Audrey L. Lamb
- Molecular Biology top 10%
- Nutrition and Dietetics top 1%
- Materials Chemistry
- Plant Science top 10%
- Oncology top 10%
- Co-authors
- Thomas V. O’HalloranAmy C. RosenzweigAmy K. WernimontKathleen M. MeneelyAndrew S. TorresDavid L. HuffmanJosé OluchaMarcia E. Newcomer
- Topics
- Enzyme Structure and Function (23 papers)Protein Structure and Dynamics (12 papers)Amino Acid Enzymes and Metabolism (11 papers)
- Journals
- Journal of the American Chemical SocietyJournal of Biological ChemistryJournal of Molecular Biology
- Partner nations
- United StatesChinaFrance
In The Last Decade
Audrey L. Lamb
52 papers receiving 1.7k citations
Peers
Comparison fields: 5 of 98
- Molecular Biology 899
- Nutrition and Dietetics 636
- Materials Chemistry 288
- Plant Science 241
- Oncology 236
Countries citing papers authored by Audrey L. Lamb
This map shows the geographic impact of Audrey L. Lamb'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 Audrey L. Lamb with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Audrey L. Lamb more than expected).
Fields of papers citing papers by Audrey L. Lamb
This network shows the impact of papers produced by Audrey L. Lamb. 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 Audrey L. Lamb. The network helps show where Audrey L. Lamb may publish in the future.
Co-authorship network of co-authors of Audrey L. Lamb
This figure shows the co-authorship network connecting the top 25 collaborators of Audrey L. Lamb. A scholar is included among the top collaborators of Audrey L. Lamb 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 Audrey L. Lamb. Audrey L. Lamb is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
| # | Work | Indexed citations |
|---|---|---|
| 1 | 1 | |
| 2 | 0 | |
| 3 | 0 | |
| 4 | 4 | |
| 5 | 2 | |
| 6 | 10 | |
| 7 | 11 | |
| 8 | 7 | |
| 9 | 7 | |
| 10 | 36 | |
| 11 | 33 | |
| 12 | 11 | |
| 13 | 7 | |
| 14 | 19 | |
| 15 | 4 | |
| 16 | 5 | |
| 17 | 56 | |
| 18 | 48 | |
| 19 | 18 | |
| 20 | 33 |
About Audrey L. Lamb
Audrey L. Lamb is a scholar working on Biochemistry, Molecular Biology and Materials Chemistry, having authored 54 papers that have together received 1.7k indexed citations. Recurring topics across this work include Enzyme Structure and Function (23 papers), Protein Structure and Dynamics (12 papers) and Amino Acid Enzymes and Metabolism (11 papers). The work is most often cited by research in Nutrition and Dietetics (636 citations), Biochemistry (148 citations) and Health, Toxicology and Mutagenesis (223 citations). Audrey L. Lamb has collaborated with scholars based in United States, China and France. Frequent co-authors include Thomas V. O’Halloran, Amy C. Rosenzweig, Amy K. Wernimont, Kathleen M. Meneely, Andrew S. Torres, David L. Huffman, José Olucha, Marcia E. Newcomer, Robert A. Pufahl and Trey A. Ronnebaum. Their work appears in journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Journal of Molecular Biology.
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.