J. F. Shaw

2.7k total citations · 1 hit paper
57 papers, 2.1k citations indexed

About

J. F. Shaw is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, J. F. Shaw has authored 57 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 10 papers in Materials Chemistry and 9 papers in Organic Chemistry. Recurrent topics in J. F. Shaw's work include Enzyme Catalysis and Immobilization (31 papers), Enzyme Structure and Function (10 papers) and Microbial Metabolic Engineering and Bioproduction (9 papers). J. F. Shaw is often cited by papers focused on Enzyme Catalysis and Immobilization (31 papers), Enzyme Structure and Function (10 papers) and Microbial Metabolic Engineering and Bioproduction (9 papers). J. F. Shaw collaborates with scholars based in Taiwan, United States and China. J. F. Shaw's co-authors include Guan-Chiun Lee, Casimir C. Akoh, Shu‐Wei Chang, Yen‐Chywan Liaw, Tai-huang Huang, Yu-Chih Lo, Su‐Chang Lin, Chwen‐Jen Shieh, Li‐Min Huang and Ming‐Tsair Chan and has published in prestigious journals such as Journal of Molecular Biology, Applied and Environmental Microbiology and Biochemistry.

In The Last Decade

J. F. Shaw

56 papers receiving 2.1k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

GDSL family of serine esterases/lipases

2004 503 citations Casimir C. Akoh, Yen‐Chywan Liaw et al. Progress in Lipid Research profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
J. F. Shaw Taiwan	23	1.6k	549	396	293	173	57	2.1k
Jei‐Fu Shaw Taiwan	33	2.1k 1.3×	412 0.8×	945 2.4×	321 1.1×	181 1.0×	126	3.1k
Joon Shick Rhee South Korea	29	1.8k 1.1×	404 0.7×	181 0.5×	222 0.8×	58 0.3×	69	2.3k
Dongming Lan China	23	1.3k 0.8×	246 0.4×	203 0.5×	158 0.5×	117 0.7×	115	2.1k
María L. Rúa Spain	29	1.8k 1.1×	376 0.7×	188 0.5×	256 0.9×	107 0.6×	76	2.3k
Zhanglin Lin China	27	1.9k 1.2×	395 0.7×	180 0.5×	260 0.9×	228 1.3×	77	2.5k
Yoshio Tsujisaka Japan	34	1.8k 1.1×	737 1.3×	504 1.3×	1.3k 4.3×	182 1.1×	138	3.1k
Xiao‐Wei Yu China	27	1.3k 0.8×	402 0.7×	155 0.4×	394 1.3×	77 0.4×	97	1.9k
Johannes Bongaerts Germany	23	1.8k 1.1×	345 0.6×	165 0.4×	222 0.8×	268 1.5×	55	2.5k
Zijun Xiao China	20	1.1k 0.7×	650 1.2×	153 0.4×	225 0.8×	143 0.8×	55	1.7k
Julio Polaina Spain	33	1.9k 1.2×	1.1k 2.0×	592 1.5×	1.3k 4.5×	235 1.4×	101	3.0k

Countries citing papers authored by J. F. Shaw

Since Specialization

Citations

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

Fields of papers citing papers by J. F. Shaw

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J. F. Shaw. 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 J. F. Shaw. The network helps show where J. F. Shaw may publish in the future.

Co-authorship network of co-authors of J. F. Shaw

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Liu, Cheng-Huan, et al.. (2018). Crystallographic analysis of the Staphylococcus epidermidis lipase involved in esterification in aqueous solution. Acta Crystallographica Section F Structural Biology Communications. 74(6). 351–354. 1 indexed citations

Huang, Li‐Min, et al.. (2017). Genome-wide analysis of GDSL-type esterases/lipases in Arabidopsis. Plant Molecular Biology. 95(1-2). 181–197. 106 indexed citations

Shaw, J. F., et al.. (2015). Conversion of crude Jatropha curcas seed oil into biodiesel using liquid recombinant Candida rugosa lipase isozymes. Bioresource Technology. 192. 54–59. 46 indexed citations

Chen, Hong‐Hwa, et al.. (2009). Functional role of a non-active site residue Trp23 on the enzyme activity of Escherichia coli thioesterase I/protease I/lysophospholipase L1. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794(10). 1467–1473. 12 indexed citations

Chen, Cammy K.-M., Guan-Chiun Lee, Tzu‐Ping Ko, et al.. (2009). Structure of the Alkalohyperthermophilic Archaeoglobus fulgidus Lipase Contains a Unique C-Terminal Domain Essential for Long-Chain Substrate Binding. Journal of Molecular Biology. 390(4). 672–685. 31 indexed citations

Lee, Guan-Chiun, et al.. (2008). Promoter Analysis and Differential Expression of the Candida rugosa Lipase Gene Family in Response to Culture Conditions. Journal of Agricultural and Food Chemistry. 56(6). 1992–1998. 16 indexed citations

Chang, Shu‐Wei, et al.. (2007). Studies of optimum conditions for covalent immobilization of Candida rugosa lipase on poly(γ-glutamic acid) by RSM. Bioresource Technology. 99(8). 2800–2805. 76 indexed citations

Chang, Shu‐Wei, Chwen‐Jen Shieh, Guan-Chiun Lee, Casimir C. Akoh, & J. F. Shaw. (2006). Optimized Growth Kinetics of <i>Pichia pastoris</i> and Recombinant <i>Candida rugosa </i>LIP1 Production by RSM. Microbial Physiology. 11(1-2). 28–40. 11 indexed citations

Shaw, J. F., et al.. (2006). (J. Agric. Food Chem., 54:815-822)Codon optimization of Candida rugosa LIP1 of improving expression in Pichia pastoris and biochemical characterization of the purified recombinant LIP1 lipase. 1 indexed citations

10.

Akoh, Casimir C., et al.. (2004). GDSL family of serine esterases/lipases. Progress in Lipid Research. 43(6). 534–552. 503 indexed citations breakdown →

11.

Lo, Yu-Chih, Su‐Chang Lin, J. F. Shaw, & Yen‐Chywan Liaw. (2003). Crystal Structure of Escherichia coli Thioesterase I/Protease I/Lysophospholipase L1: Consensus Sequence Blocks Constitute the Catalytic Center of SGNH-hydrolases through a Conserved Hydrogen Bond Network. Journal of Molecular Biology. 330(3). 539–551. 102 indexed citations

12.

Tyukhtenko, Sergiy, Chi‐Fon Chang, Yu-Chih Lo, et al.. (2003). Sequential Structural Changes of Escherichia coli Thioesterase/Protease I in the Serial Formation of Michaelis and Tetrahedral Complexes with Diethyl p-Nitrophenyl Phosphate. Biochemistry. 42(27). 8289–8297. 12 indexed citations

13.

Tyukhtenko, Sergiy, et al.. (2002). NMR studies of the hydrogen bonds involving the catalytic triad of Escherichia coli thioesterase/protease I. FEBS Letters. 528(1-3). 203–206. 14 indexed citations

14.

Tang, Shye-Jye, et al.. (2001). Recombinant Expression and Characterization of the Candida rugosa lip4 Lipase in Pichia pastoris: Comparison of Glycosylation, Activity, and Stability. Archives of Biochemistry and Biophysics. 387(1). 93–98. 58 indexed citations

15.

Sagare, Abhay P., et al.. (2001). Formation of Protoberberine-Type Alkaloids by the Tubers of Somatic Embryo-Derived Plants of Corydalis yanhusuo. Planta Medica. 67(9). 839–842. 14 indexed citations

16.

Shaw, J. F., et al.. (1998). Molecular Cloning of a cDNA Coding for Copper/Zinc Superoxide Dismutase from Zebrafish and Its Expression inEscherichia coli. Journal of Agricultural and Food Chemistry. 46(7). 2863–2867. 12 indexed citations

17.

Shaw, J. F., et al.. (1997). (Biochem. Biophys Res. Commun., 231: 452-456)The thioesterase of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates. 10 indexed citations

18.

Shaw, J. F., et al.. (1997). (J. Am. Oil Chem. Soc., 74: 1477-1482)Synthesis of cocoa butter equivalent by lipase-catalyzed interesterification in supercritical carbon dioxide. 1 indexed citations

19.

Shaw, J. F., et al.. (1996). Characterization of the Ferrous Ion Binding Sites of Apple 1-Aminocyclopropane-1-carboxylate Oxidase by Site-Directed Mutagenesis. Biochemical and Biophysical Research Communications. 225(3). 697–700. 32 indexed citations

20.

Wang, Yajun, et al.. (1988). (Biotechnol. Bioeng., 31: 628-633)The lipase-catalyzed oil hydrolysis in the absence of added emulsifier. 14 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.

Explore authors with similar magnitude of impact