Bi‐Ching Sang

3.8k total citations
30 papers, 2.2k citations indexed

About

Bi‐Ching Sang is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Bi‐Ching Sang has authored 30 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 11 papers in Oncology and 8 papers in Organic Chemistry. Recurrent topics in Bi‐Ching Sang's work include Synthesis and biological activity (7 papers), Melanoma and MAPK Pathways (7 papers) and Protein Kinase Regulation and GTPase Signaling (5 papers). Bi‐Ching Sang is often cited by papers focused on Synthesis and biological activity (7 papers), Melanoma and MAPK Pathways (7 papers) and Protein Kinase Regulation and GTPase Signaling (5 papers). Bi‐Ching Sang collaborates with scholars based in United States, Japan and Switzerland. Bi‐Ching Sang's co-authors include Hua Zou, R.J. Skene, Clifford D. Mol, Michelle L. Kraus, Daniel Scheibe, Miguel Barbosa, G. Snell, Kathleen Aertgeerts, Douglas R. Dougan and T. Schneider and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Bi‐Ching Sang

30 papers receiving 2.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Bi‐Ching Sang United States 18 1.2k 711 337 246 232 30 2.2k
R.J. Skene United States 22 1.4k 1.1× 816 1.1× 485 1.4× 142 0.6× 203 0.9× 34 2.5k
Douglas R. Dougan United States 19 918 0.8× 293 0.4× 378 1.1× 118 0.5× 219 0.9× 32 1.6k
Anne T. Truesdale United States 13 1.1k 0.9× 972 1.4× 404 1.2× 202 0.8× 183 0.8× 16 2.3k
Emily A. Liu United States 5 2.9k 2.3× 2.3k 3.2× 448 1.3× 239 1.0× 171 0.7× 5 3.9k
Jeffrey H. Till United States 11 1.3k 1.1× 431 0.6× 166 0.5× 173 0.7× 250 1.1× 12 1.9k
David J. Bearss United States 34 4.9k 4.0× 1.5k 2.1× 306 0.9× 657 2.7× 457 2.0× 114 6.5k
Paul Nimmer United States 8 1.8k 1.5× 665 0.9× 222 0.7× 315 1.3× 344 1.5× 11 2.4k
Stephen K. Tahir United States 22 2.4k 1.9× 980 1.4× 331 1.0× 391 1.6× 337 1.5× 35 3.3k
Swee Y. Sharp United Kingdom 25 2.0k 1.7× 750 1.1× 417 1.2× 287 1.2× 100 0.4× 45 2.8k
Longchuan Bai United States 32 2.7k 2.2× 1.2k 1.7× 363 1.1× 421 1.7× 469 2.0× 68 3.5k

Countries citing papers authored by Bi‐Ching Sang

Since Specialization
Citations

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

Fields of papers citing papers by Bi‐Ching Sang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Bi‐Ching Sang. 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 Bi‐Ching Sang. The network helps show where Bi‐Ching Sang may publish in the future.

Co-authorship network of co-authors of Bi‐Ching Sang

This figure shows the co-authorship network connecting the top 25 collaborators of Bi‐Ching Sang. A scholar is included among the top collaborators of Bi‐Ching Sang 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 Bi‐Ching Sang. Bi‐Ching Sang 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.
Takahashi, Masashi, Rei Okamoto, Shinji Morimoto, et al.. (2019). Structure‐Based Design, Synthesis, and Biological Evaluation of Imidazo[4,5‐b]Pyridin‐2‐one‐Based p38 MAP Kinase Inhibitors: Part 2. ChemMedChem. 14(24). 2093–2101. 3 indexed citations
2.
Nakagawa, Hideyuki, Yusuke Kamada, Atsuko Ochida, et al.. (2018). Biochemical Properties of TAK-828F, a Potent and Selective Retinoid-Related Orphan Receptor Gamma t Inverse Agonist. Pharmacology. 102(5-6). 244–252. 8 indexed citations
3.
Takahashi, Masashi, Takafumi Takai, Takahiro Miyazaki, et al.. (2017). Structure-based design, synthesis, and biological evaluation of imidazo[1,2-b]pyridazine-based p38 MAP kinase inhibitors. Bioorganic & Medicinal Chemistry. 26(3). 647–660. 17 indexed citations
4.
Fukase, Yoshiyuki, Atsuko Ochida, Kazuko Yonemori, et al.. (2017). Identification of novel quinazolinedione derivatives as RORγt inverse agonist. Bioorganic & Medicinal Chemistry. 26(3). 721–736. 17 indexed citations
5.
Katoh, Taisuke, Takafumi Takai, Tetsuya Tsukamoto, et al.. (2016). Discovery and optimization of 1,7-disubstituted-2,2-dimethyl-2,3-dihydroquinazolin-4(1H)-ones as potent and selective PKCθ inhibitors. Bioorganic & Medicinal Chemistry. 24(11). 2466–2475. 19 indexed citations
6.
Shi, Lihong, Deepika Balakrishna, Takashi Hoshino, et al.. (2013). Biological Characterization of TAK-901, an Investigational, Novel, Multitargeted Aurora B Kinase Inhibitor. Molecular Cancer Therapeutics. 12(4). 460–470. 34 indexed citations
7.
Yamashita, Takashi, Satoshi Endo, Mitsuo Yamamoto, et al.. (2011). Design, synthesis, and structure–activity relationships of spirolactones bearing 2-ureidobenzothiophene as acetyl-CoA carboxylases inhibitors. Bioorganic & Medicinal Chemistry Letters. 21(21). 6314–6318. 16 indexed citations
8.
Aertgeerts, Kathleen, R.J. Skene, Jason K. Yano, et al.. (2011). Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. Journal of Biological Chemistry. 286(21). 18756–18765. 310 indexed citations
9.
Zou, Hua, Yiqin Wu, Marc Navre, & Bi‐Ching Sang. (2006). Characterization of the two catalytic domains in histone deacetylase 6. Biochemical and Biophysical Research Communications. 341(1). 45–50. 121 indexed citations
10.
Xu, Rongda, Bi‐Ching Sang, Marc Navre, & Daniel B. Kassel. (2006). Cell‐based assay for screening 11 β ‐hydroxysteroid dehydrogenase inhibitors using liquid chromatography/tandem mass spectrometry detection. Rapid Communications in Mass Spectrometry. 20(11). 1643–1647. 9 indexed citations
11.
Aertgeerts, Kathleen, Sheng Ye, Mike Tennant, et al.. (2004). Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Science. 13(2). 412–421. 162 indexed citations
12.
Mol, Clifford D., Douglas R. Dougan, T. Schneider, et al.. (2004). Structural Basis for the Autoinhibition and STI-571 Inhibition of c-Kit Tyrosine Kinase. Journal of Biological Chemistry. 279(30). 31655–31663. 463 indexed citations
13.
Mol, Clifford D., Kheng B. Lim, Vandana Sridhar, et al.. (2003). Structure of a c-Kit Product Complex Reveals the Basis for Kinase Transactivation. Journal of Biological Chemistry. 278(34). 31461–31464. 193 indexed citations
14.
Aertgeerts, Kathleen, Sheng Ye, Lihong Shi, et al.. (2003). N‐linked glycosylation of dipeptidyl peptidase IV (CD26): Effects on enzyme activity, homodimer formation, and adenosine deaminase binding. Protein Science. 13(1). 145–154. 55 indexed citations
15.
Nowakowski, Jacek, Ciarán N. Cronin, Duncan E. McRee, et al.. (2002). Structures of the Cancer-Related Aurora-A, FAK, and EphA2 Protein Kinases from Nanovolume Crystallography. Structure. 10(12). 1659–1667. 168 indexed citations
16.
Fourie, Anne M., Ted R. Hupp, David P. Lane, et al.. (1997). HSP70 Binding Sites in the Tumor Suppressor Protein p53. Journal of Biological Chemistry. 272(31). 19471–19479. 74 indexed citations
17.
Sang, Bi‐Ching & Miguel Barbosa. (1992). Increased E6/E7 transcription in HPV 18-immortalized human keratinocytes results from inactivation of E2 and additional cellular events. Virology. 189(2). 448–455. 22 indexed citations
18.
Sang, Bi‐Ching & Miguel Barbosa. (1992). Single amino acid substitutions in "low-risk" human papillomavirus (HPV) type 6 E7 protein enhance features characteristic of the "high-risk" HPV E7 oncoproteins.. Proceedings of the National Academy of Sciences. 89(17). 8063–8067. 73 indexed citations
19.
Sang, Bi‐Ching & Donald M. Gray. (1989). Specificity of the Binding of fd Gene 5 Protein to Polydeoxyribonucleotides. Journal of Biomolecular Structure and Dynamics. 7(3). 693–706. 18 indexed citations
20.
Sang, Bi‐Ching & Donald M. Gray. (1987). fd Gene 5 protein binds to double-stranded polydeoxyribonucleotides poly(dA.cntdot.dT) and poly[d(A-T).cntdot.d(A-T)]. Biochemistry. 26(23). 7210–7214. 7 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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