David E. Ong

4.9k total citations
95 papers, 3.8k citations indexed

About

David E. Ong is a scholar working on Molecular Biology, Biochemistry and Cell Biology. According to data from OpenAlex, David E. Ong has authored 95 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 81 papers in Molecular Biology, 31 papers in Biochemistry and 20 papers in Cell Biology. Recurrent topics in David E. Ong's work include Retinoids in leukemia and cellular processes (69 papers), Antioxidant Activity and Oxidative Stress (31 papers) and Estrogen and related hormone effects (17 papers). David E. Ong is often cited by papers focused on Retinoids in leukemia and cellular processes (69 papers), Antioxidant Activity and Oxidative Stress (31 papers) and Estrogen and related hormone effects (17 papers). David E. Ong collaborates with scholars based in United States, Singapore and France. David E. Ong's co-authors include Frank Chytil, Marcia E. Newcomer, Wen Zheng, Fiona Herr, Marie‐Claire Orgebin‐Crist, James Davis, Robert N. Brady, Paul N. MacDonald, Bharati Kakkad and Kevin G. Osteen and has published in prestigious journals such as Nature, Science and Journal of Biological Chemistry.

In The Last Decade

David E. Ong

95 papers receiving 3.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David E. Ong United States 39 2.8k 1.0k 751 498 372 95 3.8k
Dianne Robert Soprano United States 36 3.2k 1.1× 498 0.5× 827 1.1× 416 0.8× 68 0.2× 107 4.0k
William W. Lamph United States 38 4.3k 1.5× 569 0.6× 1.7k 2.3× 282 0.6× 60 0.2× 70 6.1k
Elizabeth A. Allegretto United States 25 1.9k 0.7× 122 0.1× 1.3k 1.8× 213 0.4× 158 0.4× 35 3.3k
Xiao-kun Zhang United States 29 3.4k 1.2× 494 0.5× 2.1k 2.8× 165 0.3× 54 0.1× 77 4.2k
Carmel Hensey Ireland 16 1.1k 0.4× 281 0.3× 180 0.2× 221 0.4× 114 0.3× 29 1.7k
John M. Kokontis United States 34 2.6k 0.9× 167 0.2× 1.3k 1.7× 207 0.4× 216 0.6× 52 4.7k
Kiyoshi Nose Japan 38 3.0k 1.1× 118 0.1× 400 0.5× 627 1.3× 45 0.1× 121 4.5k
F. Bayard France 31 1.2k 0.4× 97 0.1× 1.2k 1.7× 158 0.3× 264 0.7× 89 3.0k
Urs Eppenberger Switzerland 35 2.5k 0.9× 78 0.1× 875 1.2× 278 0.6× 128 0.3× 120 4.1k
Hong-Wu Chen United States 27 4.2k 1.5× 127 0.1× 949 1.3× 224 0.4× 49 0.1× 54 5.4k

Countries citing papers authored by David E. Ong

Since Specialization
Citations

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

Fields of papers citing papers by David E. Ong

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David E. Ong. 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 David E. Ong. The network helps show where David E. Ong may publish in the future.

Co-authorship network of co-authors of David E. Ong

This figure shows the co-authorship network connecting the top 25 collaborators of David E. Ong. A scholar is included among the top collaborators of David E. Ong 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 David E. Ong. David E. Ong 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.
Everts, Helen B., Kathleen A. Silva, Susan R. Opalenik, et al.. (2021). Estrogen regulates the expression of retinoic acid synthesis enzymes and binding proteins in mouse skin. Nutrition Research. 94. 10–24. 7 indexed citations
2.
Chiu, Han‐Mo, Hyun‐Soo Kim, Jeong‐Sik Byeon, et al.. (2018). Adenoma detection rates in colonoscopies for positive fecal immunochemical tests versus direct screening colonoscopies. Gastrointestinal Endoscopy. 89(3). 607–613.e1. 36 indexed citations
3.
Everts, Helen B., et al.. (2012). Retinoid Metabolism Is Altered in Human and Mouse Cicatricial Alopecia. Journal of Investigative Dermatology. 133(2). 325–333. 22 indexed citations
5.
Thompson, Maxwell, Jacques Lapointe, Yoon‐La Choi, et al.. (2008). Identification of candidate prostate cancer genes through comparative expression‐profiling of seminal vesicle. The Prostate. 68(11). 1248–1256. 21 indexed citations
6.
Everts, Helen B., John P. Sundberg, Lloyd E. King, & David E. Ong. (2007). Immunolocalization of Enzymes, Binding Proteins, and Receptors Sufficient for Retinoic Acid Synthesis and Signaling During the Hair Cycle. Journal of Investigative Dermatology. 127(7). 1593–1604. 42 indexed citations
7.
Alexeev, Dmitry, Maureen E. Estevez, Peter D. Calvert, et al.. (2006). Cyclic Nucleotide-gated Ion Channels in Rod Photoreceptors Are Protected from Retinoid Inhibition. The Journal of General Physiology. 128(4). 473–485. 5 indexed citations
8.
Kim, Hanna, Jacques Lapointe, Gülşah Kaygusuz, et al.. (2005). The Retinoic Acid Synthesis Gene ALDH1a2 Is a Candidate Tumor Suppressor in Prostate Cancer. Cancer Research. 65(18). 8118–8124. 110 indexed citations
9.
Everts, Helen B., Lloyd E. King, John P. Sundberg, & David E. Ong. (2004). Hair Cycle-Specific Immunolocalization of Retinoic Acid Synthesizing Enzymes Aldh1a2 and Aldh1a3 Indicate Complex Regulation. Journal of Investigative Dermatology. 123(2). 258–263. 27 indexed citations
10.
Fouchécourt, Sophie, Pierre Chaurand, Beverly B. DaGue, et al.. (2003). Identification, Immunolocalization, Regulation, and Postnatal Development of the Lipocalin EP17 (Epididymal Protein of 17 Kilodaltons) in the Mouse and Rat Epididymis. Endocrinology. 144(3). 887–900. 32 indexed citations
11.
Newcomer, Marcia E. & David E. Ong. (2000). Plasma retinol binding protein: structure and function of the prototypic lipocalin. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1482(1-2). 57–64. 138 indexed citations
12.
Lareyre, Jean‐Jacques, Tania Z. Thomas, Siegfried Kasper, et al.. (1999). A 5-Kilobase Pair Promoter Fragment of the Murine Epididymal Retinoic Acid-binding Protein Gene Drives the Tissue-specific, Cell-specific, and Androgen-regulated Expression of a Foreign Gene in the Epididymis of Transgenic Mice. Journal of Biological Chemistry. 274(12). 8282–8290. 37 indexed citations
13.
Zhao, Guang-Quan, Siegfried Kasper, Marcia E. Newcomer, et al.. (1998). Molecular Cloning and Hormonal Regulation of a Murine Epididymal Retinoic Acid-Binding Protein Messenger Ribonucleic Acid. Endocrinology. 139(6). 2971–2981. 44 indexed citations
14.
Newcomer, Marcia E., et al.. (1998). Detection of Conformational Changes in Cellular Retinoid-Binding Proteins by Limited Proteolysis. Humana Press eBooks. 89. 165–176. 2 indexed citations
15.
Lareyre, Jean‐Jacques, Marie‐Geneviève Mattéi, Siegfried Kasper, et al.. (1998). Genomic organization and chromosomal localization of the murine epididymal retinoic acid-binding protein (mE-RABP) gene. Molecular Reproduction and Development. 50(4). 387–395. 17 indexed citations
16.
Davis, James & David E. Ong. (1995). Retinol Processing by the Peritubular Cell from Rat Testis1. Biology of Reproduction. 52(2). 356–364. 33 indexed citations
17.
Newcomer, Marcia E., et al.. (1994). Cellular Retinoid-Binding Proteins: Limited Proteolysis Reveals a Conformational Change upon Ligand Binding. Biochemistry. 33(10). 2873–2879. 40 indexed citations
18.
Ong, David E., et al.. (1992). Purification and Partial Characterization of Cellular Retinol-Binding Protein, Type Two, from Human Small Intestine. Journal of Nutrition. 122(3). 450–456. 10 indexed citations
19.
Ong, David E. & Frank Chytil. (1988). Presence of novel retinoic acid-binding proteins in the lumen of rat epididymis. Archives of Biochemistry and Biophysics. 267(2). 474–478. 35 indexed citations
20.
Ong, David E., Sachiko Takase, & Frank Chytil. (1987). Cellular Vitamin A‐Binding Proteins in the Testisa. Annals of the New York Academy of Sciences. 513(1). 172–178. 10 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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