Chris Dealwis

2.4k total citations
51 papers, 1.7k citations indexed

About

Chris Dealwis is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Chris Dealwis has authored 51 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Molecular Biology, 22 papers in Materials Chemistry and 18 papers in Oncology. Recurrent topics in Chris Dealwis's work include Metal-Catalyzed Oxygenation Mechanisms (18 papers), Enzyme Structure and Function (17 papers) and Protein Structure and Dynamics (12 papers). Chris Dealwis is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (18 papers), Enzyme Structure and Function (17 papers) and Protein Structure and Dynamics (12 papers). Chris Dealwis collaborates with scholars based in United States, United Kingdom and China. Chris Dealwis's co-authors include Elias Lolis, B. Bennett, Shabbir Ahmad, Hai Xu, Tomoaki Uchiki, Jodi B. Lubetsky, Paul R. Blake, Włodek Mandecki, Paul Langan and J.W. Fairman and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Chris Dealwis

51 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Chris Dealwis United States 24 968 381 333 274 255 51 1.7k
Marjolein Thunnissen Sweden 22 967 1.0× 341 0.9× 247 0.7× 73 0.3× 194 0.8× 44 1.7k
Bernard Gsell Switzerland 17 907 0.9× 200 0.5× 244 0.7× 157 0.6× 126 0.5× 19 1.7k
M. Stihle Switzerland 23 1.7k 1.8× 315 0.8× 324 1.0× 199 0.7× 362 1.4× 29 2.8k
Irimpan I. Mathews United States 33 1.8k 1.9× 435 1.1× 583 1.8× 151 0.6× 340 1.3× 85 3.1k
Steven R. Jordan United States 24 2.2k 2.3× 501 1.3× 280 0.8× 84 0.3× 214 0.8× 46 3.2k
B.A. Katz United States 27 1.3k 1.3× 391 1.0× 334 1.0× 89 0.3× 213 0.8× 49 2.5k
S. Terzyan United States 25 1.1k 1.1× 256 0.7× 226 0.7× 116 0.4× 118 0.5× 53 2.2k
Stephen F. Betz United States 24 2.6k 2.7× 325 0.9× 616 1.8× 180 0.7× 177 0.7× 58 3.1k
Robert X. Xu United States 22 1.5k 1.6× 339 0.9× 247 0.7× 54 0.2× 206 0.8× 30 2.3k
Yan Ling United States 23 1.0k 1.1× 230 0.6× 133 0.4× 116 0.4× 183 0.7× 60 1.8k

Countries citing papers authored by Chris Dealwis

Since Specialization
Citations

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

Fields of papers citing papers by Chris Dealwis

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Chris Dealwis

This figure shows the co-authorship network connecting the top 25 collaborators of Chris Dealwis. A scholar is included among the top collaborators of Chris Dealwis 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 Chris Dealwis. Chris Dealwis 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.
Wan, Qun, B. Bennett, Troy Wymore, et al.. (2021). Capturing the Catalytic Proton of Dihydrofolate Reductase: Implications for General Acid–Base Catalysis. ACS Catalysis. 11(9). 5873–5884. 9 indexed citations
2.
Ahmad, Shabbir, Sarah Huff, John J. Pink, et al.. (2015). Identification of Non-nucleoside Human Ribonucleotide Reductase Modulators. Journal of Medicinal Chemistry. 58(24). 9498–9509. 14 indexed citations
3.
Wan, Qun, Andrey Kovalevsky, Mark A. Wilson, et al.. (2014). Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+. Acta Crystallographica Section F Structural Biology Communications. 70(6). 814–818. 7 indexed citations
4.
Ahmad, Shabbir, et al.. (2012). Evaluating the Therapeutic Potential of a Non-Natural Nucleotide That Inhibits Human Ribonucleotide Reductase. Molecular Cancer Therapeutics. 11(10). 2077–2086. 6 indexed citations
5.
Wan, Qun, Shabbir Ahmad, J.W. Fairman, et al.. (2011). X-Ray Crystallography and Isothermal Titration Calorimetry Studies of the Salmonella Zinc Transporter ZntB. Structure. 19(5). 700–710. 23 indexed citations
6.
Miyagi, Masaru, Qun Wan, Shabbir Ahmad, et al.. (2011). Histidine Hydrogen-Deuterium Exchange Mass Spectrometry for Probing the Microenvironment of Histidine Residues in Dihydrofolate Reductase. PLoS ONE. 6(2). e17055–e17055. 27 indexed citations
7.
Minami, Sakura, Elkhansa Sidahmed, Saba Aïd, et al.. (2010). Therapeutic versus neuroinflammatory effects of passive immunization is dependent on Aβ/amyloid burden in a transgenic mouse model of Alzheimer's disease. Journal of Neuroinflammation. 7(1). 57–57. 19 indexed citations
8.
Gardberg, A.S., Lezlee Dice, Jan Ko, et al.. (2009). Structures of Aβ-Related Peptide−Monoclonal Antibody Complexes,. Biochemistry. 48(23). 5210–5217. 13 indexed citations
9.
Bennett, B., Qun Wan, Shabbir Ahmad, Paul Langan, & Chris Dealwis. (2009). X-ray structure of the ternary MTX·NADPH complex of the anthrax dihydrofolate reductase: A pharmacophore for dual-site inhibitor design. Journal of Structural Biology. 166(2). 162–171. 22 indexed citations
10.
Gardberg, A.S., Lezlee Dice, Susan Ou, et al.. (2007). Molecular basis for passive immunotherapy of Alzheimer's disease. Proceedings of the National Academy of Sciences. 104(40). 15659–15664. 94 indexed citations
11.
Xu, Hai, et al.. (2006). Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation. Proceedings of the National Academy of Sciences. 103(11). 4022–4027. 63 indexed citations
12.
Wall, Jonathan S., Vibha Gupta, Matthew D. Wilkerson, et al.. (2004). Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vλ6 proteins. Journal of Molecular Recognition. 17(4). 323–331. 62 indexed citations
13.
Dealwis, Chris & Jonathan S. Wall. (2004). Towards Understanding the Structure-Function Relationship of Human Amyloid Disease. Current Drug Targets. 5(2). 159–171. 21 indexed citations
14.
Uchiki, Tomoaki, et al.. (2002). Characterization of Monomeric and Dimeric Forms of Recombinant Sml1p-histag Protein by Electrospray Mass Spectrometry. Analytical Biochemistry. 301(1). 35–48. 8 indexed citations
15.
Aguilar, C. F., V. Dhanaraj, Kunchur Guruprasad, et al.. (1995). Comparisons of the Three-Dimensional Structures, Specificities and Glycosylation of Renins, Yeast Proteinase A and Cathepsin D. Advances in experimental medicine and biology. 362. 155–166. 6 indexed citations
16.
Dealwis, Chris, Carlos Frazão, M. Badasso, et al.. (1994). X-ray Analysis at 2·0 Å Resolution of Mouse Submaxillary Renin Complexed with a Decapeptide Inhibitor CH-66, Based on the 4-16 Fragment of Rat Angiotensinogen. Journal of Molecular Biology. 236(1). 342–360. 34 indexed citations
17.
Lisgarten, J. N., Dominique Maes, L. Wyns, et al.. (1993). Structure of the crystalline complex of cytidylic acid (2'-CMP) with ribonuclease at 1.6 Å resolution. Conservation of solvent sites in RNase-A high-resolution structures. Acta Crystallographica Section D Biological Crystallography. 49(6). 541–547. 30 indexed citations
18.
Dhanaraj, V., Chris Dealwis, Carlos Frazão, et al.. (1992). X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature. 357(6378). 466–472. 102 indexed citations
19.
Badasso, M., B. L. Sibanda, J.B. Cooper, Chris Dealwis, & S. P. Wood. (1992). Crystal quality and inhibitor binding by aspartic proteinases; preparation of high quality crystals of mouse renin. Journal of Crystal Growth. 122(1-4). 393–399. 3 indexed citations
20.
Pitts, Jim E., V. Dhanaraj, Chris Dealwis, et al.. (1992). Multidisciplinary cycles for protein engineering: Site-directed mutagenesis and X-ray structural studies of aspartic proteinases. Scandinavian Journal of Clinical and Laboratory Investigation. 52(sup210). 39–50. 18 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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