Robert S. Freeman

4.5k total citations · 4 hit papers
38 papers, 3.8k citations indexed

About

Robert S. Freeman is a scholar working on Molecular Biology, Cancer Research and Cellular and Molecular Neuroscience. According to data from OpenAlex, Robert S. Freeman has authored 38 papers receiving a total of 3.8k indexed citations (citations by other indexed papers that have themselves been cited), including 25 papers in Molecular Biology, 12 papers in Cancer Research and 10 papers in Cellular and Molecular Neuroscience. Recurrent topics in Robert S. Freeman's work include Cell death mechanisms and regulation (9 papers), Cancer, Hypoxia, and Metabolism (9 papers) and Nerve injury and regeneration (9 papers). Robert S. Freeman is often cited by papers focused on Cell death mechanisms and regulation (9 papers), Cancer, Hypoxia, and Metabolism (9 papers) and Nerve injury and regeneration (9 papers). Robert S. Freeman collaborates with scholars based in United States, France and Germany. Robert S. Freeman's co-authors include Robert J. Crowder, Eugene M. Johnson, Steven Estus, William J. Zaks, M C Gruda, R Bravo, Patrick D. Sarmiere, Elizabeth A. Lipscomb, Sanjay B. Maggirwar and Stephen Dewhurst and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Neuron.

In The Last Decade

Robert S. Freeman

38 papers receiving 3.8k citations

Hit Papers

Altered gene expression in neurons during programmed cell... 1994 2026 2004 2015 1994 1994 1998 2005 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert S. Freeman United States 27 2.6k 1.1k 1.0k 454 376 38 3.8k
Gang Pei China 36 3.9k 1.5× 670 0.6× 1.3k 1.3× 523 1.2× 345 0.9× 92 5.3k
Mario Encinas Spain 29 2.0k 0.8× 345 0.3× 780 0.7× 402 0.9× 343 0.9× 49 3.4k
Ryoji Yao Japan 21 3.4k 1.3× 502 0.5× 880 0.8× 813 1.8× 658 1.8× 42 5.0k
Keejung Yoon South Korea 29 3.1k 1.2× 663 0.6× 492 0.5× 420 0.9× 653 1.7× 74 4.5k
Deborah J. Stumpo United States 37 3.5k 1.4× 610 0.6× 426 0.4× 347 0.8× 626 1.7× 88 4.5k
Norihisa Masuyama Japan 26 4.0k 1.5× 540 0.5× 568 0.5× 789 1.7× 824 2.2× 31 5.1k
Jonathan R. Whitfield United Kingdom 19 3.0k 1.2× 551 0.5× 936 0.9× 897 2.0× 302 0.8× 34 4.0k
Chia‐Yi Kuan United States 16 4.4k 1.7× 579 0.5× 1.2k 1.1× 717 1.6× 789 2.1× 21 5.7k
Syu-ichi Hirai Japan 29 2.9k 1.1× 554 0.5× 642 0.6× 563 1.2× 845 2.2× 45 4.2k
Michio Tamatani Japan 24 1.7k 0.7× 439 0.4× 659 0.6× 206 0.5× 543 1.4× 43 3.0k

Countries citing papers authored by Robert S. Freeman

Since Specialization
Citations

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

Fields of papers citing papers by Robert S. Freeman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert S. Freeman

This figure shows the co-authorship network connecting the top 25 collaborators of Robert S. Freeman. A scholar is included among the top collaborators of Robert S. Freeman 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 S. Freeman. Robert S. Freeman 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.
Papasergi-Scott, Makaía M., Hannah M. Stoveken, PuiYee Chan, et al.. (2018). Dual phosphorylation of Ric-8A enhances its ability to mediate G protein α subunit folding and to stimulate guanine nucleotide exchange. Science Signaling. 11(532). 12 indexed citations
2.
Bellizzi, Matthew J., et al.. (2018). The Mixed-Lineage Kinase Inhibitor URMC-099 Protects Hippocampal Synapses in Experimental Autoimmune Encephalomyelitis. eNeuro. 5(6). ENEURO.0245–18.2018. 15 indexed citations
3.
Holmes, Brent, et al.. (2017). mTORC2/AKT/HSF1/HuR constitute a feed-forward loop regulating Rictor expression and tumor growth in glioblastoma. Oncogene. 37(6). 732–743. 44 indexed citations
4.
Fernandes, Kimberly A., Jeffrey M. Harder, Robert S. Freeman, et al.. (2012). JNK2 and JNK3 are major regulators of axonal injury-induced retinal ganglion cell death. Neurobiology of Disease. 46(2). 393–401. 115 indexed citations
5.
Zhong, Zhihui, Yaoming Wang, Huang Guo, et al.. (2010). Protein S Protects Neurons from Excitotoxic Injury by Activating the TAM Receptor Tyro3–Phosphatidylinositol 3-Kinase–Akt Pathway through Its Sex Hormone-Binding Globulin-Like Region. Journal of Neuroscience. 30(46). 15521–15534. 47 indexed citations
6.
Xie, Liang, Kunhong Xiao, Erin J. Whalen, et al.. (2009). Oxygen-Regulated β 2 -Adrenergic Receptor Hydroxylation by EGLN3 and Ubiquitylation by pVHL. Science Signaling. 2(78). ra33–ra33. 125 indexed citations
7.
Freeman, Robert S., et al.. (2009). The von Hippel-Lindau protein sensitizes renal carcinoma cells to apoptotic stimuli through stabilization of BIMEL. Oncogene. 28(16). 1864–1874. 24 indexed citations
9.
Freeman, Robert S., et al.. (2007). Prolyl hydroxylase inhibitors delay neuronal cell death caused by trophic factor deprivation. Journal of Neurochemistry. 103(5). 1897–1906. 41 indexed citations
10.
Fu, Jian, Keon E. Menzies, Robert S. Freeman, & Mark B. Taubman. (2007). EGLN3 Prolyl Hydroxylase Regulates Skeletal Muscle Differentiation and Myogenin Protein Stability. Journal of Biological Chemistry. 282(17). 12410–12418. 67 indexed citations
11.
Freeman, Robert S., et al.. (2004). NGF deprivation-induced gene expression: after ten years, where do we stand?. Progress in brain research. 146. 111–126. 82 indexed citations
12.
Farhana, Lulu, Marcia I. Dawson, Ying Huang, et al.. (2004). Apoptosis signaling by the novel compound 3-Cl-AHPC involves increased EGFR proteolysis and accompanying decreased phosphatidylinositol 3-kinase and AKT kinase activities. Oncogene. 23(10). 1874–1884. 14 indexed citations
13.
Lipscomb, Elizabeth A., et al.. (2003). Induction of SM‐20 in PC12 cells leads to increased cytochrome c levels, accumulation of cytochrome c in the cytosol, and caspase‐dependent cell death. Journal of Neurochemistry. 85(2). 318–328. 35 indexed citations
14.
Wolf, Günter, Sigrid Harendza, Regine Schroeder, et al.. (2002). Angiotensin II's Antiproliferative Effects Mediated Through AT2-Receptors Depend On Down-Regulation of SM-20. Laboratory Investigation. 82(10). 1305–1317. 33 indexed citations
15.
Lipscomb, Elizabeth A., Patrick D. Sarmiere, & Robert S. Freeman. (2001). SM-20 Is a Novel Mitochondrial Protein That Causes Caspase-dependent Cell Death in Nerve Growth Factor-dependent Neurons. Journal of Biological Chemistry. 276(7). 5085–5092. 85 indexed citations
16.
Lipscomb, Elizabeth A., Patrick D. Sarmiere, Robert J. Crowder, & Robert S. Freeman. (1999). Expression of the SM‐20 Gene Promotes Death in Nerve Growth Factor‐Dependent Sympathetic Neurons. Journal of Neurochemistry. 73(1). 429–432. 69 indexed citations
17.
Freeman, Robert S.. (1994). Adult treatment with removal of all four permanent canines. American Journal of Orthodontics and Dentofacial Orthopedics. 106(5). 549–554. 2 indexed citations
18.
Freeman, Robert S., Steven Estus, & Eugene M. Johnson. (1994). Analysis of cell cycle-related gene expression in postmitotic neurons: Selective induction of cyclin D1 during programmed cell death. Neuron. 12(2). 343–355. 511 indexed citations breakdown →
19.
Smith, Carthage J., Eugene M. Johnson, Patricia A. Osborne, et al.. (1993). NGF deprivation and neuronal degeneration trigger altered β-amyloid precursor protein gene expression in the rat superior cervical ganglia in vivo and in vitro. Molecular Brain Research. 17(3-4). 328–334. 21 indexed citations
20.
Freeman, Robert S., Steven Estus, Kazuhiko Horigome, & Eugene M. Johnson. (1993). Cell death genes in invertebrates and (maybe) vertebrates. Current Opinion in Neurobiology. 3(1). 25–31. 36 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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