Robert T. Nolte

7.5k total citations · 3 hit papers
33 papers, 5.8k citations indexed

About

Robert T. Nolte is a scholar working on Molecular Biology, Organic Chemistry and Genetics. According to data from OpenAlex, Robert T. Nolte has authored 33 papers receiving a total of 5.8k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 5 papers in Organic Chemistry and 5 papers in Genetics. Recurrent topics in Robert T. Nolte's work include Estrogen and related hormone effects (5 papers), Retinoids in leukemia and cellular processes (5 papers) and Peroxisome Proliferator-Activated Receptors (5 papers). Robert T. Nolte is often cited by papers focused on Estrogen and related hormone effects (5 papers), Retinoids in leukemia and cellular processes (5 papers) and Peroxisome Proliferator-Activated Receptors (5 papers). Robert T. Nolte collaborates with scholars based in United States, Japan and Australia. Robert T. Nolte's co-authors include Millard H. Lambert, Christopher K. Glass, Stefan Westin, Timothy M. Willson, G. Bruce Wisely, Jeffery E. Cobb, Riki Kurokawa, Michael V. Milburn, Michael G. Rosenfeld and David Atkinson and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Robert T. Nolte

32 papers receiving 5.6k citations

Hit Papers

Ligand binding and co-activator assembly of the peroxisom... 1998 2026 2007 2016 1998 2002 1998 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert T. Nolte United States 27 4.3k 1.4k 623 567 534 33 5.8k
Marc Labelle Canada 23 3.6k 0.9× 348 0.2× 873 1.4× 455 0.8× 819 1.5× 40 6.0k
Doris M. Benbrook United States 38 3.4k 0.8× 1.0k 0.7× 459 0.7× 126 0.2× 988 1.9× 144 5.2k
Khalil Ahmed United States 43 5.1k 1.2× 375 0.3× 396 0.6× 359 0.6× 1.5k 2.8× 240 6.9k
Jules A. Shafer United States 44 2.9k 0.7× 332 0.2× 684 1.1× 1.2k 2.2× 600 1.1× 130 6.0k
Dolores Pérez‐Sala Spain 45 3.8k 0.9× 294 0.2× 351 0.6× 922 1.6× 475 0.9× 144 6.7k
R L Erikson United States 31 3.2k 0.8× 1.2k 0.9× 333 0.5× 231 0.4× 580 1.1× 49 5.3k
Yves Gareau Canada 26 3.5k 0.8× 342 0.2× 1.1k 1.7× 443 0.8× 803 1.5× 49 6.1k
S. Stoney Simons United States 43 3.5k 0.8× 3.1k 2.2× 280 0.4× 235 0.4× 697 1.3× 149 6.0k
Robert L. Geahlen United States 56 4.7k 1.1× 332 0.2× 542 0.9× 835 1.5× 1.3k 2.5× 155 9.5k

Countries citing papers authored by Robert T. Nolte

Since Specialization
Citations

This map shows the geographic impact of Robert T. Nolte'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 Robert T. Nolte with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Robert T. Nolte more than expected).

Fields of papers citing papers by Robert T. Nolte

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert T. Nolte. 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 Robert T. Nolte. The network helps show where Robert T. Nolte may publish in the future.

Co-authorship network of co-authors of Robert T. Nolte

This figure shows the co-authorship network connecting the top 25 collaborators of Robert T. Nolte. A scholar is included among the top collaborators of Robert T. Nolte 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 Robert T. Nolte. Robert T. Nolte 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.
Nolte, Robert T., et al.. (2023). AZATHIOPRINE HYPERSENSITIVITY MIMICKING SEPSIS. Annals of Allergy Asthma & Immunology. 131(5). S98–S98.
2.
Pearce, Kenneth H., Laurie K. Overton, Robert T. Gampe, et al.. (2019). BacMam production and crystal structure of nonglycosylated apo human furin at 1.89 Å resolution. Acta Crystallographica Section F Structural Biology Communications. 75(4). 239–245. 12 indexed citations
3.
Deanda, Felix, Kendra E. Hightower, Robert T. Nolte, et al.. (2013). Dolutegravir Interactions with HIV-1 Integrase-DNA: Structural Rationale for Drug Resistance and Dissociation Kinetics. PLoS ONE. 8(10). e77448–e77448. 44 indexed citations
4.
Gampe, Robert T., Millard H. Lambert, Derek J. Parks, et al.. (2010). Structure of Rev-erbα bound to N-CoR reveals a unique mechanism of nuclear receptor–co-repressor interaction. Nature Structural & Molecular Biology. 17(7). 808–814. 68 indexed citations
5.
Sparks, Steven M., D. Mark Bickett, H. Luke Carter, et al.. (2008). Anthranilimide-based glycogen phosphorylase inhibitors for the treatment of type 2 diabetes: 1. Identification of 1-amino-1-cycloalkyl carboxylic acid headgroups. Bioorganic & Medicinal Chemistry Letters. 19(3). 976–980. 6 indexed citations
6.
Thomson, Stephen A., D. Mark Bickett, Joyce A. Boucheron, et al.. (2008). Anthranilimide based glycogen phosphorylase inhibitors for the treatment of type 2 diabetes. Part 3: X-ray crystallographic characterization, core and urea optimization and in vivo efficacy. Bioorganic & Medicinal Chemistry Letters. 19(4). 1177–1182. 16 indexed citations
7.
Trump, Ryan P., Barry G. Shearer, Millard H. Lambert, et al.. (2007). Co-crystal structure guided array synthesis of PPARγ inverse agonists. Bioorganic & Medicinal Chemistry Letters. 17(14). 3916–3920. 15 indexed citations
8.
Miyazaki, Yasushi, Jun Tang, Yutaka Maeda, et al.. (2006). Orally active 4-amino-5-diarylurea-furo[2,3-d]pyrimidine derivatives as anti-angiogenic agent inhibiting VEGFR2 and Tie-2. Bioorganic & Medicinal Chemistry Letters. 17(6). 1773–1778. 29 indexed citations
9.
Wang, Liping, William J. Zuercher, Thomas G. Consler, et al.. (2006). X-ray Crystal Structures of the Estrogen-related Receptor-γ Ligand Binding Domain in Three Functional States Reveal the Molecular Basis of Small Molecule Regulation. Journal of Biological Chemistry. 281(49). 37773–37781. 110 indexed citations
10.
Hassell, Anne M., Gang An, Randy K. Bledsoe, et al.. (2006). Crystallization of protein–ligand complexes. Acta Crystallographica Section D Biological Crystallography. 63(1). 72–79. 120 indexed citations
11.
Chao, Esther Y., Jon L. Collins, Stéphanie Gaillard, et al.. (2005). Structure-guided synthesis of tamoxifen analogs with improved selectivity for the orphan ERRγ. Bioorganic & Medicinal Chemistry Letters. 16(4). 821–824. 79 indexed citations
12.
Miyazaki, Yasushi, Jun Tang, Yutaka Maeda, et al.. (2005). Novel 4-amino-furo[2,3-d]pyrimidines as Tie-2 and VEGFR2 dual inhibitors. Bioorganic & Medicinal Chemistry Letters. 15(9). 2203–2207. 141 indexed citations
13.
Veal, James M., Robert T. Nolte, Liping Wang, et al.. (2005). Discovery of a novel and potent series of dianilinopyrimidineurea and urea isostere inhibitors of VEGFR2 tyrosine kinase. Bioorganic & Medicinal Chemistry Letters. 15(15). 3519–3523. 27 indexed citations
14.
Xu, Robert X., Warren J. Rocque, Millard H. Lambert, et al.. (2004). Crystal Structures of the Catalytic Domain of Phosphodiesterase 4B Complexed with AMP, 8-Br-AMP, and Rolipram. Journal of Molecular Biology. 337(2). 355–365. 92 indexed citations
15.
Xu, H. Eric, Thomas B. Stanley, Valerie G. Montana, et al.. (2002). Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARα. Nature. 415(6873). 813–817. 521 indexed citations breakdown →
16.
Dutta, Shuchismita, Ildikó V. Akey, Colin Dingwall, et al.. (2001). The Crystal Structure of Nucleoplasmin-Core. Molecular Cell. 8(4). 841–853. 138 indexed citations
17.
Westin, Stefan, Riki Kurokawa, Robert T. Nolte, et al.. (1998). Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators. Nature. 395(6698). 199–202. 284 indexed citations
18.
McInerney, Eileen M., David W. Rose, Sarah E. Flynn, et al.. (1998). Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes & Development. 12(21). 3357–3368. 503 indexed citations breakdown →
19.
Nolte, Robert T., Michael J. Eck, Joseph Schlessinger, Steven E. Shoelson, & Stephen C. Harrison. (1996). Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes. Nature Structural & Molecular Biology. 3(4). 364–374. 115 indexed citations
20.
Nolte, Robert T. & David Atkinson. (1992). Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism. Biophysical Journal. 63(5). 1221–1239. 147 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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