Gialih Lin

1.0k total citations
64 papers, 882 citations indexed

About

Gialih Lin is a scholar working on Molecular Biology, Computational Theory and Mathematics and Pharmacology. According to data from OpenAlex, Gialih Lin has authored 64 papers receiving a total of 882 indexed citations (citations by other indexed papers that have themselves been cited), including 39 papers in Molecular Biology, 33 papers in Computational Theory and Mathematics and 28 papers in Pharmacology. Recurrent topics in Gialih Lin's work include Computational Drug Discovery Methods (33 papers), Cholinesterase and Neurodegenerative Diseases (27 papers) and Enzyme Catalysis and Immobilization (23 papers). Gialih Lin is often cited by papers focused on Computational Drug Discovery Methods (33 papers), Cholinesterase and Neurodegenerative Diseases (27 papers) and Enzyme Catalysis and Immobilization (23 papers). Gialih Lin collaborates with scholars based in Taiwan and United States. Gialih Lin's co-authors include Cheng‐Yue Lai, Wen‐Yuan Lin, Wei‐Cheng Liao, Ming‐Daw Tsai, Chun‐Ping Lu, C. Frank Bennett, Yanfu Lin, Yi-Chin Candace Tsai, Long‐Yau Lin and Chuanfu Huang and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Biochemistry.

In The Last Decade

Gialih Lin

63 papers receiving 865 citations

Peers

Gialih Lin
Mario Brufani Italy
Huizhe Lu China
Generosa Gómez Spain
Carmen Lúcia Cardoso Brazil
Prasanna Sivaprakasam United States
Carmen Terán Spain
Luisa Chiasserini Italy
Giorgio Grosa Italy
E. Manivannan India
Ondřej Holas Czechia
Mario Brufani Italy
Gialih Lin
Citations per year, relative to Gialih Lin Gialih Lin (= 1×) peers Mario Brufani

Countries citing papers authored by Gialih Lin

Since Specialization
Citations

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

Fields of papers citing papers by Gialih Lin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gialih Lin

This figure shows the co-authorship network connecting the top 25 collaborators of Gialih Lin. A scholar is included among the top collaborators of Gialih Lin 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 Gialih Lin. Gialih Lin 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.
Lin, Gialih, et al.. (2014). Molecular docking of different inhibitors and activators to butyrylcholinesterase. Journal of Biomolecular Structure and Dynamics. 33(3). 563–572. 15 indexed citations
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Lin, Ming‐Cheng, et al.. (2011). Stereoselective Inhibition of Cholesterol Esterase by Enantiomers of exo- and endo-2-Norbornyl-N–n-butylcarbamates. The Protein Journal. 30(3). 220–227. 6 indexed citations
4.
Lin, Gialih, et al.. (2009). Stereoselective inhibition of butyrylcholinesterase by enantiomers of exo - and endo -2-norbornyl- N - n -butylcarbamates. Journal of Enzyme Inhibition and Medicinal Chemistry. 25(1). 13–20. 4 indexed citations
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Huang, Chuanfu, et al.. (2009). Comparison of active sites of butyrylcholinesterase and acetylcholinesterase based on inhibition by geometric isomers of benzene‐di‐N‐substituted carbamates. Journal of Biochemical and Molecular Toxicology. 23(5). 303–308. 26 indexed citations
7.
Lin, Gialih, et al.. (2008). Activation Mechanisms of Butyrylcholinesterase by 2,4,6-Trinitrotoluene, 3,3-Dimethylbutyl-N-n-butylcarbamate, and 2-Trimethylsilyl-ethyl-N-n-butylcarbamate. Applied Biochemistry and Biotechnology. 150(3). 337–344. 1 indexed citations
8.
Lin, Gialih, et al.. (2005). A rate determining step change in the pre-steady state of acetylcholinesterase inhibitions by 1,n-alkane-di-N-butylcarbamates. Bioorganic & Medicinal Chemistry Letters. 15(4). 951–955. 12 indexed citations
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Lin, Gialih, et al.. (2005). Quantitative structure-activity relationships for the pre-steady state acetylcholinesterase inhibition by carbamates. Journal of Biochemical and Molecular Toxicology. 18(6). 353–360. 14 indexed citations
13.
Lin, Gialih, et al.. (2004). Ortho Effects in Quantitative Structure-activity Relationships for Acetylcholinesterase Inhibition by Aryl Carbamates. Journal of Enzyme Inhibition and Medicinal Chemistry. 19(5). 395–401. 19 indexed citations
14.
Lin, Gialih, et al.. (2003). Cage amines as the stopper inhibitors of cholinesterases. Bioorganic & Medicinal Chemistry Letters. 13(17). 2887–2890. 22 indexed citations
15.
Lin, Gialih, et al.. (2003). Benzene-di-N-octylcarbamates as conformationally constrained phospholipase A2 inhibitors. Bioorganic & Medicinal Chemistry Letters. 14(3). 751–755. 5 indexed citations
16.
Lin, Gialih, et al.. (2000). Quantitative structure–activity relationships for the pre-steady-state inhibition of cholesterol esterase by 4-nitrophenyl-n-substituted carbamates. Bioorganic & Medicinal Chemistry. 8(11). 2601–2607. 20 indexed citations
17.
Lin, Gialih, et al.. (1999). Structure-reactivity probes for active site shapes of cholesterol esterase by carbamate inhibitors. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1431(2). 500–511. 27 indexed citations
18.
Lin, Gialih, Cheng‐Yue Lai, & Wei‐Cheng Liao. (1999). Molecular recognition by acetylcholinesterase at the peripheral anionic site: structure–activity relationships for inhibitions by aryl carbamates. Bioorganic & Medicinal Chemistry. 7(12). 2683–2689. 35 indexed citations
19.
Lin, Gialih, et al.. (1998). Conformationally restricted carbamate inhibitors of horse serum butyrylcholinesterase. Bioorganic & Medicinal Chemistry Letters. 8(19). 2747–2750. 16 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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