David W. Rodgers

4.4k total citations
84 papers, 3.5k citations indexed

About

David W. Rodgers is a scholar working on Molecular Biology, Oncology and Cellular and Molecular Neuroscience. According to data from OpenAlex, David W. Rodgers has authored 84 papers receiving a total of 3.5k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 18 papers in Oncology and 14 papers in Cellular and Molecular Neuroscience. Recurrent topics in David W. Rodgers's work include Peptidase Inhibition and Analysis (16 papers), Neuropeptides and Animal Physiology (12 papers) and Protein Structure and Dynamics (7 papers). David W. Rodgers is often cited by papers focused on Peptidase Inhibition and Analysis (16 papers), Neuropeptides and Animal Physiology (12 papers) and Protein Structure and Dynamics (7 papers). David W. Rodgers collaborates with scholars based in United States, Canada and United Kingdom. David W. Rodgers's co-authors include Stephen C. Harrison, Louis B. Hersh, Aneel K. Aggarwal, Marie Drottar, Mark Ptashne, F. W. H. Beamish, Anne‐Frances Miller, Chad Haynes, Ronald L. Koder and Jia‐Huai Wang and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David W. Rodgers

80 papers receiving 3.3k citations

Peers

David W. Rodgers
Hans Wolf Germany
Donald J. Nelson United States
James G. Omichinski United States
Larry J. W. Miercke United States
Xuefeng Ren United States
Soyeon Kim United States
Jayasimha Rao United States
Andrew J. Link United States
Hans Wolf Germany
David W. Rodgers
Citations per year, relative to David W. Rodgers David W. Rodgers (= 1×) peers Hans Wolf

Countries citing papers authored by David W. Rodgers

Since Specialization
Citations

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

Fields of papers citing papers by David W. Rodgers

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David W. Rodgers

This figure shows the co-authorship network connecting the top 25 collaborators of David W. Rodgers. A scholar is included among the top collaborators of David W. Rodgers 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 W. Rodgers. David W. Rodgers 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.
Rodgers, David W., et al.. (2024). Translation of circular RNAs. Nucleic Acids Research. 53(1). 14 indexed citations
2.
Geddes, James W., Vimala Bondada, Dorothy E. Croall, David W. Rodgers, & József Gál. (2023). Impaired activity and membrane association of most calpain-5 mutants causal for neovascular inflammatory vitreoretinopathy. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1869(6). 166747–166747. 1 indexed citations
3.
Gál, József, Vimala Bondada, Charles Mashburn, et al.. (2022). S-acylation regulates the membrane association and activity of Calpain-5. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1869(9). 119298–119298. 2 indexed citations
4.
Bondada, Vimala, József Gál, Charles Mashburn, et al.. (2021). The C2 domain of calpain 5 contributes to enzyme activation and membrane localization. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1868(7). 119019–119019. 10 indexed citations
5.
Song, Eun Suk, David W. Rodgers, & Louis B. Hersh. (2018). Insulin-degrading enzyme is not secreted from cultured cells. Scientific Reports. 8(1). 2335–2335. 20 indexed citations
6.
Song, Eun Suk, Manana Melikishvili, Michael G. Fried, et al.. (2012). Cysteine 904 Is Required for Maximal Insulin Degrading Enzyme Activity and Polyanion Activation. PLoS ONE. 7(10). e46790–e46790. 3 indexed citations
7.
Noinaj, Nicholas, et al.. (2011). Anion Activation Site of Insulin-degrading Enzyme. Journal of Biological Chemistry. 287(1). 48–57. 27 indexed citations
8.
Bruce, Catherine R., Deborah A. Smith, David W. Rodgers, et al.. (2011). Identification of a Novel Response Regulator, Crr1, That Is Required for Hydrogen Peroxide Resistance in Candida albicans. PLoS ONE. 6(12). e27979–e27979. 10 indexed citations
9.
Shen, Xin‐Ming, Thomas O. Crawford, Joan M. Brengman, et al.. (2011). Functional consequences and structural interpretation of mutations of human choline acetyltransferase. Human Mutation. 32(11). 1259–1267. 30 indexed citations
10.
Hellman, Lance M., David W. Rodgers, & Michael G. Fried. (2009). Phenomenological partial-specific volumes for G-quadruplex DNAs. European Biophysics Journal. 39(3). 389–396. 20 indexed citations
11.
Adams, Claire, Manana Melikishvili, David W. Rodgers, et al.. (2009). Topologies of Complexes Containing O6-Alkylguanine–DNA Alkyltransferase and DNA. Journal of Molecular Biology. 389(2). 248–263. 26 indexed citations
12.
Cai, Yiying, Harvey F. Chin, Darina L. Lazarova, et al.. (2008). The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell. 133(7). 1202–1213. 156 indexed citations
14.
Ray, Kallol, et al.. (2004). Crystal Structure of Human Thimet Oligopeptidase Provides Insight into Substrate Recognition, Regulation, and Localization. Journal of Biological Chemistry. 279(19). 20480–20489. 59 indexed citations
15.
Yao, Jia, et al.. (2003). Proteolytic cleavage of the puromycin-sensitive aminopeptidase generates a substrate binding domain. Archives of Biochemistry and Biophysics. 415(1). 80–86. 6 indexed citations
16.
Ray, Kallol, Christina S. Hines, & David W. Rodgers. (2002). Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition. Protein Science. 11(9). 2237–2246. 21 indexed citations
17.
Lian, Wei, Guojin Chen, Donghai Wu, et al.. (2000). Crystallization and preliminary analysis of neurolysin. Acta Crystallographica Section D Biological Crystallography. 56(12). 1644–1646. 8 indexed citations
18.
Hong, Yiling, et al.. (2000). Molecular Basis of Competition between HSF2 and Catalytic Subunit for Binding to the PR65/A Subunit of PP2A. Biochemical and Biophysical Research Communications. 272(1). 84–89. 13 indexed citations
19.
Rodgers, David W., et al.. (1987). Effects of pH and feeding regime on methylmercury accumulation within aquatic microcosms. Environmental Pollution. 45(4). 261–274. 19 indexed citations
20.
Rodgers, David W., et al.. (1976). Cow-Calf Beef Production on Irrigated Pasture and in Drylot at Carrington. NDSU Repository (North Dakota State University).

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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