Christopher T. Veldkamp

1.8k total citations
29 papers, 1.4k citations indexed

About

Christopher T. Veldkamp is a scholar working on Oncology, Immunology and Molecular Biology. According to data from OpenAlex, Christopher T. Veldkamp has authored 29 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Oncology, 21 papers in Immunology and 18 papers in Molecular Biology. Recurrent topics in Christopher T. Veldkamp's work include Chemokine receptors and signaling (27 papers), Immunotherapy and Immune Responses (17 papers) and Glycosylation and Glycoproteins Research (14 papers). Christopher T. Veldkamp is often cited by papers focused on Chemokine receptors and signaling (27 papers), Immunotherapy and Immune Responses (17 papers) and Glycosylation and Glycoproteins Research (14 papers). Christopher T. Veldkamp collaborates with scholars based in United States, Denmark and Switzerland. Christopher T. Veldkamp's co-authors include Brian F. Volkman, Francis C. Peterson, Thomas P. Sakmar, Christoph Seibert, Joshua J. Ziarek, Harihar Basnet, Adam J. Pelzek, John Haugner, Norberto Cruz and Michael B. Dwinell and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Christopher T. Veldkamp

29 papers receiving 1.4k 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 T. Veldkamp United States 17 888 732 710 272 136 29 1.4k
Veronica Steri United States 17 827 0.9× 705 1.0× 796 1.1× 158 0.6× 122 0.9× 34 1.8k
Aldo Borroto Spain 18 329 0.4× 609 0.8× 365 0.5× 121 0.4× 129 0.9× 29 1.1k
Byron B. Au‐Yeung United States 17 423 0.5× 1.1k 1.5× 368 0.5× 118 0.4× 62 0.5× 27 1.5k
Namir J. Hassan United Kingdom 15 450 0.5× 557 0.8× 382 0.5× 169 0.6× 48 0.4× 26 1.1k
Sansana Sawasdikosol United States 22 381 0.4× 557 0.8× 699 1.0× 87 0.3× 87 0.6× 31 1.2k
Michael Kragh Denmark 23 753 0.8× 318 0.4× 509 0.7× 488 1.8× 87 0.6× 51 1.4k
Mina D. Marmor Israel 9 450 0.5× 233 0.3× 749 1.1× 166 0.6× 236 1.7× 9 1.2k
Gabriele Schaefer United States 17 899 1.0× 241 0.3× 900 1.3× 784 2.9× 63 0.5× 31 1.7k
Toru Fukazawa Japan 19 343 0.4× 895 1.2× 710 1.0× 393 1.4× 116 0.9× 39 1.7k
Jason W. Pyrdol United States 19 742 0.8× 1.9k 2.6× 601 0.8× 300 1.1× 43 0.3× 22 2.4k

Countries citing papers authored by Christopher T. Veldkamp

Since Specialization
Citations

This map shows the geographic impact of Christopher T. Veldkamp'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 T. Veldkamp with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Christopher T. Veldkamp more than expected).

Fields of papers citing papers by Christopher T. Veldkamp

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher T. Veldkamp

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher T. Veldkamp. A scholar is included among the top collaborators of Christopher T. Veldkamp 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 T. Veldkamp. Christopher T. Veldkamp 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.
Lewandowski, Eric M., Lian Jacobs, Xiujun Zhang, et al.. (2022). Structural Insights into Molecular Recognition by Human Chemokine CCL19. Biochemistry. 61(5). 311–318. 3 indexed citations
2.
Gutjahr, Julia, Kyler Crawford, Davin R. Jensen, et al.. (2021). The dimeric form of CXCL12 binds to atypical chemokine receptor 1. Science Signaling. 14(696). 22 indexed citations
3.
Egerod, Kristoffer L., Frederik Vilhardt, Paweł Kaliński, et al.. (2021). The C-terminal peptide of CCL21 drastically augments CCL21 activity through the dendritic cell lymph node homing receptor CCR7 by interaction with the receptor N-terminus. Cellular and Molecular Life Sciences. 78(21-22). 6963–6978. 17 indexed citations
4.
Larsen, Olav, Edith Uetz‐von Allmen, Michael Lückmann, et al.. (2019). Biased Signaling of CCL21 and CCL19 Does Not Rely on N-Terminal Differences, but Markedly on the Chemokine Core Domains and Extracellular Loop 2 of CCR7. Frontiers in Immunology. 10. 2156–2156. 16 indexed citations
5.
Ziarek, Joshua J., Andrew B. Kleist, Nir London, et al.. (2017). Structural basis for chemokine recognition by a G protein–coupled receptor and implications for receptor activation. Science Signaling. 10(471). 71 indexed citations
6.
Getschman, Anthony E., et al.. (2017). Differences in Sulfotyrosine Binding amongst CXCR1 and CXCR2 Chemokine Ligands. International Journal of Molecular Sciences. 18(9). 1894–1894. 15 indexed citations
7.
Veldkamp, Christopher T., et al.. (2016). Transferring the C-terminus of the chemokine CCL21 to CCL19 confers enhanced heparin binding. Biochemical and Biophysical Research Communications. 477(4). 602–606. 16 indexed citations
8.
Kiermaier, Eva, Christine Moussion, Christopher T. Veldkamp, et al.. (2015). Polysialylation controls dendritic cell trafficking by regulating chemokine recognition. Science. 351(6269). 186–190. 128 indexed citations
9.
Veldkamp, Christopher T., Davin R. Jensen, Francis C. Peterson, et al.. (2015). Production of Recombinant Chemokines and Validation of Refolding. Methods in enzymology on CD-ROM/Methods in enzymology. 570. 539–565. 32 indexed citations
10.
Seibert, Christoph, Anthony Sanfiz, Thomas P. Sakmar, & Christopher T. Veldkamp. (2015). Preparation and Analysis of N-Terminal Chemokine Receptor Sulfopeptides Using Tyrosylprotein Sulfotransferase Enzymes. Methods in enzymology on CD-ROM/Methods in enzymology. 570. 357–388. 7 indexed citations
11.
Phillips, Andrew J., et al.. (2014). The solution structure of the forkhead box‐ODNA binding domain of Brugia malayiDAF‐16a. Proteins Structure Function and Bioinformatics. 82(12). 3490–3496. 4 indexed citations
13.
Peterson, Francis C., et al.. (2012). Solution structure of the cold-shock-like protein fromRickettsia rickettsii. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(11). 1284–1288. 3 indexed citations
14.
Ziarek, Joshua J., et al.. (2011). Sulfotyrosine Recognition as Marker for Druggable Sites in the Extracellular Space. International Journal of Molecular Sciences. 12(6). 3740–3756. 15 indexed citations
15.
Veldkamp, Christopher T., Joshua J. Ziarek, Francis C. Peterson, Yu Chen, & Brian F. Volkman. (2010). Targeting SDF-1/CXCL12 with a Ligand That Prevents Activation of CXCR4 through Structure-Based Drug Design. Journal of the American Chemical Society. 132(21). 7242–7243. 59 indexed citations
16.
Veldkamp, Christopher T., Joshua J. Ziarek, Jidong Su, et al.. (2009). Monomeric structure of the cardioprotective chemokine SDF‐1/CXCL12. Protein Science. 18(7). 1359–1369. 69 indexed citations
17.
Veldkamp, Christopher T., Christoph Seibert, Francis C. Peterson, et al.. (2008). Structural Basis of CXCR4 Sulfotyrosine Recognition by the Chemokine SDF-1/CXCL12. Science Signaling. 1(37). ra4–ra4. 242 indexed citations
18.
Veldkamp, Christopher T., Christoph Seibert, Francis C. Peterson, Thomas P. Sakmar, & Brian F. Volkman. (2006). Recognition of a CXCR4 Sulfotyrosine by the Chemokine Stromal Cell-derived Factor-1α (SDF-1α/CXCL12). Journal of Molecular Biology. 359(5). 1400–1409. 105 indexed citations
19.
Veldkamp, Christopher T., et al.. (2006). On-column refolding of recombinant chemokines for NMR studies and biological assays. Protein Expression and Purification. 52(1). 202–209. 28 indexed citations
20.
Veldkamp, Christopher T., Francis C. Peterson, Adam J. Pelzek, & Brian F. Volkman. (2005). The monomer–dimer equilibrium of stromal cell‐derived factor‐1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin. Protein Science. 14(4). 1071–1081. 147 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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