Judith G. Levin

6.1k total citations
83 papers, 5.1k citations indexed

About

Judith G. Levin is a scholar working on Virology, Molecular Biology and Infectious Diseases. According to data from OpenAlex, Judith G. Levin has authored 83 papers receiving a total of 5.1k indexed citations (citations by other indexed papers that have themselves been cited), including 60 papers in Virology, 48 papers in Molecular Biology and 46 papers in Infectious Diseases. Recurrent topics in Judith G. Levin's work include HIV Research and Treatment (60 papers), HIV/AIDS drug development and treatment (43 papers) and RNA and protein synthesis mechanisms (24 papers). Judith G. Levin is often cited by papers focused on HIV Research and Treatment (60 papers), HIV/AIDS drug development and treatment (43 papers) and RNA and protein synthesis mechanisms (24 papers). Judith G. Levin collaborates with scholars based in United States, Poland and Cameroon. Judith G. Levin's co-authors include Louis E. Henderson, Jianhui Guo, Karin Musier‐Forsyth, Alan Rein, A Rein, Ioulia Rouzina, Robert J. Gorelick, Yasumasa Iwatani, Tiyun Wu and Robert M. Friedman and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Judith G. Levin

82 papers receiving 4.9k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Judith G. Levin United States 44 3.2k 3.1k 2.1k 872 528 83 5.1k
Jean‐Luc Darlix France 37 3.0k 0.9× 2.5k 0.8× 1.4k 0.7× 510 0.6× 365 0.7× 89 4.2k
Jonathan Leis United States 46 3.8k 1.2× 3.2k 1.0× 2.4k 1.2× 1.2k 1.4× 747 1.4× 108 6.8k
Wei-Shau Hu United States 36 2.3k 0.7× 3.2k 1.1× 1.9k 0.9× 931 1.1× 666 1.3× 105 4.6k
J L Darlix France 33 2.7k 0.8× 2.4k 0.8× 1.4k 0.7× 454 0.5× 283 0.5× 60 3.8k
Anna Marie Skalka United States 44 3.7k 1.1× 2.7k 0.9× 2.7k 1.3× 732 0.8× 333 0.6× 103 5.6k
Bahige M. Baroudy United States 37 1.2k 0.4× 1.8k 0.6× 1.7k 0.8× 1.1k 1.2× 758 1.4× 65 4.3k
Robert J. Gorelick United States 52 5.0k 1.6× 5.8k 1.9× 3.5k 1.7× 1.5k 1.7× 1.2k 2.3× 133 8.6k
Jean‐Christophe Paillart France 35 2.8k 0.9× 2.1k 0.7× 1.0k 0.5× 591 0.7× 417 0.8× 68 3.7k
Stephen R. Petteway United States 25 1.6k 0.5× 3.1k 1.0× 2.1k 1.0× 1.1k 1.2× 1.4k 2.6× 47 4.8k
José L. Nieva Spain 36 2.5k 0.8× 1.4k 0.4× 896 0.4× 683 0.8× 657 1.2× 118 4.1k

Countries citing papers authored by Judith G. Levin

Since Specialization
Citations

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

Fields of papers citing papers by Judith G. Levin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Judith G. Levin. 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 Judith G. Levin. The network helps show where Judith G. Levin may publish in the future.

Co-authorship network of co-authors of Judith G. Levin

This figure shows the co-authorship network connecting the top 25 collaborators of Judith G. Levin. A scholar is included among the top collaborators of Judith G. Levin 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 Judith G. Levin. Judith G. Levin 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.
Olson, Erik D., Robert J. Gorelick, Ioulia Rouzina, et al.. (2016). Mechanistic differences between HIV-1 and SIV nucleocapsid proteins and cross-species HIV-1 genomic RNA recognition. Retrovirology. 13(1). 89–89. 13 indexed citations
2.
Wu, Tiyun, Robert J. Gorelick, & Judith G. Levin. (2014). Selection of fully processed HIV-1 nucleocapsid protein is required for optimal nucleic acid chaperone activity in reverse transcription. Virus Research. 193. 52–64. 12 indexed citations
3.
Chaurasiya, Kathy R., Micah J. McCauley, Wei Wang, et al.. (2013). Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein. Nature Chemistry. 6(1). 28–33. 59 indexed citations
4.
Byeon, In‐Ja L., Jin-Woo Ahn, Mithun Mitra, et al.. (2013). NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. Nature Communications. 4(1). 1890–1890. 110 indexed citations
5.
Mitra, Mithun, Kamil Hercík, Jin-Woo Ahn, et al.. (2013). Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties. Nucleic Acids Research. 42(2). 1095–1110. 58 indexed citations
6.
Hergott, Christopher A., Mithun Mitra, Jianhui Guo, et al.. (2012). Zinc finger function of HIV-1 nucleocapsid protein is required for removal of 5′-terminal genomic RNA fragments: A paradigm for RNA removal reactions in HIV-1 reverse transcription. Virus Research. 171(2). 346–355. 9 indexed citations
7.
Jiang, Jiyang, Sherimay D. Ablan, Kamil Hercík, et al.. (2011). The interdomain linker region of HIV-1 capsid protein is a critical determinant of proper core assembly and stability. Virology. 421(2). 253–265. 43 indexed citations
8.
Levin, Judith G., Mithun Mitra, Anjali Mascarenhas, & Karin Musier‐Forsyth. (2010). Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription. RNA Biology. 7(6). 754–774. 126 indexed citations
9.
Kankia, Besik, Victoria Yang, Elizabeth Cramer, et al.. (2009). Fidelity of plus-strand priming requires the nucleic acid chaperone activity of HIV-1 nucleocapsid protein. Nucleic Acids Research. 37(6). 1755–1766. 21 indexed citations
10.
Tang, Shixing, Sherimay D. Ablan, Megan E. Dueck, et al.. (2006). A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Virology. 359(1). 105–115. 5 indexed citations
11.
Iwatani, Yasumasa, et al.. (2003). Efficient Initiation of HIV-1 Reverse Transcriptionin Vitro. Journal of Biological Chemistry. 278(16). 14185–14195. 41 indexed citations
12.
Harbron, Elizabeth J., Donald B. O’Connor, Jianhui Guo, et al.. (2002). Nucleic Acid Conformational Changes Essential for HIV-1 Nucleocapsid Protein-mediated Inhibition of Self-priming in Minus-strand Transfer. Journal of Molecular Biology. 325(1). 1–10. 60 indexed citations
13.
Powell, Michael D., William A. Beard, Katarzyna Bębenek, et al.. (1999). Residues in the αH and αI Helices of the HIV-1 Reverse Transcriptase Thumb Subdomain Required for the Specificity of RNase H-catalyzed Removal of the Polypurine Tract Primer. Journal of Biological Chemistry. 274(28). 19885–19893. 42 indexed citations
14.
15.
Roth, Robert I., Wiesław Kaca, & Judith G. Levin. (1994). Hemoglobin: a newly recognized binding protein for bacterial endotoxins (LPS).. PubMed. 388. 161–72. 15 indexed citations
16.
17.
Woerner, Amy M., Michael Klutch, Judith G. Levin, & Carol J. Marcus-Sekura. (1992). Localization of DNA Binding Activity of HIV-1 Integrase to the C-Terminal Half of the Protein. AIDS Research and Human Retroviruses. 8(2). 297–304. 83 indexed citations
18.
Marcus-Sekura, Carol J., Amy M. Woerner, M Zweig, et al.. (1990). Expression of HIV-1 Integrase in E. coli: Immunological Analysis of the Recombinant Protein. AIDS Research and Human Retroviruses. 6(12). 1399–1408. 7 indexed citations
19.
20.
Feng, Yan, Dolph L. Hatfield, A Rein, & Judith G. Levin. (1989). Translational readthrough of the murine leukemia virus gag gene amber codon does not require virus-induced alteration of tRNA. Journal of Virology. 63(5). 2405–2410. 35 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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