Mark A. Currie

585 total citations
18 papers, 406 citations indexed

About

Mark A. Currie is a scholar working on Molecular Biology, Plant Science and Biomedical Engineering. According to data from OpenAlex, Mark A. Currie has authored 18 papers receiving a total of 406 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 8 papers in Plant Science and 4 papers in Biomedical Engineering. Recurrent topics in Mark A. Currie's work include Genomics and Chromatin Dynamics (5 papers), Biofuel production and bioconversion (4 papers) and Polysaccharides and Plant Cell Walls (4 papers). Mark A. Currie is often cited by papers focused on Genomics and Chromatin Dynamics (5 papers), Biofuel production and bioconversion (4 papers) and Polysaccharides and Plant Cell Walls (4 papers). Mark A. Currie collaborates with scholars based in Canada, United States and Israel. Mark A. Currie's co-authors include Danesh Moazed, Nahid Iglesias, Gloria Jih, João A. Paulo, Zongchao Jia, Steven P. Gygi, Edward A. Bayer, Steven P. Smith, Natarajan V. Bhanu and Benjamin A. García 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

Mark A. Currie

17 papers receiving 404 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mark A. Currie Canada 11 319 98 65 43 25 18 406
Juliana Helena Costa Smetana Brazil 11 219 0.7× 94 1.0× 68 1.0× 65 1.5× 11 0.4× 18 334
Pascal Martinez France 12 504 1.6× 118 1.2× 30 0.5× 47 1.1× 20 0.8× 14 605
Bang Wang China 14 419 1.3× 86 0.9× 168 2.6× 38 0.9× 19 0.8× 23 485
Julien Fey United States 10 231 0.7× 54 0.6× 74 1.1× 29 0.7× 8 0.3× 14 359
Gianni Frascotti Italy 12 297 0.9× 29 0.3× 58 0.9× 20 0.5× 44 1.8× 20 381
Ronald I. W. Osmond Australia 7 209 0.7× 83 0.8× 34 0.5× 10 0.2× 19 0.8× 9 400
Yoko Motoda Japan 13 309 1.0× 77 0.8× 32 0.5× 52 1.2× 25 1.0× 20 404
Søren Møgelsvang United States 9 380 1.2× 108 1.1× 36 0.6× 21 0.5× 6 0.2× 9 522
Meihui Song China 9 265 0.8× 44 0.4× 76 1.2× 79 1.8× 10 0.4× 14 327
Verena Puxbaum Austria 12 509 1.6× 34 0.3× 105 1.6× 89 2.1× 10 0.4× 15 613

Countries citing papers authored by Mark A. Currie

Since Specialization
Citations

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

Fields of papers citing papers by Mark A. Currie

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mark A. Currie

This figure shows the co-authorship network connecting the top 25 collaborators of Mark A. Currie. A scholar is included among the top collaborators of Mark A. Currie 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 Mark A. Currie. Mark A. Currie 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.
Auld, Douglas S., et al.. (2024). Tight-Binding Small-Molecule Carboxylesterase 2 Inhibitors Reduce Intracellular Irinotecan Activation. Journal of Medicinal Chemistry. 67(3). 2019–2030. 2 indexed citations
2.
Bergman, Matthew E., et al.. (2024). Plastid ancestors lacked a complete Entner-Doudoroff pathway, limiting plants to glycolysis and the pentose phosphate pathway. Nature Communications. 15(1). 1102–1102. 9 indexed citations
3.
Erclik, Ted, et al.. (2024). Mint/X11 PDZ domains from non-bilaterian animals recognize and bind CaV2 calcium channel C-termini in vitro. Scientific Reports. 14(1). 21615–21615.
4.
Yáñez-Guerra, Luis Alfonso, et al.. (2023). Function and phylogeny support the independent evolution of an ASIC-like Deg/ENaC channel in the Placozoa. Communications Biology. 6(1). 951–951. 13 indexed citations
5.
Currie, Mark A., et al.. (2022). Targets of histone H3 lysine 9 methyltransferases. Frontiers in Cell and Developmental Biology. 10. 1026406–1026406. 7 indexed citations
6.
Ringel, Alison E., William Yuan, João A. Paulo, et al.. (2021). Development of a colorimetric α-ketoglutarate detection assay for prolyl hydroxylase domain (PHD) proteins. Journal of Biological Chemistry. 296. 100397–100397. 15 indexed citations
7.
Iglesias, Nahid, Mark A. Currie, Gloria Jih, et al.. (2018). Automethylation-induced conformational switch in Clr4 (Suv39h) maintains epigenetic stability. Nature. 560(7719). 504–508. 57 indexed citations
8.
Jih, Gloria, Nahid Iglesias, Mark A. Currie, et al.. (2017). Unique roles for histone H3K9me states in RNAi and heritable silencing of transcription. Nature. 547(7664). 463–467. 86 indexed citations
9.
Currie, Mark A., Greg Brown, Andrew Wong, et al.. (2016). Structural and functional characterization of the TYW3/Taw3 class of SAM-dependent methyltransferases. RNA. 23(3). 346–354. 10 indexed citations
10.
Behrouzi, Reza, et al.. (2016). Heterochromatin assembly by interrupted Sir3 bridges across neighboring nucleosomes. eLife. 5. 25 indexed citations
11.
Currie, Mark A., Kate Cameron, Fernando M. V. Dias, et al.. (2013). Small Angle X-ray Scattering Analysis of Clostridium thermocellum Cellulosome N-terminal Complexes Reveals a Highly Dynamic Structure. Journal of Biological Chemistry. 288(11). 7978–7985. 21 indexed citations
12.
Ye, Qilu, Yanxia Yin, Frédérick Faucher, et al.. (2013). Structural basis of calcineurin activation by calmodulin. Cellular Signalling. 25(12). 2661–2667. 23 indexed citations
13.
Wang, Feng, Geng Li, Mohammad Altaf, et al.. (2013). Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA. Proceedings of the National Academy of Sciences. 110(21). 8495–8500. 50 indexed citations
14.
Currie, Mark A., Jarrett Adams, Frédérick Faucher, et al.. (2012). Scaffoldin Conformation and Dynamics Revealed by a Ternary Complex from the Clostridium thermocellum Cellulosome. Journal of Biological Chemistry. 287(32). 26953–26961. 30 indexed citations
15.
16.
Currie, Mark A., et al.. (2010). Purification and crystallization of a multimodular heterotrimeric complex containing both type I and type II cohesin–dockerin interactions from the cellulosome ofClostridium thermocellum. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(3). 327–329. 3 indexed citations
17.
Currie, Mark A., Felipe Merino, T. Skarina, et al.. (2009). ADP-dependent 6-Phosphofructokinase from Pyrococcus horikoshii OT3. Journal of Biological Chemistry. 284(34). 22664–22671. 22 indexed citations
18.
Matte, Allan, Guennadi Kozlov, Jean‐François Trempe, et al.. (2009). Preparation and Characterization of Bacterial Protein Complexes for Structural Analysis. Advances in protein chemistry and structural biology. 76. 1–42. 3 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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