Wei-Ya Ma

2.0k total citations
28 papers, 1.7k citations indexed

About

Wei-Ya Ma is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, Wei-Ya Ma has authored 28 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 10 papers in Oncology and 5 papers in Cell Biology. Recurrent topics in Wei-Ya Ma's work include Cancer-related Molecular Pathways (4 papers), Cytokine Signaling Pathways and Interactions (4 papers) and Melanoma and MAPK Pathways (3 papers). Wei-Ya Ma is often cited by papers focused on Cancer-related Molecular Pathways (4 papers), Cytokine Signaling Pathways and Interactions (4 papers) and Melanoma and MAPK Pathways (3 papers). Wei-Ya Ma collaborates with scholars based in United States, China and Japan. Wei-Ya Ma's co-authors include Zigang Dong, Chuanshu Huang, Ann M. Bode, Rhoderick E. Brown, Yi Sun, Yong‐Yeon Cho, Duo Zheng, Feng Zhu, G. Tim Bowden and Min Ding and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Molecular and Cellular Biology.

In The Last Decade

Wei-Ya Ma

28 papers receiving 1.7k citations

Peers

Wei-Ya Ma
Nanyue Chen United States
Ke Yao United States
Jian Du China
Song Xu China
Eui‐Ju Yeo South Korea
Cindy R. Moomaw United States
Ok‐Sun Bang South Korea
Nanyue Chen United States
Wei-Ya Ma
Citations per year, relative to Wei-Ya Ma Wei-Ya Ma (= 1×) peers Nanyue Chen

Countries citing papers authored by Wei-Ya Ma

Since Specialization
Citations

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

Fields of papers citing papers by Wei-Ya Ma

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Wei-Ya Ma. 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 Wei-Ya Ma. The network helps show where Wei-Ya Ma may publish in the future.

Co-authorship network of co-authors of Wei-Ya Ma

This figure shows the co-authorship network connecting the top 25 collaborators of Wei-Ya Ma. A scholar is included among the top collaborators of Wei-Ya Ma 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 Wei-Ya Ma. Wei-Ya Ma 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.
Wang, Qiushi, Tianshun Zhang, Do Young Lim, et al.. (2020). ARC Is a Critical Protector against Inflammatory Bowel Disease (IBD) and IBD-Associated Colorectal Tumorigenesis. Cancer Research. 80(19). 4158–4171. 5 indexed citations
2.
Zhang, Tianshun, Keke Wang, Mee‐Hyun Lee, et al.. (2020). Targeting Opsin4/Melanopsin with a Novel Small Molecule Suppresses PKC/RAF/MEK/ERK Signaling and Inhibits Lung Adenocarcinoma Progression. Molecular Cancer Research. 18(7). 1028–1038. 8 indexed citations
3.
Zhang, Tianshun, Qiushi Wang, Moeez Rathore, et al.. (2020). HI-511 overcomes melanoma drug resistance via targeting AURKB and BRAF V600E. Theranostics. 10(21). 9721–9740. 20 indexed citations
4.
Yao, Ke, Sungyoung Lee, Cong Peng, et al.. (2018). RSK2 is required for TRAF6 phosphorylation-mediated colon inflammation. Oncogene. 37(26). 3501–3513. 15 indexed citations
5.
Sheng, Yuqiao, Kangdong Liu, Qiong Wu, et al.. (2016). PPMP, a novel tubulin-depolymerizing agent against esophageal cancer in patient-derived tumor xenografts. Oncotarget. 7(21). 30977–30989. 3 indexed citations
6.
He, Zhiwei, Ping Cui, Caiguo Ye, et al.. (2012). Analysis of the role of p38 MAP kinase in epidermal growth factor-induced JB6 Cl41 cell transformation by cDNA array. Gene. 497(1). 71–78. 2 indexed citations
7.
Zhu, Feng, Tatyana A. Zykova, Cong Peng, et al.. (2011). Phosphorylation of H2AX at Ser139 and a New Phosphorylation Site Ser16 by RSK2 Decreases H2AX Ubiquitination and Inhibits Cell Transformation. Cancer Research. 71(2). 393–403. 33 indexed citations
8.
Peng, Cong, Yong‐Yeon Cho, Feng Zhu, et al.. (2010). Phosphorylation of Caspase-8 (Thr-263) by Ribosomal S6 Kinase 2 (RSK2) Mediates Caspase-8 Ubiquitination and Stability. Journal of Biological Chemistry. 286(9). 6946–6954. 42 indexed citations
9.
Wen, Weihong, Feng Zhu, Jishuai Zhang, et al.. (2010). MST1 Promotes Apoptosis through Phosphorylation of Histone H2AX. Journal of Biological Chemistry. 285(50). 39108–39116. 60 indexed citations
10.
Bode, Ann M., Yong‐Yeon Cho, Duo Zheng, et al.. (2009). Transient Receptor Potential Type Vanilloid 1 Suppresses Skin Carcinogenesis. Cancer Research. 69(3). 905–913. 74 indexed citations
11.
Zheng, Duo, Yong‐Yeon Cho, Andy T. Y. Lau, et al.. (2008). Cyclin-Dependent Kinase 3–Mediated Activating Transcription Factor 1 Phosphorylation Enhances Cell Transformation. Cancer Research. 68(18). 7650–7660. 51 indexed citations
12.
Liu, Jinping, Wei-Ya Ma, Zigang Dong, et al.. (2004). Human αA- and αB-crystallins prevent UVA-induced apoptosis through regulation of PKCα, RAF/MEK/ERK and AKT signaling pathways. Experimental Eye Research. 79(3). 393–403. 112 indexed citations
13.
Cho, Yong‐Yeon, et al.. (2003). p38 Mitogen-activated Protein Kinase Regulation of JB6 Cl41 Cell Transformation Promoted by Epidermal Growth Factor. Journal of Biological Chemistry. 278(29). 26435–26442. 21 indexed citations
14.
Liu, Guang‐Ming, Wei-Ya Ma, Ann M. Bode, Yiguo Zhang, & Zigang Dong. (2003). NS-398 and Piroxicam Suppress UVB-induced Activator Protein 1 Activity by Mechanisms Independent of Cyclooxygenase-2. Journal of Biological Chemistry. 278(4). 2124–2130. 20 indexed citations
15.
Zhang, Yiguo, Shuping Zhong, Ziming Dong, et al.. (2001). UVA Induces Ser381 Phosphorylation of p90RSK/MAPKAP-K1 via ERK and JNK Pathways. Journal of Biological Chemistry. 276(18). 14572–14580. 74 indexed citations
16.
Chen, Nanyue, Wei-Ya Ma, Qing‐Bai She, et al.. (2001). Transactivation of the Epidermal Growth Factor Receptor Is Involved in 12-O-Tetradecanoylphorbol-13-acetate-induced Signal Transduction. Journal of Biological Chemistry. 276(50). 46722–46728. 58 indexed citations
17.
Huang, Chuanshu, et al.. (1999). p38 Kinase Mediates UV-induced Phosphorylation of p53 Protein at Serine 389. Journal of Biological Chemistry. 274(18). 12229–12235. 249 indexed citations
18.
Dong, Zigang, Chuanshu Huang, Rhoderick E. Brown, & Wei-Ya Ma. (1997). Inhibition of Activator Protein 1 Activity and Neoplastic Transformation by Aspirin. Journal of Biological Chemistry. 272(15). 9962–9970. 152 indexed citations
19.
Huang, Chuanshu, Wei-Ya Ma, Min Ding, G. Tim Bowden, & Zigang Dong. (1997). Direct Evidence for an Important Role of Sphingomyelinase in Ultraviolet-induced Activation of c-Jun N-Terminal Kinase. Journal of Biological Chemistry. 272(44). 27753–27757. 105 indexed citations
20.
Dong, Zigang, et al.. (1996). AP-1/Jun Is Required for Early Xenopus Development and Mediates Mesoderm Induction by Fibroblast Growth Factor but Not by Activin. Journal of Biological Chemistry. 271(17). 9942–9946. 43 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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