Huei‐Fen Lo

578 total citations
44 papers, 510 citations indexed

About

Huei‐Fen Lo is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Huei‐Fen Lo has authored 44 papers receiving a total of 510 indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 21 papers in Materials Chemistry and 20 papers in Biotechnology. Recurrent topics in Huei‐Fen Lo's work include Enzyme Structure and Function (21 papers), Enzyme Production and Characterization (19 papers) and Amino Acid Enzymes and Metabolism (13 papers). Huei‐Fen Lo is often cited by papers focused on Enzyme Structure and Function (21 papers), Enzyme Production and Characterization (19 papers) and Amino Acid Enzymes and Metabolism (13 papers). Huei‐Fen Lo collaborates with scholars based in Taiwan and United States. Huei‐Fen Lo's co-authors include Long‐Liu Lin, Wen-Hwei Hsu, Meng‐Chun Chi, Chen-Tien Chang, Min-Guan Lin, Yiyu Chen, Huiyu Hu, Chen‐Tien Chang, Wen‐Ching Wang and Yipu Chen and has published in prestigious journals such as International Journal of Molecular Sciences, International Journal of Biological Macromolecules and Process Biochemistry.

In The Last Decade

Huei‐Fen Lo

44 papers receiving 491 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Huei‐Fen Lo Taiwan 14 343 267 135 119 99 44 510
Meng‐Chun Chi Taiwan 15 424 1.2× 153 0.6× 92 0.7× 121 1.0× 168 1.7× 55 599
Alexander W.M. Strasser Germany 13 600 1.7× 159 0.6× 232 1.7× 97 0.8× 50 0.5× 14 796
M Kossmann Germany 8 278 0.8× 105 0.4× 59 0.4× 153 1.3× 56 0.6× 8 479
Gen-Jun Xu China 14 314 0.9× 152 0.6× 58 0.4× 81 0.7× 37 0.4× 36 511
Søren F. Lassen Denmark 10 560 1.6× 143 0.5× 262 1.9× 118 1.0× 18 0.2× 11 756
Haruhiko Kanai Japan 9 306 0.9× 214 0.8× 116 0.9× 46 0.4× 17 0.2× 9 423
Cynthia A. Haseltine United States 12 343 1.0× 143 0.5× 62 0.5× 76 0.6× 16 0.2× 17 447
B Esmon United States 10 1.0k 2.9× 99 0.4× 194 1.4× 58 0.5× 36 0.4× 10 1.2k
Jin Kuk Yang South Korea 13 459 1.3× 126 0.5× 109 0.8× 66 0.6× 10 0.1× 22 624
Sebastiana Angelaccio Italy 17 534 1.6× 73 0.3× 61 0.5× 373 3.1× 304 3.1× 38 734

Countries citing papers authored by Huei‐Fen Lo

Since Specialization
Citations

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

Fields of papers citing papers by Huei‐Fen Lo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Huei‐Fen Lo. 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 Huei‐Fen Lo. The network helps show where Huei‐Fen Lo may publish in the future.

Co-authorship network of co-authors of Huei‐Fen Lo

This figure shows the co-authorship network connecting the top 25 collaborators of Huei‐Fen Lo. A scholar is included among the top collaborators of Huei‐Fen Lo 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 Huei‐Fen Lo. Huei‐Fen Lo 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.
Chi, Meng‐Chun, et al.. (2018). High-level expression and molecular characterization of a recombinant prolidase from Escherichia coli NovaBlue. PeerJ. 6. e5863–e5863. 5 indexed citations
2.
Lo, Huei‐Fen, et al.. (2018). Protective Effect of Biological Osmolytes against Heat- and Chaotropic Agent-Induced Denaturation of Bacillus licheniformis ��-Glutamyl Transpeptidase. Journal of Microbiology and Biotechnology. 28(9). 1457–1466. 2 indexed citations
3.
4.
Chi, Meng‐Chun, Yiyu Chen, Huei‐Fen Lo, & Long‐Liu Lin. (2012). Experimental evidence for the involvement of amino acid residue Glu398 in the autocatalytic processing of Bacillus licheniformis γ‐glutamyltranspeptidase. FEBS Open Bio. 2(1). 298–304. 10 indexed citations
5.
Lo, Huei‐Fen, et al.. (2012). Characterization of Glycine Substitution Mutations within the Putative NAD+-binding Site of Bacillus licheniformis Aldehyde Dehydrogenase. Protein and Peptide Letters. 19(11). 1183–1193. 2 indexed citations
6.
Chen, Yiyu, et al.. (2011). Biophysical characterization of Bacillus licheniformis and Escherichia coli γ-glutamyltranspeptidases: A comparative analysis. International Journal of Biological Macromolecules. 48(3). 414–422. 22 indexed citations
7.
Chi, Meng‐Chun, et al.. (2010). Biophysical Characterization of a Recombinant α-Amylase from Thermophilic Bacillus sp. strain TS-23. The Protein Journal. 29(8). 572–582. 4 indexed citations
8.
Lo, Huei‐Fen, et al.. (2010). Gene Cloning and Biochemical Characterization of a NAD(P)+-Dependent Aldehyde Dehydrogenase from Bacillus licheniformis. Molecular Biotechnology. 46(2). 157–167. 14 indexed citations
9.
Lin, Min-Guan, et al.. (2009). Deletion analysis of the C-terminal region of a molecular chaperone DnaK from Bacillus licheniformis. Archives of Microbiology. 191(7). 583–593. 8 indexed citations
10.
Lo, Huei‐Fen, et al.. (2008). Influence of signal‐peptide truncations on the functional expression of Escherichia coli γ ‐glutamyltranspeptidase. Journal of Basic Microbiology. 48(4). 260–268. 5 indexed citations
11.
Lo, Huei‐Fen, et al.. (2008). Immobilization of Escherichia coli novablue γ-glutamyltranspeptidase in Ca-alginate-k-carrageenan beads. Applied Biochemistry and Biotechnology. 150(2). 157–170. 35 indexed citations
12.
13.
Chi, Meng‐Chun, et al.. (2005). Adsorption-elution purification of chimeric Bacillus stearothermophilus leucine aminopeptidase II with raw-starch-binding activity. World Journal of Microbiology and Biotechnology. 21(5). 689–694. 3 indexed citations
14.
Lo, Huei‐Fen, et al.. (2004). (Journal of Industrial Microbiology & Biotechnology,31(6):273-277)Fusion of Bacillus stearothermophilus leucine aminopeptidase II with the raw starch-binding domain of Bacillus sp. strain TS-23 α-amylase generates a chimeric enzyme with enhanced thermostability and catalytic activity. 1 indexed citations
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Chang, Chen-Tien, et al.. (2003). Identification of essential histidine residues in a recombinant ?-amylase of thermophilic and alkaliphilic Bacillus sp. strain TS-23. Extremophiles. 7(6). 505–509. 13 indexed citations
18.
19.
Lo, Huei‐Fen, et al.. (2002). Deletion analysis of the C-terminal region of the α-amylase of Bacillus sp. strain TS-23. Archives of Microbiology. 178(2). 115–123. 45 indexed citations
20.

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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