Ming‐Cheh Liu

646 total citations
26 papers, 471 citations indexed

About

Ming‐Cheh Liu is a scholar working on Molecular Biology, Oncology and Physiology. According to data from OpenAlex, Ming‐Cheh Liu has authored 26 papers receiving a total of 471 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 4 papers in Oncology and 4 papers in Physiology. Recurrent topics in Ming‐Cheh Liu's work include Receptor Mechanisms and Signaling (8 papers), Ion Transport and Channel Regulation (5 papers) and Glycosylation and Glycoproteins Research (3 papers). Ming‐Cheh Liu is often cited by papers focused on Receptor Mechanisms and Signaling (8 papers), Ion Transport and Channel Regulation (5 papers) and Glycosylation and Glycoproteins Research (3 papers). Ming‐Cheh Liu collaborates with scholars based in United States, Japan and Taiwan. Ming‐Cheh Liu's co-authors include Yoichi Sakakibara, Masahito Suiko, Takuya Sugahara, Tong-Kun Pai, Shin Yasuda, Yoshimitsu Kakuta, Yasunari Takami, Makoto Kimura, Christian Zwieb and Takamasa Teramoto and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Biochemistry.

In The Last Decade

Ming‐Cheh Liu

26 papers receiving 459 citations

Peers

Ming‐Cheh Liu

PHARM

EDM

GENET

IMMUN

Seokjoo Yoon South Korea

Patricia W. Pan Canada

Deanna L. Howarth United States

Perry M. Kim Canada

Yuko Kamada Japan

Nil Turan United Kingdom

D.E. Hall United Kingdom

Francis Fouchier France

Giuseppina Pichiri Italy

Roger E. Ganschow United States

Seokjoo Yoon South Korea

Ming‐Cheh Liu

293 ×1.0

52 ×0.5

PHARM

23 ×0.5

EDM

26 ×0.6

GENET

43 ×0.9

IMMUN

Citations per year, relative to Ming‐Cheh Liu Ming‐Cheh Liu (= 1×) peers Seokjoo Yoon

Countries citing papers authored by Ming‐Cheh Liu

Since Specialization

Citations

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

Fields of papers citing papers by Ming‐Cheh Liu

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ming‐Cheh Liu. 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 Ming‐Cheh Liu. The network helps show where Ming‐Cheh Liu may publish in the future.

Co-authorship network of co-authors of Ming‐Cheh Liu

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

All Works

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20 of 20 papers shown

Kurogi, Katsuhisa, et al.. (2017). Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1. Scientific Reports. 7(1). 8776–8776. 20 indexed citations

Kurogi, Katsuhisa, et al.. (2017). Δ 4 -3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases. Biochimica et Biophysica Acta (BBA) - General Subjects. 1861(11). 2883–2890. 6 indexed citations

Teramoto, Takamasa, Katsuhisa Kurogi, Emi Mishiro‐Sato, et al.. (2013). Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction. Nature Communications. 4(1). 1572–1572. 54 indexed citations

Shetty, Shwetha K., Amarnath S. Marudamuthu, Daniel G. Abernathy, et al.. (2011). Regulation of Urokinase Expression at the Posttranscription Level by Lung Epithelial Cells. Biochemistry. 51(1). 205–213. 8 indexed citations

Sugahara, Takuya, Yoichi Sakakibara, Masahito Suiko, et al.. (2010). Zebrafish as a Model for the Study of the Phase II Cytosolic Sulfotransferases. Current Drug Metabolism. 11(6). 538–546. 30 indexed citations

Teramoto, Takamasa, Yoichi Sakakibara, Ming‐Cheh Liu, et al.. (2009). Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate. Biochemical and Biophysical Research Communications. 383(1). 83–87. 19 indexed citations

Teramoto, Takamasa, Yoichi Sakakibara, Ming‐Cheh Liu, et al.. (2009). On the similar spatial arrangement of active site residues in PAPS‐dependent and phenolic sulfate‐utilizing sulfotransferases. FEBS Letters. 583(18). 3091–3094. 5 indexed citations

Teramoto, Takamasa, Yoichi Sakakibara, Ming‐Cheh Liu, et al.. (2008). Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase—mSULT1D1. Biochemical and Biophysical Research Communications. 379(1). 76–80. 2 indexed citations

Liu, Ming‐Cheh, et al.. (2008). Blockade of LOX-1 Prevents Endotoxin-Induced Acute Lung Inflammation and Injury in Mice. Journal of Innate Immunity. 1(4). 358–365. 28 indexed citations

10.

Teramoto, Takamasa, Yoichi Sakakibara, Katsuhisa Kurogi, et al.. (2008). Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase. FEBS Letters. 582(28). 3909–3914. 8 indexed citations

11.

Yasuda, Shin, Ming‐Yih Liu, Masahito Suiko, Yoichi Sakakibara, & Ming‐Cheh Liu. (2007). Hydroxylated serotonin and dopamine as substrates and inhibitors for human cytosolic SULT1A3. Journal of Neurochemistry. 103(6). 2679–2689. 23 indexed citations

12.

Yang, Yuh‐Shyong, et al.. (2005). Identification of a novel zebrafish SULT1 cytosolic sulfotransferase: Cloning, expression, characterization, and developmental expression study. Archives of Biochemistry and Biophysics. 437(1). 10–19. 19 indexed citations

13.

Shetty, Sreerama, et al.. (2005). Regulation of urokinase receptor expression by phosphoglycerate kinase is independent of its catalytic activity. American Journal of Physiology-Lung Cellular and Molecular Physiology. 289(4). L591–L598. 14 indexed citations

14.

Sugahara, Takuya, et al.. (2003). Molecular cloning, expression, and functional characterization of a novel zebrafish cytosolic sulfotransferase. Biochemical and Biophysical Research Communications. 300(3). 725–730. 28 indexed citations

15.

Sugahara, Takuya, Chau‐Ching Liu, Tong-Kun Pai, et al.. (2003). Sulfation of hydroxychlorobiphenyls. European Journal of Biochemistry. 270(11). 2404–2411. 29 indexed citations

16.

Sakakibara, Yoichi, Masahito Suiko, Tong-Kun Pai, et al.. (2002). Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization. Gene. 285(1-2). 39–47. 47 indexed citations

17.

Gowda, Krishne, et al.. (1998). Protein SRP54 of human signal recognition particle: cloning, expression, and comparative analysis of functional sites. Gene. 207(2). 197–207. 16 indexed citations

18.

Liu, Ming‐Cheh, Yoichi Sakakibara, & Masahito Suiko. (1997). Role of a putative tyrosine-O-sulfate receptor in the targeting and/or intracellular transport of tyrosine-sulfated proteins. Cytotechnology. 23(1-3). 143–149. 2 indexed citations

19.

Sakakibara, Yoichi, et al.. (1997). Tissue-specific and developmental stage-dependent expression of a novel rat dopa/tyrosine sulfotransferase. The International Journal of Biochemistry & Cell Biology. 29(5). 801–806. 15 indexed citations

20.

Sakakibara, Yoichi, Yasunari Takami, Christian Zwieb, et al.. (1995). Purification, Characterization, and Molecular Cloning of A Novel Rat Liver Dopa/Tyrosine Sulfotransferase. Journal of Biological Chemistry. 270(51). 30470–30478. 49 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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