Eong Cheah

2.9k total citations · 1 hit paper
13 papers, 2.4k citations indexed

About

Eong Cheah is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Eong Cheah has authored 13 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 7 papers in Materials Chemistry and 6 papers in Genetics. Recurrent topics in Eong Cheah's work include Enzyme Structure and Function (7 papers), Bacterial Genetics and Biotechnology (6 papers) and RNA and protein synthesis mechanisms (4 papers). Eong Cheah is often cited by papers focused on Enzyme Structure and Function (7 papers), Bacterial Genetics and Biotechnology (6 papers) and RNA and protein synthesis mechanisms (4 papers). Eong Cheah collaborates with scholars based in Australia, United States and Netherlands. Eong Cheah's co-authors include David L. Ollis, Joseph D. Schrag, Joel L. Sussman, Michal Harel, Israel Silman, Sybille Franken, Mirosław Cygler, Koen H. G. Verschueren, Bauke W. Dijkstra and Adrian Goldman and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Molecular Biology and FEBS Letters.

In The Last Decade

Eong Cheah

13 papers receiving 2.4k citations

Hit Papers

The α/β hydrolase fold 1992 2026 2003 2014 1992 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eong Cheah Australia 10 1.9k 447 372 304 297 13 2.4k
Maria Krook Sweden 15 1.6k 0.9× 495 1.1× 175 0.5× 232 0.8× 186 0.6× 18 2.4k
Derek J. Jamieson United Kingdom 27 2.3k 1.3× 134 0.3× 538 1.4× 197 0.6× 140 0.5× 40 3.3k
Georg Thierbach Germany 17 2.3k 1.3× 316 0.7× 897 2.4× 192 0.6× 231 0.8× 21 3.5k
George Diallinas Greece 37 2.5k 1.3× 247 0.6× 894 2.4× 231 0.8× 217 0.7× 116 3.5k
Kenzo Yokozeki Japan 27 1.7k 0.9× 325 0.7× 156 0.4× 501 1.6× 97 0.3× 114 2.4k
Pekka Mäntsälä Finland 37 2.2k 1.2× 465 1.0× 483 1.3× 167 0.5× 1.5k 4.9× 113 3.2k
Fredric S. Jacobson United States 11 1.6k 0.9× 161 0.4× 168 0.5× 197 0.6× 43 0.1× 13 2.4k
Margaret E. Daub United States 33 1.7k 0.9× 384 0.9× 2.2k 5.8× 88 0.3× 330 1.1× 82 3.6k
Hugo Gramajo Argentina 31 2.4k 1.3× 246 0.6× 358 1.0× 103 0.3× 1.5k 5.0× 92 3.3k
Luigi Mandrich Italy 22 1.0k 0.6× 213 0.5× 325 0.9× 137 0.5× 121 0.4× 66 1.6k

Countries citing papers authored by Eong Cheah

Since Specialization
Citations

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

Fields of papers citing papers by Eong Cheah

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Eong Cheah

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

All Works

13 of 13 papers shown
1.
Xu, Yibin, Eong Cheah, Paul D. Carr, et al.. (1998). GlnK, a PII-homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. Journal of Molecular Biology. 282(1). 149–165. 138 indexed citations
2.
Cheah, Eong, et al.. (1998). Crystallization and preliminary X-ray analysis of IND, an enzyme with indole oxygenase activity fromChromobacterium violaceum. Acta Crystallographica Section D Biological Crystallography. 54(4). 657–658. 2 indexed citations
3.
Xu, Yibin, Eong Cheah, Paul D. Carr, et al.. (1998). Crystallization and preliminary X-ray analysis of Escherichia coli GlnK. Acta Crystallographica Section D Biological Crystallography. 54(5). 996–998. 12 indexed citations
4.
Newcomb, Richard D., Peter M. Campbell, David L. Ollis, et al.. (1997). A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly. Proceedings of the National Academy of Sciences. 94(14). 7464–7468. 296 indexed citations
5.
Cheah, Eong, et al.. (1996). The role of the T‐loop of the signal transducing protein PII from Escherichia coli. FEBS Letters. 391(1-2). 223–228. 40 indexed citations
6.
Carr, Paul D., et al.. (1996). X-ray structure of the signal transduction protein from Escherichia coli at 1.9 Å. Acta Crystallographica Section D Biological Crystallography. 52(1). 93–104. 54 indexed citations
7.
Edwards, Karen J., et al.. (1996). Crystallization and Preliminary X-ray Diffraction Studies of New Crystal Forms ofEscherichia coliPIIComplexed with Various Ligands. Acta Crystallographica Section D Biological Crystallography. 52(4). 738–742. 2 indexed citations
8.
Edwards, Karen J., et al.. (1996). New crystal forms ofEscherichia coliPIIcomplexed with various ligands and structure solution of PII/ATP/2-ketoglutarate. Acta Crystallographica Section A Foundations of Crystallography. 52(a1). C232–C233. 2 indexed citations
9.
Vasudevan, Subhash G., Craig Gedye, Nicholas E. Dixon, et al.. (1994). Escherichia coli PII protein: purification, crystallization and oligomeric structure. FEBS Letters. 337(3). 255–258. 27 indexed citations
10.
Cheah, Eong, et al.. (1994). Structure of the Escherichia coli signal transducing protein PII. Structure. 2(10). 981–990. 72 indexed citations
11.
Cheah, Eong, et al.. (1993). Catalysis by dienelactone hydrolase: A variation on the protease mechanism. Proteins Structure Function and Bioinformatics. 16(1). 64–78. 32 indexed citations
12.
Cheah, Eong, et al.. (1993). Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad. Protein Engineering Design and Selection. 6(6). 575–583. 27 indexed citations
13.
Ollis, David L., Eong Cheah, Mirosław Cygler, et al.. (1992). The α/β hydrolase fold. Protein Engineering Design and Selection. 5(3). 197–211. 1741 indexed citations breakdown →

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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