Irene T. Weber

14.9k total citations · 3 hit papers
260 papers, 12.2k citations indexed

About

Irene T. Weber is a scholar working on Infectious Diseases, Virology and Molecular Biology. According to data from OpenAlex, Irene T. Weber has authored 260 papers receiving a total of 12.2k indexed citations (citations by other indexed papers that have themselves been cited), including 141 papers in Infectious Diseases, 132 papers in Virology and 105 papers in Molecular Biology. Recurrent topics in Irene T. Weber's work include HIV/AIDS drug development and treatment (139 papers), HIV Research and Treatment (132 papers) and Enzyme Structure and Function (38 papers). Irene T. Weber is often cited by papers focused on HIV/AIDS drug development and treatment (139 papers), HIV Research and Treatment (132 papers) and Enzyme Structure and Function (38 papers). Irene T. Weber collaborates with scholars based in United States, Japan and Hungary. Irene T. Weber's co-authors include Robert W. Harrison, Thomas A. Steitz, Arun K. Ghosh, John M. Louis, Johnson Agniswamy, Randall M. Story, Hiroaki Mitsuya, Yuan‐Fang Wang, Alexander Wlodawer and Péter Boross and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Irene T. Weber

257 papers receiving 11.8k citations

Hit Papers

align trajectories sort by overperformance

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease

1989 937 citations Alexander Wlodawer, Eric T. Baldwin et al. profile →
The structure of the E. coli recA protein monomer and polymer

1992 643 citations Randall M. Story, Irene T. Weber et al. Nature profile →
Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution

1987 441 citations Irene T. Weber, Thomas A. Steitz Journal of Molecular Biology profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Irene T. Weber United States	56	6.2k	4.9k	4.4k	1.5k	1.3k	260	12.2k
Jianping Ding China	49	7.8k 1.2×	3.5k 0.7×	3.0k 0.7×	430 0.3×	921 0.7×	187	11.8k
Masanori Baba Japan	62	5.0k 0.8×	6.9k 1.4×	5.9k 1.3×	3.6k 2.4×	663 0.5×	372	16.0k
Stephen H. Hughes United States	79	11.3k 1.8×	9.3k 1.9×	9.3k 2.1×	1.5k 1.0×	3.0k 2.4×	374	21.1k
David R. Davies United States	62	14.0k 2.2×	2.0k 0.4×	1.6k 0.4×	1.0k 0.7×	1.1k 0.9×	146	20.1k
Timothy N. C. Wells Switzerland	74	5.2k 0.8×	1.5k 0.3×	2.4k 0.6×	832 0.6×	934 0.7×	236	19.8k
James M. Berger United States	64	12.1k 1.9×	1.4k 0.3×	1.3k 0.3×	1.0k 0.7×	2.4k 1.9×	164	15.2k
Jacques Fantini France	54	5.2k 0.8×	1.8k 0.4×	1.9k 0.4×	633 0.4×	390 0.3×	242	9.7k
Piet Herdewijn Belgium	64	12.5k 2.0×	6.0k 1.2×	2.9k 0.7×	5.2k 3.5×	806 0.6×	787	19.5k
Robert Esnouf United Kingdom	34	3.8k 0.6×	2.0k 0.4×	1.6k 0.4×	717 0.5×	454 0.4×	76	6.7k
Rudi Pauwels Belgium	63	4.4k 0.7×	9.2k 1.9×	8.1k 1.8×	2.8k 1.9×	522 0.4×	145	14.9k

Countries citing papers authored by Irene T. Weber

Since Specialization

Citations

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

Fields of papers citing papers by Irene T. Weber

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Irene T. Weber

This figure shows the co-authorship network connecting the top 25 collaborators of Irene T. Weber. A scholar is included among the top collaborators of Irene T. Weber 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 Irene T. Weber. Irene T. Weber is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Weber, Irene T., Christopher Penschke, Angelos Michaelides, & Karina Morgenstern. (2025). Importance of Ion Size on the Dominance of Water–Ion Versus Water–Water Interactions in Au-Supported Solvatomers. Nano Letters. 25(6). 2188–2194. 2 indexed citations

Ghosh, Arun K., Arun K. Ghosh, Megan Johnson, et al.. (2023). Exploration of imatinib and nilotinib-derived templates as the P2-Ligand for HIV-1 protease inhibitors: Design, synthesis, protein X-ray structural studies, and biological evaluation. European Journal of Medicinal Chemistry. 255. 115385–115385. 4 indexed citations

Ghosh, Arun K., Dana Shahabi, Megan Johnson, et al.. (2023). Evaluation of darunavir-derived HIV-1 protease inhibitors incorporating P2′ amide-derivatives: Synthesis, biological evaluation and structural studies. Bioorganic & Medicinal Chemistry Letters. 83. 129168–129168. 3 indexed citations

Wang, Yuan-Fang, Daniel W. Kneller, Andrey Kovalevsky, et al.. (2022). HIV-1 protease with 10 lopinavir and darunavir resistance mutations exhibits altered inhibition, structural rearrangements and extreme dynamics. Journal of Molecular Graphics and Modelling. 117. 108315–108315. 3 indexed citations

Ghosh, Arun K., Arun K. Ghosh, Dana Shahabi, et al.. (2022). Design, Synthesis and X‐Ray Structural Studies of Potent HIV‐1 Protease Inhibitors Containing C‐4 Substituted Tricyclic Hexahydro‐Furofuran Derivatives as P2 Ligands. ChemMedChem. 17(9). e202200058–e202200058. 5 indexed citations

Ghosh, Arun K., Zilei Xia, William L. Robinson, et al.. (2019). Potent HIV‐1 Protease Inhibitors Containing Carboxylic and Boronic Acids: Effect on Enzyme Inhibition and Antiviral Activity and Protein‐Ligand X‐ray Structural Studies. ChemMedChem. 14(21). 1863–1872. 18 indexed citations

Tie, Yunfeng, Yuan‐Fang Wang, Péter Boross, et al.. (2012). Critical differences in HIV‐1 and HIV‐2 protease specificity for clinical inhibitors. Protein Science. 21(3). 339–350. 39 indexed citations

Chumanevich, Alexander A., et al.. (2008). Structural basis for executioner caspase recognition of P5 position in substrates. APOPTOSIS. 13(11). 1291–1302. 29 indexed citations

Fang, Bin, Péter Boross, József Tőzsér, & Irene T. Weber. (2006). Structural and Kinetic Analysis of Caspase-3 Reveals Role for S5 Binding Site in Substrate Recognition. Journal of Molecular Biology. 360(3). 654–666. 61 indexed citations

10.

Kovalevsky, Andrey, Fengling Liu, Sofiya Leshchenko, et al.. (2006). Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114. Journal of Molecular Biology. 363(1). 161–173. 116 indexed citations

11.

Chen, Aiping, Irene T. Weber, Robert W. Harrison, & Jonathan Leis. (2005). Identification of Amino Acids in HIV-1 and Avian Sarcoma Virus Integrase Subsites Required for Specific Recognition of the Long Terminal Repeat Ends. Journal of Biological Chemistry. 281(7). 4173–4182. 52 indexed citations

12.

Daniel, René, Joseph Kulkosky, Konstantin D. Taganov, et al.. (2004). Characterization of a Naphthalene Derivative Inhibitor of Retroviral Integrases. AIDS Research and Human Retroviruses. 20(2). 135–144. 6 indexed citations

13.

Torshin, I. Yu., Yuan‐Fang Wang, Garrett C. Du Bois, et al.. (2002). Crystal Structures of Tcl1 Family Oncoproteins and Their Conserved Surface Features. The Scientific World JOURNAL. 2. 1876–1884. 8 indexed citations

14.

Cartas, Maria, Satya P. Singh, Tahir A. Rizvi, et al.. (2001). Display of a Peptide Corresponding to the Dimer Structure of Protease Attenuates HIV-1 Replication. DNA and Cell Biology. 20(12). 797–805. 6 indexed citations

15.

Tőzsér, József, Gábor Zahuczky, Péter Bagossi, et al.. (2000). Comparison of the substrate specificity of the human T‐cell leukemia virus and human immunodeficiency virus proteinases. European Journal of Biochemistry. 267(20). 6287–6295. 52 indexed citations

16.

Xu, Liang, Robert W. Harrison, Irene T. Weber, & Simon J. Pilkis. (1995). Human β-Cell Glucokinase. Journal of Biological Chemistry. 270(17). 9939–9946. 44 indexed citations

17.

Story, Randall M., Irene T. Weber, & Thomas A. Steitz. (1992). The structure of the E. coli recA protein monomer and polymer. Nature. 355(6358). 318–325. 643 indexed citations breakdown →

18.

Grinde, Bjørn, Craig E. Cameron, Jonathan Leis, et al.. (1992). Analysis of substrate interactions of the Rous sarcoma virus wild type and mutant proteases and human immunodeficiency virus-1 protease using a set of systematically altered peptide substrates.. Journal of Biological Chemistry. 267(14). 9491–9498. 46 indexed citations

19.

Tőzsér, József, Alla Gustchina, Irene T. Weber, et al.. (1991). Studies on the role of the S₄ substrate binding site of HIV proteinases. FEBS Letters. 279(2). 356–360. 62 indexed citations

20.

Baldwin, Eric T., Irene T. Weber, Robert Charles, et al.. (1991). Crystal structure of interleukin 8: symbiosis of NMR and crystallography.. Proceedings of the National Academy of Sciences. 88(2). 502–506. 300 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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