Rati Verma

5.1k total citations · 1 hit paper
30 papers, 4.0k citations indexed

About

Rati Verma is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, Rati Verma has authored 30 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 14 papers in Oncology and 8 papers in Cell Biology. Recurrent topics in Rati Verma's work include Ubiquitin and proteasome pathways (19 papers), Peptidase Inhibition and Analysis (9 papers) and Fungal and yeast genetics research (8 papers). Rati Verma is often cited by papers focused on Ubiquitin and proteasome pathways (19 papers), Peptidase Inhibition and Analysis (9 papers) and Fungal and yeast genetics research (8 papers). Rati Verma collaborates with scholars based in United States, Germany and Switzerland. Rati Verma's co-authors include Raymond J. Deshaies, Robert Oania, John R. Yates, W. Hayes McDonald, L. Aravind, Eugene V. Koonin, R. M. Renny Feldman, Michael J. Huddleston, Roland S. Annan and Johannes Graumann and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Rati Verma

29 papers receiving 4.0k citations

Hit Papers

Role of Rpn11 Metalloprotease in Deubiquitination and Deg... 2002 2026 2010 2018 2002 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Rati Verma United States 23 3.8k 1.3k 1.1k 731 373 30 4.0k
Thibault Mayor Canada 24 3.0k 0.8× 1.7k 1.4× 451 0.4× 311 0.4× 469 1.3× 50 3.4k
H Heller Israel 16 3.8k 1.0× 1.1k 0.9× 1.2k 1.1× 611 0.8× 244 0.7× 16 4.3k
Colin Gordon United Kingdom 31 3.2k 0.9× 1.1k 0.9× 805 0.8× 608 0.8× 350 0.9× 53 3.6k
Michael H. Tatham United Kingdom 31 4.5k 1.2× 526 0.4× 1.6k 1.5× 602 0.8× 490 1.3× 53 4.9k
Chunshui Zhou United States 12 2.6k 0.7× 718 0.6× 524 0.5× 306 0.4× 197 0.5× 15 2.9k
Anita Saraf United States 26 2.7k 0.7× 583 0.5× 443 0.4× 262 0.4× 311 0.8× 41 3.4k
Alfred C.O. Vertegaal Netherlands 44 5.5k 1.5× 637 0.5× 1.9k 1.7× 459 0.6× 527 1.4× 98 6.1k
David M. Duda United States 26 3.4k 0.9× 630 0.5× 931 0.9× 1.2k 1.7× 216 0.6× 38 4.0k
Erica S. Johnson United States 26 5.6k 1.5× 1.1k 0.8× 1.7k 1.5× 712 1.0× 625 1.7× 33 5.9k
Ellis Jaffray United Kingdom 39 4.6k 1.2× 502 0.4× 1.6k 1.5× 492 0.7× 576 1.5× 57 5.3k

Countries citing papers authored by Rati Verma

Since Specialization
Citations

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

Fields of papers citing papers by Rati Verma

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Rati Verma. 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 Rati Verma. The network helps show where Rati Verma may publish in the future.

Co-authorship network of co-authors of Rati Verma

This figure shows the co-authorship network connecting the top 25 collaborators of Rati Verma. A scholar is included among the top collaborators of Rati Verma 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 Rati Verma. Rati Verma 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.
Sherman, David J., Lei Liu, Jennifer L. Mamrosh, et al.. (2024). The fatty liver disease–causing protein PNPLA3-I148M alters lipid droplet–Golgi dynamics. Proceedings of the National Academy of Sciences. 121(18). e2318619121–e2318619121. 16 indexed citations
2.
Verma, Rati. (2021). Exploiting Ubiquitin Ligases for Induced Target Degradation as an Antiviral Strategy. Advances in experimental medicine and biology. 1322. 339–357. 5 indexed citations
3.
Verma, Rati, Dane Mohl, & Raymond J. Deshaies. (2020). Harnessing the Power of Proteolysis for Targeted Protein Inactivation. Molecular Cell. 77(3). 446–460. 130 indexed citations
4.
Verma, Rati, Kurt M. Reichermeier, A. Maxwell Burroughs, et al.. (2018). Vms1 and ANKZF1 peptidyl-tRNA hydrolases release nascent chains from stalled ribosomes. Nature. 557(7705). 446–451. 121 indexed citations
5.
Verma, Rati, et al.. (2013). Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome. eLife. 2. e00308–e00308. 203 indexed citations
6.
Besten, Willem den, Rati Verma, Gary Kleiger, Robert Oania, & Raymond J. Deshaies. (2012). NEDD8 links cullin-RING ubiquitin ligase function to the p97 pathway. Nature Structural & Molecular Biology. 19(5). 511–516. 66 indexed citations
7.
Rabut, Gwénaël, Gaëlle Le Dez, Rati Verma, et al.. (2011). The TFIIH Subunit Tfb3 Regulates Cullin Neddylation. Molecular Cell. 43(3). 488–495. 46 indexed citations
8.
Verma, Rati, Robert Oania, Ruihua Fang, Geoffrey T. Smith, & Raymond J. Deshaies. (2011). Cdc48/p97 Mediates UV-Dependent Turnover of RNA Pol II. Molecular Cell. 41(1). 82–92. 170 indexed citations
9.
Goh, Amanda M., Kylie J. Walters, Suzanne Elsasser, et al.. (2008). Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins. BMC Biochemistry. 9(1). 4–4. 22 indexed citations
10.
Haririnia, Aydin, et al.. (2007). Mutations in the Hydrophobic Core of Ubiquitin Differentially Affect Its Recognition by Receptor Proteins. Journal of Molecular Biology. 375(4). 979–996. 39 indexed citations
11.
Verma, Rati, Noël R. Peters, Mariapina D’Onofrio, et al.. (2004). Ubistatins Inhibit Proteasome-Dependent Degradation by Binding the Ubiquitin Chain. Science. 306(5693). 117–120. 154 indexed citations
12.
Verma, Rati, Robert Oania, Johannes Graumann, & Raymond J. Deshaies. (2004). Multiubiquitin Chain Receptors Define a Layer of Substrate Selectivity in the Ubiquitin-Proteasome System. Cell. 118(1). 99–110. 367 indexed citations
13.
Sakamoto, Kathleen M., et al.. (2003). Development of Protacs to Target Cancer-promoting Proteins for Ubiquitination and Degradation. Molecular & Cellular Proteomics. 2(12). 1350–1358. 334 indexed citations
14.
Verma, Rati, L. Aravind, Robert Oania, et al.. (2002). Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26 S Proteasome. Science. 298(5593). 611–615. 810 indexed citations breakdown →
15.
Deshaies, Raymond J., Jae Hong Seol, W. Hayes McDonald, et al.. (2002). Charting the Protein Complexome in Yeast by Mass Spectrometry. Molecular & Cellular Proteomics. 1(1). 3–10. 35 indexed citations
16.
Verma, Rati, W. Hayes McDonald, John R. Yates, & Raymond J. Deshaies. (2001). Selective Degradation of Ubiquitinated Sic1 by Purified 26S Proteasome Yields Active S Phase Cyclin-Cdk. Molecular Cell. 8(2). 439–448. 78 indexed citations
17.
Reynolds, William, et al.. (2000). Cks1 Is Required for G 1 Cyclin–Cyclin-Dependent Kinase Activity in Budding Yeast. Molecular and Cellular Biology. 20(16). 5858–5864. 58 indexed citations
18.
Verma, Rati & Raymond J. Deshaies. (2000). A Proteasome Howdunit. Cell. 101(4). 341–344. 113 indexed citations
19.
Verma, Rati, Yong Chi, & Raymond J. Deshaies. (1997). Cell-free ubiquitination of cell cycle regulators in budding yeast extracts. Methods in enzymology on CD-ROM/Methods in enzymology. 283. 365–376. 19 indexed citations
20.
Verma, Rati, John F. Smiley, Brenda Andrews, & John Campbell. (1992). Regulation of the yeast DNA replication genes through the Mlu I cell cycle box is dependent on SWI6.. Proceedings of the National Academy of Sciences. 89(20). 9479–9483. 40 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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