16 papers), Peptidase Inhibition and Analysis (13 papers) and Protease and Inhibitor Mechanisms (10 papers). Christopher Tsu is often cited by papers focused on Ubiquitin and proteasome pathways (16 papers), Peptidase Inhibition and Analysis (13 papers) and Protease and Inhibitor Mechanisms (10 papers). Christopher Tsu collaborates with scholars based in United States, Germany and Japan. Christopher Tsu's co-authors include Lawrence R. Dick, Charles S. Craik, John J. Perona, Olke C. Uhlenbeck, Paul Hales, Robert J. Fletterick, Frank J. Bruzzese, Jonathan L. Blank, Paul Fleming and Khristofer Garcia and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Blood.

In The Last Decade

Christopher Tsu

34 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Christopher Tsu United States 26 1.4k 584 284 211 163 34 1.8k
Michael A. Milhollen United States 14 1.5k 1.0× 538 0.9× 107 0.4× 201 1.0× 105 0.6× 26 1.9k
Christopher Cubitt United States 26 691 0.5× 500 0.9× 184 0.6× 123 0.6× 277 1.7× 57 1.7k
C. Tallant United Kingdom 23 1.6k 1.2× 499 0.9× 560 2.0× 281 1.3× 116 0.7× 34 2.1k
Donald J. Davidson United States 21 1.3k 0.9× 227 0.4× 193 0.7× 646 3.1× 273 1.7× 35 1.9k
Simon R. Green United States 23 2.1k 1.5× 692 1.2× 141 0.5× 230 1.1× 386 2.4× 44 2.8k
Huizhou Fan United States 20 852 0.6× 434 0.7× 94 0.3× 176 0.8× 192 1.2× 50 1.6k
Mark Egerton Australia 19 1.3k 0.9× 428 0.7× 166 0.6× 145 0.7× 732 4.5× 23 2.2k
Dyfed L. Evans United Kingdom 10 707 0.5× 252 0.4× 267 0.9× 478 2.3× 208 1.3× 10 1.3k
Dorit K. Nägler Germany 20 664 0.5× 402 0.7× 109 0.4× 657 3.1× 220 1.3× 33 1.5k
Christian Boudier France 26 845 0.6× 143 0.2× 183 0.6× 383 1.8× 238 1.5× 58 1.7k

Countries citing papers authored by Christopher Tsu

Since Specialization
Citations

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

Fields of papers citing papers by Christopher Tsu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher Tsu

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher Tsu. A scholar is included among the top collaborators of Christopher Tsu 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 Christopher Tsu. Christopher Tsu 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.
Xie, Stanley C., Riley D. Metcalfe, Eric Hanssen, et al.. (2019). The structure of the PA28–20S proteasome complex from Plasmodium falciparum and implications for proteostasis. Nature Microbiology. 4(11). 1990–2000. 29 indexed citations
2.
Basler, Michael, Michelle Lindström, Jacob LaStant, et al.. (2018). Co‐inhibition of immunoproteasome subunits LMP2 and LMP7 is required to block autoimmunity. EMBO Reports. 19(12). 62 indexed citations
3.
Akopian, Tatos, Olga Kandror, Christopher Tsu, et al.. (2015). Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity. Journal of Biological Chemistry. 290(17). 11008–11020. 48 indexed citations
4.
Li, Hao, Christopher Tsu, Christopher Blackburn, et al.. (2014). Identification of Potent and Selective Non-covalent Inhibitors of the Plasmodium falciparum Proteasome. Journal of the American Chemical Society. 136(39). 13562–13565. 46 indexed citations
5.
Bannerman, Bret, Ling Xu, Matthew D. Jones, et al.. (2011). Preclinical evaluation of the antitumor activity of bortezomib in combination with vitamin C or with epigallocatechin gallate, a component of green tea. Cancer Chemotherapy and Pharmacology. 68(5). 1145–1154. 32 indexed citations
6.
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
7.
Kupperman, Erik, Edmund C. Lee, Yueying Cao, et al.. (2010). Evaluation of the Proteasome Inhibitor MLN9708 in Preclinical Models of Human Cancer. Cancer Research. 70(5). 1970–1980. 409 indexed citations
8.
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
9.
Bruzzese, Frank J., Christopher Tsu, Jingya Ma, et al.. (2009). Development of a charcoal paper adenosine triphosphate:pyrophosphate exchange assay: Kinetic characterization of NEDD8 activating enzyme. Analytical Biochemistry. 394(1). 24–29. 12 indexed citations
10.
Lin, Gang, Christopher Tsu, Lawrence R. Dick, Xi Kathy Zhou, & Carl Nathan. (2008). Distinct Specificities of Mycobacterium tuberculosis and Mammalian Proteasomes for N-Acetyl Tripeptide Substrates. Journal of Biological Chemistry. 283(49). 34423–34431. 45 indexed citations
11.
Williamson, Mark J., Jonathan L. Blank, Frank J. Bruzzese, et al.. (2006). Comparison of biochemical and biological effects of ML858 (salinosporamide A) and bortezomib. Molecular Cancer Therapeutics. 5(12). 3052–3061. 57 indexed citations
12.
Badola, Sunita, Keith Robison, Eric R. Fedyk, et al.. (2006). Correlation of serpin–protease expression by comparative analysis of real-time PCR profiling data. Genomics. 88(2). 173–184. 17 indexed citations
13.
Pak, Stephen C., Vasantha Kumar, Christopher Tsu, et al.. (2004). SRP-2 Is a Cross-class Inhibitor That Participates in Postembryonic Development of the Nematode Caenorhabditis elegans. Journal of Biological Chemistry. 279(15). 15448–15459. 35 indexed citations
14.
Tsu, Christopher, Karl Kossen, & Olke C. Uhlenbeck. (2001). The Escherichia coli DEAD protein DbpA recognizes a small RNA hairpin in 23S rRNA. RNA. 7(5). 702–709. 80 indexed citations
15.
Uemura, Yoshiki, Stephen C. Pak, Cliff J. Luke, et al.. (2000). Circulating serpin tumor markers SCCA1 and SCCA2 are not actively secreted but reside in the cytosol of squamous carcinoma cells. International Journal of Cancer. 89(4). 368–377. 63 indexed citations
16.
Luke, Cliff J., Charles Schick, Christopher Tsu, et al.. (2000). Simple Modifications of the Serpin Reactive Site Loop Convert SCCA2 into a Cysteine Proteinase Inhibitor:  A Critical Role for the P3‘ Proline in Facilitating RSL Cleavage. Biochemistry. 39(24). 7081–7091. 41 indexed citations
17.
Perona, John J., Christopher Tsu, Charles S. Craik, & Robert J. Fletterick. (1997). Crystal Structure of an Ecotin−Collagenase Complex Suggests a Model for Recognition and Cleavage of the Collagen Triple Helix. Biochemistry. 36(18). 5381–5392. 64 indexed citations
18.
Tsu, Christopher & Charles S. Craik. (1996). Substrate Recognition by Recombinant Serine Collagenase 1 from Uca pugilator. Journal of Biological Chemistry. 271(19). 11563–11570. 27 indexed citations
19.
Perona, John J., et al.. (1993). Relocating a Negative Charge in the Binding Pocket of Trypsin. Journal of Molecular Biology. 230(3). 934–949. 60 indexed citations
20.
Perona, John J., Christopher Tsu, Charles S. Craik, & Robert J. Fletterick. (1993). Crystal Structure of Rat Anionic Trypsin Complexed with the Protein Inhibitors APPI and BPTI. Journal of Molecular Biology. 230(3). 919–933. 61 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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