Travis Stams

3.6k total citations
18 papers, 1.2k citations indexed

About

Travis Stams is a scholar working on Molecular Biology, Oncology and Immunology. According to data from OpenAlex, Travis Stams has authored 18 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 4 papers in Oncology and 4 papers in Immunology. Recurrent topics in Travis Stams's work include Enzyme function and inhibition (3 papers), Protein Tyrosine Phosphatases (3 papers) and Bacterial Genetics and Biotechnology (3 papers). Travis Stams is often cited by papers focused on Enzyme function and inhibition (3 papers), Protein Tyrosine Phosphatases (3 papers) and Bacterial Genetics and Biotechnology (3 papers). Travis Stams collaborates with scholars based in United States, China and Switzerland. Travis Stams's co-authors include David W. Christianson, Carol A. Fierke, Niranjanakumari Somashekarappa, Sharon M. Crary, Michael D. Shultz, Abdül Waheed, William S. Sly, Satish K. Nair, David W. Christianson and Torayuki Okuyama and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Nature Communications.

In The Last Decade

Travis Stams

18 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Travis Stams United States 15 983 270 162 157 139 18 1.2k
Robert B. Lobell United States 18 991 1.0× 258 1.0× 232 1.4× 236 1.5× 155 1.1× 30 1.4k
John A. Newitt United States 16 790 0.8× 162 0.6× 207 1.3× 342 2.2× 63 0.5× 25 1.5k
Wai-Kwong Eng United States 15 1.2k 1.2× 388 1.4× 84 0.5× 43 0.3× 81 0.6× 15 1.3k
Stephen M. Coutts Germany 16 533 0.5× 184 0.7× 126 0.8× 56 0.4× 105 0.8× 43 996
Bainan Wu United States 22 880 0.9× 244 0.9× 150 0.9× 69 0.4× 103 0.7× 28 1.2k
Barbara Valsasina Italy 23 978 1.0× 292 1.1× 173 1.1× 93 0.6× 119 0.9× 42 1.5k
Tatiana V. Rakitina Russia 17 639 0.7× 147 0.5× 57 0.4× 89 0.6× 53 0.4× 94 907
Jordi Frigola Spain 16 1.2k 1.2× 142 0.5× 194 1.2× 251 1.6× 23 0.2× 42 1.6k
Gongqin Sun United States 24 1.1k 1.1× 273 1.0× 188 1.2× 51 0.3× 142 1.0× 77 1.4k
Arsenio Nueda Spain 18 622 0.6× 109 0.4× 97 0.6× 45 0.3× 229 1.6× 29 959

Countries citing papers authored by Travis Stams

Since Specialization
Citations

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

Fields of papers citing papers by Travis Stams

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Travis Stams

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

All Works

18 of 18 papers shown
1.
LaRochelle, Jonathan R., Michelle Fodor, Vidyasiri Vemulapalli, et al.. (2018). Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition. Nature Communications. 9(1). 4508–4508. 105 indexed citations
2.
Chopra, Rajiv, Ruth E. Caughlan, Doriano Fabbro, et al.. (2018). Acylated-acyl carrier protein stabilizes the Pseudomonas aeruginosa WaaP lipopolysaccharide heptose kinase. Scientific Reports. 8(1). 14124–14124. 7 indexed citations
3.
Camargo, Luiz Miguel, Mary Ellen Digan, Honglin Niu, et al.. (2017). A NMDA-receptor calcium influx assay sensitive to stimulation by glutamate and glycine/D-serine. Scientific Reports. 7(1). 11608–11608. 44 indexed citations
4.
Hu, Tiancen, Elizabeth R. Sprague, Michelle Fodor, et al.. (2017). The impact of structural biology in medicine illustrated with four case studies. Journal of Molecular Medicine. 96(1). 9–19. 7 indexed citations
5.
LaRochelle, Jonathan R., Michelle Fodor, Jana M. Ellegast, et al.. (2017). Identification of an allosteric benzothiazolopyrimidone inhibitor of the oncogenic protein tyrosine phosphatase SHP2. Bioorganic & Medicinal Chemistry. 25(24). 6479–6485. 33 indexed citations
6.
LaRochelle, Jonathan R., Michelle Fodor, Xiang Xu, et al.. (2016). Structural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2. Biochemistry. 55(15). 2269–2277. 46 indexed citations
7.
Shultz, Michael D., Dyuti Majumdar, Donovan N. Chin, et al.. (2013). Structure–Efficiency Relationship of [1,2,4]Triazol-3-ylamines as Novel Nicotinamide Isosteres that Inhibit Tankyrases. Journal of Medicinal Chemistry. 56(17). 7049–7059. 24 indexed citations
8.
Kirby, C.A., Atwood K. Cheung, Aleem Fazal, Michael D. Shultz, & Travis Stams. (2012). Structure of human tankyrase 1 in complex with small-molecule inhibitors PJ34 and XAV939. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(2). 115–118. 41 indexed citations
9.
Shultz, Michael D., C.A. Kirby, Travis Stams, et al.. (2012). [1,2,4]Triazol-3-ylsulfanylmethyl)-3-phenyl-[1,2,4]oxadiazoles: Antagonists of the Wnt Pathway That Inhibit Tankyrases 1 and 2 via Novel Adenosine Pocket Binding. Journal of Medicinal Chemistry. 55(3). 1127–1136. 58 indexed citations
10.
Whitehead, Lewis, Markus Dobler, Branko Radetich, et al.. (2011). Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors. Bioorganic & Medicinal Chemistry. 19(15). 4626–4634. 129 indexed citations
11.
Kulathila, Raviraj, David R. Sage, Susan Cornell-Kennon, et al.. (2008). The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9. Acta Crystallographica Section D Biological Crystallography. 65(1). 58–66. 28 indexed citations
12.
Stams, Travis & David W. Christianson. (2000). X-ray crystallographic studies of mammalian carbonic anhydrase isozymes. Birkhäuser Basel eBooks. 159–174. 40 indexed citations
13.
Stams, Travis, Yun Chen, David W. Christianson, et al.. (1998). Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme‐drug discrimination. Protein Science. 7(3). 556–563. 83 indexed citations
14.
Stams, Travis, Niranjanakumari Somashekarappa, Carol A. Fierke, & David W. Christianson. (1998). Ribonuclease P Protein Structure: Evolutionary Origins in the Translational Apparatus. Science. 280(5364). 752–755. 122 indexed citations
15.
Somashekarappa, Niranjanakumari, Travis Stams, Sharon M. Crary, David W. Christianson, & Carol A. Fierke. (1998). Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA. Proceedings of the National Academy of Sciences. 95(26). 15212–15217. 140 indexed citations
16.
Stams, Travis, Satish K. Nair, Torayuki Okuyama, et al.. (1996). Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-Å resolution. Proceedings of the National Academy of Sciences. 93(24). 13589–13594. 117 indexed citations
17.
Malinowski, John, Bruce Grasberger, G M Trakshel, et al.. (1995). Production, purification, and crystallization of human interleukin‐1β converting enzyme derived from an Escherichia coli expression system. Protein Science. 4(10). 2149–2155. 4 indexed citations
18.
Stams, Travis, John Spurlino, Douglas L. Smith, et al.. (1994). Structure of human neutrophil collagenase reveals large S1′ specificity pocket. Nature Structural & Molecular Biology. 1(2). 119–123. 134 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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