Igor Kurinov

3.7k total citations
71 papers, 2.5k citations indexed

About

Igor Kurinov is a scholar working on Molecular Biology, Cell Biology and Oncology. According to data from OpenAlex, Igor Kurinov has authored 71 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Molecular Biology, 16 papers in Cell Biology and 12 papers in Oncology. Recurrent topics in Igor Kurinov's work include Protein Structure and Dynamics (14 papers), Ubiquitin and proteasome pathways (14 papers) and Enzyme Structure and Function (12 papers). Igor Kurinov is often cited by papers focused on Protein Structure and Dynamics (14 papers), Ubiquitin and proteasome pathways (14 papers) and Enzyme Structure and Function (12 papers). Igor Kurinov collaborates with scholars based in United States, Canada and Russia. Igor Kurinov's co-authors include Robert W. Harrison, Frank Sicheri, Brenda A. Schulman, Fatih M. Uckun, Amanda Nourse, David M. Duda, Ki Hyun Nam, Ailong Ke, Jennifer L. Olszewski and Darcie J. Miller and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Igor Kurinov

71 papers receiving 2.4k citations

Peers

Igor Kurinov

ONCOL

EPIDE

IMMUN

Ramón Campos‐Olivas Spain

Jean‐Michel Wieruszeski France

Abdellah Allali‐Hassani Canada

F. Niesen United Kingdom

W. Tempel Canada

Takayoshi Okabe Japan

Marina Ignatushchenko United States

Chaohong Sun United States

Danielle L. Swaney United States

Naixia Zhang China

Ramón Campos‐Olivas Spain

Igor Kurinov

2.0k ×1.1

435 ×1.1

ONCOL

181 ×0.5

384 ×1.1

EPIDE

321 ×1.5

IMMUN

Citations per year, relative to Igor Kurinov Igor Kurinov (= 1×) peers Ramón Campos‐Olivas

Countries citing papers authored by Igor Kurinov

Since Specialization

Citations

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

Fields of papers citing papers by Igor Kurinov

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Igor Kurinov

This figure shows the co-authorship network connecting the top 25 collaborators of Igor Kurinov. A scholar is included among the top collaborators of Igor Kurinov 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 Igor Kurinov. Igor Kurinov 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

Tessier, Tanner M., Joan Teyra, Nick Jarvik, et al.. (2023). Structural and functional validation of a highly specific Smurf2 inhibitor. Protein Science. 33(2). e4885–e4885. 1 indexed citations

Dalton, Kevin M., et al.. (2022). Native SAD phasing at room temperature. Acta Crystallographica Section D Structural Biology. 78(8). 986–996. 7 indexed citations

Kurinov, Igor, et al.. (2022). Crystal structure of the CDK11 kinase domain bound to the small-molecule inhibitor OTS964. Structure. 30(12). 1615–1625.e4. 9 indexed citations

McAlear, Thomas S., Nathalie Croteau, Simon Veyron, et al.. (2021). Crystal structure of human PACRG in complex with MEIG1 reveals roles in axoneme formation and tubulin binding. Structure. 29(6). 572–586.e6. 15 indexed citations

Pourfarjam, Yasin, et al.. (2021). Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. Journal of Biological Chemistry. 296. 100692–100692. 1 indexed citations

Orlicky, Stephen, Jonah Beenstock, Derek F. Ceccarelli, et al.. (2021). Bipartite binding of the N terminus of Skp2 to cyclin A. Structure. 29(9). 975–988.e5. 7 indexed citations

Ceccarelli, Derek F., Étienne Coyaud, Pierre Maisonneuve, et al.. (2019). FAM105A/OTULINL Is a Pseudodeubiquitinase of the OTU-Class that Localizes to the ER Membrane. Structure. 27(6). 1000–1012.e6. 9 indexed citations

Pourfarjam, Yasin, et al.. (2018). Structure of human ADP-ribosyl-acceptor hydrolase 3 bound to ADP-ribose reveals a conformational switch that enables specific substrate recognition. Journal of Biological Chemistry. 293(32). 12350–12359. 28 indexed citations

Lavoie, Hugo, Malha Sahmi, Pierre Maisonneuve, et al.. (2018). MEK drives BRAF activation through allosteric control of KSR proteins. Nature. 554(7693). 549–553. 99 indexed citations

10.

Maisonneuve, Pierre, Xu Liu, G. K. Surya Prakash, et al.. (2018). Effects of rigidity on the selectivity of protein kinase inhibitors. European Journal of Medicinal Chemistry. 146. 519–528. 11 indexed citations

11.

Yang, Ge, Yang Fu, Margarita Malakhova, et al.. (2014). Caffeic Acid Directly Targets ERK1/2 to Attenuate Solar UV-Induced Skin Carcinogenesis. Cancer Prevention Research. 7(10). 1056–1066. 47 indexed citations

12.

Brown, Nicholas G., Edmond R. Watson, Florian Weissmann, et al.. (2014). Mechanism of Polyubiquitination by Human Anaphase-Promoting Complex: RING Repurposing for Ubiquitin Chain Assembly. Molecular Cell. 56(2). 246–260. 92 indexed citations

13.

Wan, Leo C. K., Daniel Y.L. Mao, Dante Neculai, et al.. (2013). Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system. Nucleic Acids Research. 41(12). 6332–6346. 61 indexed citations

14.

Taherbhoy, Asad M., Stephen W. G. Tait, Stephen E. Kaiser, et al.. (2011). Atg8 Transfer from Atg7 to Atg3: A Distinctive E1-E2 Architecture and Mechanism in the Autophagy Pathway. Molecular Cell. 44(3). 451–461. 134 indexed citations

15.

Malakhova, Margarita, et al.. (2010). The Crystal Structure of the Active Form of the C-Terminal Kinase Domain of Mitogen- and Stress-Activated Protein Kinase 1. Journal of Molecular Biology. 399(1). 41–52. 7 indexed citations

16.

Mao, Daniel Y.L., Dante Neculai, Michael Downey, et al.. (2008). Atomic Structure of the KEOPS Complex: An Ancient Protein Kinase-Containing Molecular Machine. Molecular Cell. 32(2). 259–275. 78 indexed citations

17.

Rajamohan, Francis, Igor Kurinov, T.K. Venkatachalam, & Fatih M. Uckun. (1999). Deguanylation of Human Immunodeficiency Virus (HIV-1) RNA by Recombinant Pokeweed Antiviral Protein. Biochemical and Biophysical Research Communications. 263(2). 419–424. 32 indexed citations

18.

Kurinov, Igor, Damian E. Myers, Fatih M. Uckun, & J D Irvin. (1999). X‐ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA substrate analogs. Protein Science. 8(9). 1765–1772. 42 indexed citations

19.

Kurinov, Igor, Francis Rajamohan, T.K. Venkatachalam, & Fatih M. Uckun. (1999). X‐ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA. Protein Science. 8(11). 2399–2405. 19 indexed citations

20.

Ridky, Todd W., Alexandra Kikonyogo, Jonathan Leis, et al.. (1998). Drug-Resistant HIV-1 Proteases Identify Enzyme Residues Important for Substrate Selection and Catalytic Rate. Biochemistry. 37(39). 13835–13845. 46 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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