Andrew R. Nager

2.2k total citations
22 papers, 1.5k citations indexed

About

Andrew R. Nager is a scholar working on Molecular Biology, Genetics and Oncology. According to data from OpenAlex, Andrew R. Nager has authored 22 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 12 papers in Genetics and 5 papers in Oncology. Recurrent topics in Andrew R. Nager's work include Genetic and Kidney Cyst Diseases (8 papers), Cellular transport and secretion (5 papers) and RNA and protein synthesis mechanisms (4 papers). Andrew R. Nager is often cited by papers focused on Genetic and Kidney Cyst Diseases (8 papers), Cellular transport and secretion (5 papers) and RNA and protein synthesis mechanisms (4 papers). Andrew R. Nager collaborates with scholars based in United States, France and Italy. Andrew R. Nager's co-authors include Maxence V. Nachury, Fan Ye, Robert T. Sauer, Tania A. Baker, Steven E. Glynn, Andreas Martin, Vicente Herranz‐Pérez, José Manuel García‐Verdugo, Didier Portran and Swapnil Rohidas Shinde and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Andrew R. Nager

22 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Andrew R. Nager United States 15 1.2k 792 394 167 120 22 1.5k
Mark A. DeWitt United States 18 1.9k 1.5× 451 0.6× 308 0.8× 136 0.8× 44 0.4× 22 2.1k
Jon Kenniston United States 10 780 0.6× 248 0.3× 308 0.8× 93 0.6× 45 0.4× 20 1.0k
Ali Hamiche France 28 3.4k 2.8× 337 0.4× 246 0.6× 267 1.6× 222 1.9× 51 3.8k
Kerstin S. Wendt Netherlands 19 2.8k 2.3× 483 0.6× 227 0.6× 77 0.5× 137 1.1× 29 3.0k
Stefan Lampel Germany 13 1.2k 1.0× 801 1.0× 124 0.3× 161 1.0× 72 0.6× 16 1.8k
Kyuho Han United States 14 1.4k 1.2× 382 0.5× 142 0.4× 170 1.0× 59 0.5× 24 1.7k
Claudia Cattoglio United States 25 3.6k 3.0× 784 1.0× 127 0.3× 281 1.7× 157 1.3× 40 4.0k
Cemal Gürkan Cyprus 13 1.0k 0.8× 259 0.3× 723 1.8× 43 0.3× 85 0.7× 34 1.6k
Cindy Y. Jao United States 11 1.4k 1.2× 269 0.3× 152 0.4× 124 0.7× 60 0.5× 11 1.7k
Simon J. Elsässer Sweden 24 2.0k 1.7× 218 0.3× 85 0.2× 146 0.9× 72 0.6× 43 2.3k

Countries citing papers authored by Andrew R. Nager

Since Specialization
Citations

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

Fields of papers citing papers by Andrew R. Nager

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Andrew R. Nager. 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 Andrew R. Nager. The network helps show where Andrew R. Nager may publish in the future.

Co-authorship network of co-authors of Andrew R. Nager

This figure shows the co-authorship network connecting the top 25 collaborators of Andrew R. Nager. A scholar is included among the top collaborators of Andrew R. Nager 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 Andrew R. Nager. Andrew R. Nager 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.
Liu, Zhonglin, Marscha Hirschi, Oleg Brodsky, et al.. (2024). An allosteric cyclin E-CDK2 site mapped by paralog hopping with covalent probes. Nature Chemical Biology. 21(3). 420–431. 7 indexed citations
2.
Lin, Regina, Andrew R. Nager, Spencer Park, et al.. (2022). Design and Validation of Inducible TurboCARs with Tunable Induction and Combinatorial Cytokine Signaling. Cancer Immunology Research. 10(9). 1069–1083. 6 indexed citations
3.
Liu, Weifeng, Kevin C. Lindquist, Manqing Li, et al.. (2021). Structural delineation and phase-dependent activation of the costimulatory CD27:CD70 complex. Journal of Biological Chemistry. 297(4). 101102–101102. 8 indexed citations
4.
Shinde, Swapnil Rohidas, Andrew R. Nager, & Maxence V. Nachury. (2020). Ubiquitin chains earmark GPCRs for BBSome-mediated removal from cilia. The Journal of Cell Biology. 219(12). 58 indexed citations
5.
Martinez‐Fonts, Kirby, Caroline Davis, Takuya Tomita, et al.. (2020). The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates. Nature Communications. 11(1). 477–477. 107 indexed citations
6.
Chou, Hui‐Ting, Daniel P. Farrell, Jonathan Woodsmith, et al.. (2019). The Molecular Architecture of Native BBSome Obtained by an Integrated Structural Approach. Structure. 27(9). 1384–1394.e4. 38 indexed citations
7.
Chin, Sherman M., Christopher R. Kimberlin, Zygy Roe-Žurž, et al.. (2018). Structure of the 4-1BB/4-1BBL complex and distinct binding and functional properties of utomilumab and urelumab. Nature Communications. 9(1). 4679–4679. 95 indexed citations
8.
Ye, Fan, Andrew R. Nager, & Maxence V. Nachury. (2018). BBSome trains remove activated GPCRs from cilia by enabling passage through the transition zone. The Journal of Cell Biology. 217(5). 1847–1868. 185 indexed citations
9.
Glynn, Steven E., et al.. (2017). Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation. Journal of Biological Chemistry. 292(14). 5695–5704. 12 indexed citations
10.
Nager, Andrew R., Vicente Herranz‐Pérez, Didier Portran, et al.. (2016). An Actin Network Dispatches Ciliary GPCRs into Extracellular Vesicles to Modulate Signaling. Cell. 168(1-2). 252–263.e14. 270 indexed citations
11.
Nager, Andrew R., et al.. (2015). Coordinated gripping of substrate by subunits of a AAA+ proteolytic machine. Nature Chemical Biology. 11(3). 201–206. 50 indexed citations
12.
Liew, Gerald, Fan Ye, Andrew R. Nager, et al.. (2014). The Intraflagellar Transport Protein IFT27 Promotes BBSome Exit from Cilia through the GTPase ARL6/BBS3. Developmental Cell. 31(3). 265–278. 159 indexed citations
13.
Mourão, André, Andrew R. Nager, Maxence V. Nachury, & Esben Lorentzen. (2014). Structural basis for membrane targeting of the BBSome by ARL6. Nature Structural & Molecular Biology. 21(12). 1035–1041. 64 indexed citations
14.
Olivares, Adrian O., et al.. (2014). Mechanochemical basis of protein degradation by a double-ring AAA+ machine. Nature Structural & Molecular Biology. 21(10). 871–875. 1 indexed citations
15.
Wohlever, Matthew L., Andrew R. Nager, Tania A. Baker, & Robert T. Sauer. (2013). Engineering fluorescent protein substrates for the AAA+ Lon protease. Protein Engineering Design and Selection. 26(4). 299–305. 22 indexed citations
16.
Stinson, Benjamin M., Andrew R. Nager, Steven E. Glynn, et al.. (2013). Nucleotide Binding and Conformational Switching in the Hexameric Ring of a AAA+ Machine. Cell. 153(3). 628–639. 82 indexed citations
17.
Gaidukov, Leonid, Andrew R. Nager, Shangzhe Xu, Marsha Penman, & Monty Krieger. (2011). Glycine Dimerization Motif in the N-terminal Transmembrane Domain of the High Density Lipoprotein Receptor SR-BI Required for Normal Receptor Oligomerization and Lipid Transport. Journal of Biological Chemistry. 286(21). 18452–18464. 52 indexed citations
18.
Nager, Andrew R., Tania A. Baker, & Robert T. Sauer. (2011). Stepwise Unfolding of a β Barrel Protein by the AAA+ ClpXP Protease. Journal of Molecular Biology. 413(1). 4–16. 58 indexed citations
19.
Glynn, Steven E., Andreas Martin, Andrew R. Nager, Tania A. Baker, & Robert T. Sauer. (2009). Crystal structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine. DSpace@MIT (Massachusetts Institute of Technology). 9 indexed citations
20.
Glynn, Steven E., Andreas Martin, Andrew R. Nager, Tania A. Baker, & Robert T. Sauer. (2009). Structures of Asymmetric ClpX Hexamers Reveal Nucleotide-Dependent Motions in a AAA+ Protein-Unfolding Machine. Cell. 139(4). 744–756. 211 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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