Django Sussman

2.4k total citations
33 papers, 1.6k citations indexed

About

Django Sussman is a scholar working on Molecular Biology, Oncology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Django Sussman has authored 33 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 16 papers in Oncology and 11 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Django Sussman's work include Monoclonal and Polyclonal Antibodies Research (11 papers), RNA and protein synthesis mechanisms (11 papers) and HER2/EGFR in Cancer Research (8 papers). Django Sussman is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (11 papers), RNA and protein synthesis mechanisms (11 papers) and HER2/EGFR in Cancer Research (8 papers). Django Sussman collaborates with scholars based in United States, Switzerland and South Africa. Django Sussman's co-authors include Barry Stoddard, Lori Westendorf, Jay C. Nix, Chick C. Wilson, Raymond J. Monnat, J. R. Ashworth, James J. Havranek, Carlos M. Duarte, David Baker and Dennis R. Benjamin and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Django Sussman

32 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Django Sussman United States 18 1.0k 574 476 175 150 33 1.6k
Torbjörn Gräslund Sweden 24 1.1k 1.1× 450 0.8× 1.1k 2.2× 189 1.1× 68 0.5× 67 1.7k
Edward B. Reilly United States 23 590 0.6× 566 1.0× 589 1.2× 485 2.8× 81 0.5× 54 2.1k
Uwe Jacob Germany 24 1.3k 1.2× 236 0.4× 758 1.6× 590 3.4× 130 0.9× 29 2.0k
Mehmet Kemal Tur Germany 19 627 0.6× 267 0.5× 388 0.8× 367 2.1× 81 0.5× 43 1.1k
Green Ahn United States 11 1.3k 1.3× 518 0.9× 171 0.4× 224 1.3× 51 0.3× 11 1.6k
Andrew E. Nixon United States 20 965 0.9× 153 0.3× 479 1.0× 112 0.6× 70 0.5× 44 1.3k
Kimberly A. Lee United States 15 1.8k 1.7× 403 0.7× 120 0.3× 127 0.7× 54 0.4× 19 2.4k
Pari Antoniw United Kingdom 15 684 0.7× 281 0.5× 659 1.4× 114 0.7× 97 0.6× 21 1.1k
Gregory A. Michaud United States 16 1.1k 1.1× 410 0.7× 233 0.5× 188 1.1× 62 0.4× 30 1.5k
David V. Gold United States 29 936 0.9× 883 1.5× 637 1.3× 431 2.5× 64 0.4× 67 2.0k

Countries citing papers authored by Django Sussman

Since Specialization
Citations

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

Fields of papers citing papers by Django Sussman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Django Sussman

This figure shows the co-authorship network connecting the top 25 collaborators of Django Sussman. A scholar is included among the top collaborators of Django Sussman 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 Django Sussman. Django Sussman 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.
Moquist, Philip N., Xinqun Zhang, Chris Leiske, et al.. (2024). Reversible Chemical Modification of Antibody Effector Function Mitigates Unwanted Systemic Immune Activation. Bioconjugate Chemistry. 35(6). 855–866. 2 indexed citations
2.
Sussman, Django, Lori Westendorf, David W. Meyer, et al.. (2018). Engineered cysteine antibodies: an improved antibody-drug conjugate platform with a novel mechanism of drug-linker stability. Protein Engineering Design and Selection. 31(2). 47–54. 47 indexed citations
3.
Cao, Anthony, et al.. (2018). Abstract 2742: Additional mechanisms of action of ladiratuzumab vedotin contribute to increased immune cell activation within the tumor. Cancer Research. 78(13_Supplement). 2742–2742. 21 indexed citations
4.
Waight, Andrew B., et al.. (2016). Structural Basis of Microtubule Destabilization by Potent Auristatin Anti-Mitotics. PLoS ONE. 11(8). e0160890–e0160890. 131 indexed citations
5.
Sussman, Django, Leia M. Smith, Martha E. Anderson, et al.. (2014). SGN–LIV1A: A Novel Antibody–Drug Conjugate Targeting LIV-1 for the Treatment of Metastatic Breast Cancer. Molecular Cancer Therapeutics. 13(12). 2991–3000. 104 indexed citations
6.
Okeley, Nicole M., Stephen C. Alley, Martha E. Anderson, et al.. (2013). Development of orally active inhibitors of protein and cellular fucosylation. Proceedings of the National Academy of Sciences. 110(14). 5404–5409. 147 indexed citations
7.
Sutherland, May S.K., Roland B. Walter, Scott C. Jeffrey, et al.. (2012). SGN-CD33A: A Novel CD33-Directed Antibody-Drug Conjugate, Utilizing Pyrrolobenzodiazepine Dimers, Demonstrates Preclinical Antitumor Activity Against Multi-Drug Resistant Human AML. Blood. 120(21). 3589–3589. 7 indexed citations
8.
McDonagh, Charlotte F., Kristine M. Kim, Eileen Turcott, et al.. (2008). Engineered anti-CD70 antibody-drug conjugate with increased therapeutic index. Molecular Cancer Therapeutics. 7(9). 2913–2923. 60 indexed citations
9.
Kim, Kristine M., Charlotte F. McDonagh, Lori Westendorf, et al.. (2008). Anti-CD30 diabody-drug conjugates with potent antitumor activity. Molecular Cancer Therapeutics. 7(8). 2486–2497. 73 indexed citations
10.
Lambert, Abigail R., Django Sussman, Betty Shen, et al.. (2008). Structures of the Rare-Cutting Restriction Endonuclease NotI Reveal a Unique Metal Binding Fold Involved in DNA Binding. Structure. 16(4). 558–569. 28 indexed citations
11.
Nomura, Norimichi, Yayoi Nomura, Django Sussman, Daniel J. Klein, & Barry Stoddard. (2008). Recognition of a common rDNA target site in archaea and eukarya by analogous LAGLIDADG and His–Cys box homing endonucleases. Nucleic Acids Research. 36(22). 6988–6998. 9 indexed citations
12.
Gerber, Hans Peter, Ivan J. Stone, Jamie B. Miyamoto, et al.. (2008). 507 POSTER Potent antitumor activity of the anti-CD19 auristatin antibody-drug conjugate hBU12-vcMMAE in rituximab sensitive and resistant lymphomas. European Journal of Cancer Supplements. 6(12). 161–161. 2 indexed citations
13.
Gerber, Hans‐Peter, Ivan J. Stone, Mechthild Jonas, et al.. (2007). Humanized anti-CD19 auristatin antibody-drug conjugates display potent antitumor activity in preclinical models of B-cell malignancies. Molecular Cancer Therapeutics. 6. 2 indexed citations
14.
Spiegel, Paul, B. Chevalier, Django Sussman, et al.. (2006). The Structure of I-CeuI Homing Endonuclease: Evolving Asymmetric DNA Recognition from a Symmetric Protein Scaffold. Structure. 14(5). 869–880. 27 indexed citations
15.
Rosen, Laura E., Holly A. Morrison, Selma Masri, et al.. (2006). Homing endonuclease I-CreI derivatives with novel DNA target specificities. Nucleic Acids Research. 34(17). 4791–4800. 76 indexed citations
16.
Ashworth, J. R., James J. Havranek, Carlos M. Duarte, et al.. (2006). Computational redesign of endonuclease DNA binding and cleavage specificity. Nature. 441(7093). 656–659. 256 indexed citations
17.
Sussman, Django, et al.. (2004). Isolation and Characterization of New Homing Endonuclease Specificities at Individual Target Site Positions. Journal of Molecular Biology. 342(1). 31–41. 60 indexed citations
18.
Sussman, Django & Charles B. Wilson. (2000). A water channel in the core of the vitamin B12 RNA aptamer. Structure. 8(7). 719–727. 21 indexed citations
19.
Sussman, Django, Chick C. Wilson, & Jay C. Nix. (2000). The structural basis for molecular recognition by the vitamin B 12 RNA aptamer.. Nature Structural Biology. 7(1). 53–57. 84 indexed citations
20.
Nix, Jay C., Django Sussman, & Chick C. Wilson. (2000). The 1.3 å crystal structure of a biotin-binding pseudoknot and the basis for RNA molecular recognition 1 1Edited by I. Tinoco. Journal of Molecular Biology. 296(5). 1235–1244. 44 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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