Christopher S. Fraser

3.9k total citations
54 papers, 2.9k citations indexed

About

Christopher S. Fraser is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Organic Chemistry. According to data from OpenAlex, Christopher S. Fraser has authored 54 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 11 papers in Cardiology and Cardiovascular Medicine and 6 papers in Organic Chemistry. Recurrent topics in Christopher S. Fraser's work include RNA and protein synthesis mechanisms (36 papers), RNA Research and Splicing (19 papers) and RNA modifications and cancer (17 papers). Christopher S. Fraser is often cited by papers focused on RNA and protein synthesis mechanisms (36 papers), RNA Research and Splicing (19 papers) and RNA modifications and cancer (17 papers). Christopher S. Fraser collaborates with scholars based in United States, United Kingdom and Canada. Christopher S. Fraser's co-authors include Jennifer A. Doudna, John W.B. Hershey, Masaaki Sokabe, Julie A. Leary, Richard J. Puddephatt, Eva Nogales, Michael C. Jennings, Nancy Villa, Richard Hall and Bunpote Siridechadilok and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Christopher S. Fraser

54 papers receiving 2.9k 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 S. Fraser United States 30 2.3k 467 224 181 176 54 2.9k
Keqiong Ye China 30 2.9k 1.3× 92 0.2× 163 0.7× 51 0.3× 64 0.4× 71 3.7k
Ellen W. Moomaw United States 13 1.1k 0.5× 54 0.1× 81 0.4× 344 1.9× 137 0.8× 19 1.8k
Dixie J. Goss United States 33 2.6k 1.1× 335 0.7× 235 1.0× 22 0.1× 69 0.4× 102 3.4k
Peter V. Pallai United States 19 836 0.4× 250 0.5× 98 0.4× 34 0.2× 245 1.4× 30 1.8k
Peter J. Lukavsky United Kingdom 24 2.1k 0.9× 567 1.2× 88 0.4× 278 1.5× 43 0.2× 41 2.4k
John F. Milligan United States 13 3.7k 1.6× 207 0.4× 27 0.1× 42 0.2× 173 1.0× 16 4.0k
Jacqueline R. Wyatt United States 23 2.6k 1.1× 131 0.3× 32 0.1× 25 0.1× 357 2.0× 34 3.1k
Roman Sakowicz United States 28 1.9k 0.8× 98 0.2× 1.6k 7.4× 95 0.5× 146 0.8× 54 3.1k
Dwight D. Weller United States 22 1.8k 0.8× 67 0.1× 129 0.6× 24 0.1× 385 2.2× 44 2.4k
Ana González‐García Spain 28 1.3k 0.6× 62 0.1× 146 0.7× 24 0.1× 32 0.2× 51 2.3k

Countries citing papers authored by Christopher S. Fraser

Since Specialization
Citations

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

Fields of papers citing papers by Christopher S. Fraser

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher S. Fraser

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher S. Fraser. A scholar is included among the top collaborators of Christopher S. Fraser 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 S. Fraser. Christopher S. Fraser 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.
Villa, Nancy & Christopher S. Fraser. (2024). Human eukaryotic initiation factor 4G directly binds the 40S ribosomal subunit to promote efficient translation. Journal of Biological Chemistry. 300(5). 107242–107242. 4 indexed citations
2.
Asrat, Seblewongel, et al.. (2022). 5′ Untranslated mRNA Regions Allow Bypass of Host Cell Translation Inhibition by Legionella pneumophila. Infection and Immunity. 90(11). 13–e0017922. 3 indexed citations
3.
Lapointe, Christopher P., Rosslyn Grosely, Masaaki Sokabe, et al.. (2022). eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining. Nature. 607(7917). 185–190. 38 indexed citations
4.
Querido, Jailson Brito, Masaaki Sokabe, S.H.W. Kraatz, et al.. (2020). Structure of a human 48 S translational initiation complex. Science. 369(6508). 1220–1227. 149 indexed citations
5.
Sokabe, Masaaki & Christopher S. Fraser. (2018). Toward a Kinetic Understanding of Eukaryotic Translation. Cold Spring Harbor Perspectives in Biology. 11(2). a032706–a032706. 39 indexed citations
6.
Fuchs, Gabriele, et al.. (2017). Cellular cap-binding protein, eIF4E, promotes picornavirus genome restructuring and translation. Proceedings of the National Academy of Sciences. 114(36). 9611–9616. 40 indexed citations
7.
Frieda, Kirsten L., et al.. (2015). Factor-dependent processivity in human eIF4A DEAD-box helicase. Science. 348(6242). 1486–1488. 71 indexed citations
8.
Sidrauski, Carmela, Jordan C. Tsai, Martin Kampmann, et al.. (2015). Pharmacological dimerization and activation of the exchange factor eIF2B antagonizes the integrated stress response. eLife. 4. e07314–e07314. 187 indexed citations
9.
Villa, Nancy, et al.. (2013). Human Eukaryotic Initiation Factor 4G (eIF4G) Protein Binds to eIF3c, -d, and -e to Promote mRNA Recruitment to the Ribosome. Journal of Biological Chemistry. 288(46). 32932–32940. 120 indexed citations
10.
Frank, Filipp, et al.. (2013). Structural Analysis of the DAP5 MIF4G Domain and Its Interaction with eIF4A. Structure. 21(4). 517–527. 28 indexed citations
11.
Sokabe, Masaaki, Christopher S. Fraser, & John W.B. Hershey. (2011). The human translation initiation multi-factor complex promotes methionyl-tRNA i binding to the 40S ribosomal subunit. Nucleic Acids Research. 40(2). 905–913. 58 indexed citations
12.
Özeş, Ali, et al.. (2011). Duplex Unwinding and ATPase Activities of the DEAD-Box Helicase eIF4A Are Coupled by eIF4G and eIF4B. Journal of Molecular Biology. 412(4). 674–687. 85 indexed citations
13.
Lindqvist, Lisa, Françis Robert, William C. Merrick, et al.. (2010). Inhibition of translation by cytotrienin A—a member of the ansamycin family. RNA. 16(12). 2404–2413. 17 indexed citations
14.
Fraser, Christopher S.. (2009). Chapter 1 The Molecular Basis of Translational Control. Progress in molecular biology and translational science. 90. 1–51. 13 indexed citations
15.
Damoc, Eugen, Christopher S. Fraser, Min Zhou, et al.. (2007). Structural Characterization of the Human Eukaryotic Initiation Factor 3 Protein Complex by Mass Spectrometry. Molecular & Cellular Proteomics. 6(7). 1135–1146. 104 indexed citations
16.
Fraser, Christopher S., Katherine E. Berry, John W.B. Hershey, & Jennifer A. Doudna. (2007). eIF3j Is Located in the Decoding Center of the Human 40S Ribosomal Subunit. Molecular Cell. 26(6). 811–819. 102 indexed citations
17.
18.
Fraser, Christopher S. & Jennifer A. Doudna. (2007). Quantitative studies of ribosome conformational dynamics. Quarterly Reviews of Biophysics. 40(2). 163–189. 5 indexed citations
19.
Siridechadilok, Bunpote, Christopher S. Fraser, Richard Hall, Jennifer A. Doudna, & Eva Nogales. (2005). Structural Roles for Human Translation Factor eIF3 in Initiation of Protein Synthesis. Science. 310(5753). 1513–1515. 225 indexed citations
20.
Fraser, Christopher S., Virginia M. Pain, & Simon Morley. (1999). The Association of Initiation Factor 4F with Poly(A)-binding Protein Is Enhanced in Serum-stimulated Xenopus Kidney Cells. Journal of Biological Chemistry. 274(1). 196–204. 59 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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