Christopher A. Pargellis

1.3k total citations
17 papers, 1.1k citations indexed

About

Christopher A. Pargellis is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, Christopher A. Pargellis has authored 17 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 4 papers in Organic Chemistry and 4 papers in Oncology. Recurrent topics in Christopher A. Pargellis's work include Melanoma and MAPK Pathways (9 papers), Protein Kinase Regulation and GTPase Signaling (5 papers) and Computational Drug Discovery Methods (4 papers). Christopher A. Pargellis is often cited by papers focused on Melanoma and MAPK Pathways (9 papers), Protein Kinase Regulation and GTPase Signaling (5 papers) and Computational Drug Discovery Methods (4 papers). Christopher A. Pargellis collaborates with scholars based in United States, France and Japan. Christopher A. Pargellis's co-authors include Arthur Landy, Lina Moitoso de Vargas, Susan Pav, Simone E. Nunes-Düby, Liang Tong, Della White, Charles L. Cywin, K. Crane, Sheri Rogers and Maryanne L. Brown and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Christopher A. Pargellis

17 papers receiving 1.1k citations

Peers

Christopher A. Pargellis

GENET

ONCOL

CTM

Robin A. Weinberg United States

Chunli Yan United States

Robert B. Lobell United States

Kush Dalal Canada

Klaus Godl Germany

D. Ogg United Kingdom

Till Maurer Germany

Sonja Baumli United Kingdom

Maria R. Conte United Kingdom

Dirk Brehmer Belgium

Robin A. Weinberg United States

Christopher A. Pargellis

802 ×0.9

122 ×0.6

157 ×0.8

GENET

204 ×1.1

ONCOL

51 ×0.3

CTM

Citations per year, relative to Christopher A. Pargellis Christopher A. Pargellis (= 1×) peers Robin A. Weinberg

Countries citing papers authored by Christopher A. Pargellis

Since Specialization

Citations

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

Fields of papers citing papers by Christopher A. Pargellis

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher A. Pargellis

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

All Works

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17 of 17 papers shown

Gruenbaum, Lore, Joseph R. Woska, Gregory W. Peet, et al.. (2008). Inhibition of pro-inflammatory cytokine production by the dual p38/JNK2 inhibitor BIRB796 correlates with the inhibition of p38 signaling. Biochemical Pharmacology. 77(3). 422–432. 27 indexed citations

White, André, Christopher A. Pargellis, Joey Studts, Brian Werneburg, & Bennett T. Farmer. (2007). Molecular basis of MAPK-activated protein kinase 2:p38 assembly. Proceedings of the National Academy of Sciences. 104(15). 6353–6358. 94 indexed citations

Moss, Neil, Steffen Breitfelder, Raj Betageri, et al.. (2007). New modifications to the area of pyrazole-naphthyl urea based p38 MAP kinase inhibitors that bind to the adenine/ATP site. Bioorganic & Medicinal Chemistry Letters. 17(15). 4242–4247. 10 indexed citations

Lukas, Susan, Rachel Kroe‐Barrett, Gregory W. Peet, et al.. (2004). Catalysis and Function of the p38α·MK2a Signaling Complex. Biochemistry. 43(31). 9950–9960. 47 indexed citations

Kroe‐Barrett, Rachel, John R. Regan, Gregory W. Peet, et al.. (2003). Thermal Denaturation: A Method to Rank Slow Binding, High-Affinity P38α MAP Kinase Inhibitors. Journal of Medicinal Chemistry. 46(22). 4669–4675. 36 indexed citations

Regan, John R., Christopher A. Pargellis, Pier F. Cirillo, et al.. (2003). The kinetics of binding to p38 MAP kinase by analogues of BIRB 796. Bioorganic & Medicinal Chemistry Letters. 13(18). 3101–3104. 92 indexed citations

Regan, John R., Pier F. Cirillo, Thomas D. Gilmore, et al.. (2003). Structure−Activity Relationships of the p38α MAP Kinase Inhibitor 1-(5-tert-Butyl-2-p-tolyl-2H-pyrazol-3-yl)-3-[4-(2-morpholin-4-yl-ethoxy)naph- thalen-1-yl]urea (BIRB 796). Journal of Medicinal Chemistry. 46(22). 4676–4686. 84 indexed citations

Pav, Susan, Della White, Sheri Rogers, et al.. (1997). Crystallization and preliminary crystallographic analysis of recombinant human p38 MAP kinase. Protein Science. 6(1). 242–245. 15 indexed citations

Pargellis, Christopher A., et al.. (1997). Inhibition of Dipeptidyl Peptidase iv (CD26) by Peptide Boronic Acid Dipeptides. Journal of enzyme inhibition. 11(3). 151–169. 4 indexed citations

10.

Tong, Liang, Susan Pav, Della White, et al.. (1997). A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket. Nature Structural Biology. 4(4). 311–316. 337 indexed citations

11.

Morelock, Maurice M., et al.. (1996). Kinetic Characterization of Human Immunodeficiency Virus Type 1 Protease: Determination of Inhibitor Rate Constants during Dynamic Monomer–Dimer Interconversion. Archives of Biochemistry and Biophysics. 328(2). 317–323. 1 indexed citations

12.

Jeanfavre, Deborah D., Joseph R. Woska, Christopher A. Pargellis, et al.. (1996). Effect of deoxycoformycin and Val-boroPro on the associated catalytic activities of lymphocyte CD26 and ecto-adenosine deaminase. Biochemical Pharmacology. 52(11). 1757–1765. 9 indexed citations

13.

Tirumalai, Radhakrishna S., Christopher A. Pargellis, & Arthur Landy. (1996). Identification and Characterization of the N-Ethylmaleimide-sensitive Site in λ-Integrase. Journal of Biological Chemistry. 271(47). 29599–29604. 12 indexed citations

14.

Morelock, Maurice M., et al.. (1995). Time-Resolved Ligand Exchange Reactions: Kinetic Models for Competitive Inhibitors with Recombinant Human Renin. Journal of Medicinal Chemistry. 38(10). 1751–1761. 12 indexed citations

15.

Pargellis, Christopher A., et al.. (1994). Determination of Kinetic Rate Constants for the Binding of Inhibitors to HIV-1 Protease and for the Association and Dissociation of Active Homodimer. Biochemistry. 33(41). 12527–12534. 24 indexed citations

16.

Vargas, Lina Moitoso de, et al.. (1988). Autonomous DNA binding domains of λ integrase recognize two different sequence families. Cell. 54(7). 923–929. 138 indexed citations

17.

Pargellis, Christopher A., Simone E. Nunes-Düby, Lina Moitoso de Vargas, & Arthur Landy. (1988). Suicide recombination substrates yield covalent lambda integrase-DNA complexes and lead to identification of the active site tyrosine.. Journal of Biological Chemistry. 263(16). 7678–7685. 178 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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