C. Smits

1.1k total citations
17 papers, 858 citations indexed

About

C. Smits is a scholar working on Molecular Biology, Ecology and Materials Chemistry. According to data from OpenAlex, C. Smits has authored 17 papers receiving a total of 858 indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 6 papers in Ecology and 4 papers in Materials Chemistry. Recurrent topics in C. Smits's work include RNA and protein synthesis mechanisms (8 papers), Bacteriophages and microbial interactions (6 papers) and Enzyme Structure and Function (4 papers). C. Smits is often cited by papers focused on RNA and protein synthesis mechanisms (8 papers), Bacteriophages and microbial interactions (6 papers) and Enzyme Structure and Function (4 papers). C. Smits collaborates with scholars based in United Kingdom, Australia and United States. C. Smits's co-authors include Catherine L. Day, Mark G. Hinds, W. Douglas Fairlie, Erinna F. Lee, Fengjuan Fan, Joanna M. Risk, David C.S. Huang, Michael Bailey, Peter E. Czabotar and Andrew S. W. Wong and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and PLoS ONE.

In The Last Decade

C. Smits

17 papers receiving 852 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
C. Smits United Kingdom	12	745	121	99	92	80	17	858
Yvette Roske Germany	19	744 1.0×	111 0.9×	51 0.5×	143 1.6×	70 0.9×	43	1.1k
Gorka Lasso United States	14	564 0.8×	62 0.5×	97 1.0×	50 0.5×	85 1.1×	22	876
Kim Van Roey Germany	9	1.3k 1.7×	66 0.5×	92 0.9×	90 1.0×	164 2.0×	11	1.5k
Paul G. Leonard United States	21	794 1.1×	119 1.0×	127 1.3×	84 0.9×	57 0.7×	27	1.1k
N.D. Thomsen United States	13	890 1.2×	89 0.7×	98 1.0×	53 0.6×	57 0.7×	14	1.0k
Etsuko Miyamoto‐Sato Japan	18	1.4k 1.9×	96 0.8×	75 0.8×	86 0.9×	29 0.4×	33	1.6k
Yuliya Gordiyenko United Kingdom	21	1.3k 1.7×	99 0.8×	129 1.3×	53 0.6×	86 1.1×	32	1.5k
Stephen L. Sazinsky United States	10	1.2k 1.7×	62 0.5×	166 1.7×	280 3.0×	91 1.1×	15	1.6k
Takuhiro Ito Japan	26	1.4k 1.9×	49 0.4×	87 0.9×	81 0.9×	105 1.3×	58	1.7k
Lester Carter United Kingdom	6	541 0.7×	58 0.5×	43 0.4×	42 0.5×	105 1.3×	11	773

Countries citing papers authored by C. Smits

Since Specialization

Citations

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

Fields of papers citing papers by C. Smits

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of C. Smits

This figure shows the co-authorship network connecting the top 25 collaborators of C. Smits. A scholar is included among the top collaborators of C. Smits 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 C. Smits. C. Smits 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

Low, Jason K. K., Ana P. G. Silva, Mehdi Sharifi Tabar, et al.. (2020). The Nucleosome Remodeling and Deacetylase Complex Has an Asymmetric, Dynamic, and Modular Architecture. Cell Reports. 33(9). 108450–108450. 33 indexed citations

Smits, C., Andrew S. W. Wong, Daniela Stock, et al.. (2017). Cryo-EM analysis of a domain antibody bound rotary ATPase complex. Journal of Structural Biology. 197(3). 350–353. 6 indexed citations

Smits, C., David Aragão, Andrew S. W. Wong, et al.. (2016). Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins. Structure. 24(3). 364–374. 20 indexed citations

Sobti, Meghna, C. Smits, Andrew S. W. Wong, et al.. (2016). Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states. eLife. 5. 112 indexed citations

Levdikov, V.M., et al.. (2013). The putative small terminase from the thermophilic dsDNA bacteriophage G20C is a nine-subunit oligomer. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(8). 876–879. 7 indexed citations

Luan, Weisha, et al.. (2012). Recombinant portal protein fromStaphylococcus epidermidisbacteriophage CNPH82 is a 13-subunit oligomer. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(10). 1267–1270. 2 indexed citations

Jacquet, Eric, et al.. (2012). The nuclease domain of the SPP1 packaging motor coordinates DNA cleavage and encapsidation. Nucleic Acids Research. 41(1). 340–354. 29 indexed citations

Bayfield, Oliver W., Chao-Sheng Chen, Andrea Patterson, et al.. (2012). Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer. PLoS ONE. 7(9). e44309–e44309. 6 indexed citations

Chen, Chao-Sheng, C. Smits, Guy Dodson, et al.. (2011). How to Change the Oligomeric State of a Circular Protein Assembly: Switch from 11-Subunit to 12-Subunit TRAP Suggests a General Mechanism. PLoS ONE. 6(10). e25296–e25296. 11 indexed citations

10.

Büttner, Carina R., M. Ortiz-Lombardı́a, C. Smits, et al.. (2011). Structural basis for DNA recognition and loading into a viral packaging motor. Proceedings of the National Academy of Sciences. 109(3). 811–816. 51 indexed citations

11.

Silva, Ana P. G., David G. Waterman, Chyan Leong Ng, et al.. (2011). Structure and Activity of a Novel Archaeal β-CASP Protein with N-Terminal KH Domains. Structure. 19(5). 622–632. 23 indexed citations

12.

Mace, Peter D., C. Smits, David L. Vaux, John Silke, & Catherine L. Day. (2010). Asymmetric Recruitment of cIAPs by TRAF2. Journal of Molecular Biology. 400(1). 8–15. 67 indexed citations

13.

Smits, C., Oleg Kovalevskiy, M.B. Shevtsov, et al.. (2009). Structural basis for the nuclease activity of a bacteriophage large terminase. EMBO Reports. 10(6). 592–598. 51 indexed citations

14.

Smits, C., Peter E. Czabotar, Mark G. Hinds, & Catherine L. Day. (2008). Structural Plasticity Underpins Promiscuous Binding of the Prosurvival Protein A1. Structure. 16(5). 818–829. 90 indexed citations

15.

Day, Catherine L., C. Smits, Fengjuan Fan, et al.. (2008). Structure of the BH3 Domains from the p53-Inducible BH3-Only Proteins Noxa and Puma in Complex with Mcl-1. Journal of Molecular Biology. 380(5). 958–971. 163 indexed citations

16.

Silva, Ana P. G., et al.. (2008). Expression, purification, crystallization and preliminary X-ray studies of the TAN1 orthologue fromMethanothermobacter thermautotrophicus. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64(11). 1083–1086. 8 indexed citations

17.

Hinds, Mark G., C. Smits, Joanna M. Risk, et al.. (2006). Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death and Differentiation. 14(1). 128–136. 179 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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