Jaisri R. Lingappa

2.5k total citations
36 papers, 1.9k citations indexed

About

Jaisri R. Lingappa is a scholar working on Virology, Infectious Diseases and Molecular Biology. According to data from OpenAlex, Jaisri R. Lingappa has authored 36 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Virology, 16 papers in Infectious Diseases and 15 papers in Molecular Biology. Recurrent topics in Jaisri R. Lingappa's work include HIV Research and Treatment (23 papers), HIV/AIDS drug development and treatment (14 papers) and Bacteriophages and microbial interactions (10 papers). Jaisri R. Lingappa is often cited by papers focused on HIV Research and Treatment (23 papers), HIV/AIDS drug development and treatment (14 papers) and Bacteriophages and microbial interactions (10 papers). Jaisri R. Lingappa collaborates with scholars based in United States, India and United Kingdom. Jaisri R. Lingappa's co-authors include Kevin Klein, Vishwanath R. Lingappa, Günter Blobel, Jonathan C. Reed, Heather M. Craig, Michael H. Malim, Rebecca K. Holmes, Ann M. Sheehy, Patti Kiser and Rajani Prasad and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Jaisri R. Lingappa

35 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jaisri R. Lingappa United States 21 991 949 553 506 378 36 1.9k
Andrew J. Mouland Canada 38 1.4k 1.4× 2.4k 2.5× 766 1.4× 370 0.7× 573 1.5× 90 3.5k
Robert A. Marciniak United States 20 612 0.6× 1.8k 1.9× 220 0.4× 234 0.5× 254 0.7× 28 2.4k
Erik Serrao United States 22 906 0.9× 995 1.0× 674 1.2× 257 0.5× 227 0.6× 30 1.7k
Scott W. Eastman United States 17 619 0.6× 402 0.4× 392 0.7× 294 0.6× 178 0.5× 20 1.2k
Erwann Le Rouzic France 21 959 1.0× 824 0.9× 569 1.0× 254 0.5× 359 0.9× 28 1.5k
Susana Guerra Spain 31 523 0.5× 1.8k 1.9× 320 0.6× 767 1.5× 1.3k 3.3× 67 3.2k
Ling‐Jun Zhao United States 23 701 0.7× 971 1.0× 439 0.8× 269 0.5× 480 1.3× 62 1.9k
Patrick Kanda United States 22 576 0.6× 915 1.0× 241 0.4× 199 0.4× 457 1.2× 46 1.7k
Rosemary Kiernan France 19 1.1k 1.1× 1.8k 1.8× 572 1.0× 265 0.5× 523 1.4× 33 2.6k
Betty Poon United States 22 1.2k 1.3× 1.1k 1.2× 630 1.1× 324 0.6× 626 1.7× 33 2.1k

Countries citing papers authored by Jaisri R. Lingappa

Since Specialization
Citations

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

Fields of papers citing papers by Jaisri R. Lingappa

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jaisri R. Lingappa

This figure shows the co-authorship network connecting the top 25 collaborators of Jaisri R. Lingappa. A scholar is included among the top collaborators of Jaisri R. Lingappa 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 Jaisri R. Lingappa. Jaisri R. Lingappa 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.
Reed, Jonathan C., et al.. (2020). Identification of an Antiretroviral Small Molecule That Appears To Be a Host-Targeting Inhibitor of HIV-1 Assembly. Journal of Virology. 95(3). 8 indexed citations
2.
3.
Barajas, Brook C., et al.. (2018). Identifying the assembly intermediate in which Gag first associates with unspliced HIV-1 RNA suggests a novel model for HIV-1 RNA packaging. PLoS Pathogens. 14(4). e1006977–e1006977. 22 indexed citations
4.
Sette, Paola, Vincent Dussupt, Kunio Nagashima, et al.. (2016). HIV-1 Nucleocapsid Mimics the Membrane Adaptor Syntenin PDZ to Gain Access to ESCRTs and Promote Virus Budding. Cell Host & Microbe. 19(3). 336–348. 19 indexed citations
5.
6.
Lingappa, Jaisri R. & Richard E. Zigmond. (2013). Limited Recovery of Pineal Function after Regeneration of Preganglionic Sympathetic Axons: Evidence for Loss of Ganglionic Synaptic Specificity. Journal of Neuroscience. 33(11). 4867–4874. 7 indexed citations
7.
8.
Okeoma, Chioma M., et al.. (2010). APOBEC3 Proteins Expressed in Mammary Epithelial Cells Are Packaged into Retroviruses and Can Restrict Transmission of Milk-Borne Virions. Cell Host & Microbe. 8(6). 534–543. 52 indexed citations
9.
Lingappa, Jaisri R. & Beth K Thielen. (2009). Assembly of Immature HIV-1 Capsids Using a Cell-Free System. Methods in molecular biology. 485. 185–195. 7 indexed citations
10.
Thielen, Beth K, et al.. (2007). T Cells Contain an RNase-Insensitive Inhibitor of APOBEC3G Deaminase Activity. PLoS Pathogens. 3(9). e135–e135. 39 indexed citations
11.
12.
Lingappa, Vishwanath R. & Jaisri R. Lingappa. (2005). Recent insights into biological regulation from cell-free protein-synthesizing systems.. PubMed. 72(3). 141–60. 7 indexed citations
13.
Klein, Kevin, et al.. (2005). Identification of Residues in the Hepatitis C Virus Core Protein That Are Critical for Capsid Assembly in a Cell-Free System. Journal of Virology. 79(11). 6814–6826. 46 indexed citations
14.
Lingappa, Jaisri R., et al.. (2005). Comparing capsid assembly of primate lentiviruses and hepatitis B virus using cell-free systems. Virology. 333(1). 114–123. 18 indexed citations
15.
Klein, Kevin, et al.. (2005). Identification of Residues in the Hepatitis C Virus Core Protein That Are Critical for Capsid Assembly in a Cell-Free System. Journal of Virology. 79(15). 10098–10098. 2 indexed citations
16.
Holmes, Rebecca K., Heather M. Craig, Kevin Klein, et al.. (2005). Antiviral Function of APOBEC3G Can Be Dissociated from Cytidine Deaminase Activity. Current Biology. 15(2). 166–170. 410 indexed citations
17.
Pineda, Mario Javier, et al.. (2004). Characterization of virus infectivity and cell‐free capsid assembly of SIVMneCL8. Journal of Medical Primatology. 33(5-6). 262–271. 5 indexed citations
18.
Lingappa, Jaisri R., et al.. (2004). Cell‐free systems for capsid assembly of primate lentiviruses from three different lineages. Journal of Medical Primatology. 33(5-6). 272–280. 7 indexed citations
19.
Klein, Kevin, et al.. (2002). Identification of a host protein essential for assembly of immature HIV-1 capsids. Nature. 415(6867). 88–92. 187 indexed citations
20.
Singh, Aalok R., et al.. (2001). Effect of Mutations in Gag on Assembly of Immature Human Immunodeficiency Virus Type 1 Capsids in a Cell-Free System. Virology. 279(1). 257–270. 27 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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