John Kuriyan

51.1k total citations · 20 hit papers
235 papers, 38.8k citations indexed

About

John Kuriyan is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, John Kuriyan has authored 235 papers receiving a total of 38.8k indexed citations (citations by other indexed papers that have themselves been cited), including 187 papers in Molecular Biology, 41 papers in Materials Chemistry and 39 papers in Oncology. Recurrent topics in John Kuriyan's work include Protein Kinase Regulation and GTPase Signaling (52 papers), Protein Structure and Dynamics (39 papers) and Enzyme Structure and Function (39 papers). John Kuriyan is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (52 papers), Protein Structure and Dynamics (39 papers) and Enzyme Structure and Function (39 papers). John Kuriyan collaborates with scholars based in United States, Germany and Singapore. John Kuriyan's co-authors include Martin Karplus, Mike O’Donnell, Morgan Huse, Frank Sicheri, Axel T. Brünger, Ismail Moarefi, Patricia Pellicena, Thomas H. Schindler, William G. Bornmann and Dafna Bar‐Sagi and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

John Kuriyan

233 papers receiving 38.0k citations

Hit Papers

Crystallographic R Factor... 1986 2026 1999 2012 1987 2000 2002 2006 1997 500 1000 1.5k
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.

  1. Crystallographic R Factor Refinement by Molecular Dynamics
    1987 1.8k citations Axel T. Brünger, John Kuriyan et al. Science profile →
  2. Structural Mechanism for STI-571 Inhibition of Abelson Tyrosine Kinase
    2000 1.4k citations Patricia Pellicena, John Kuriyan et al. Science profile →
  3. The Conformational Plasticity of Protein Kinases
    2002 1.3k citations John Kuriyan et al. profile →
  4. An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor
    2006 1.2k citations Jodi Gureasko, John Kuriyan et al. profile →
  5. Crystal structure of the Src family tyrosine kinase Hck
    1997 988 citations John Kuriyan et al. profile →
  6. Molecular dynamics and protein function
    2005 861 citations John Kuriyan et al. Proceedings of the National Academy of Sciences profile →
  7. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    1994 765 citations John Kuriyan et al. profile →
  8. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).
    2002 731 citations Bhushan Nagar, Patricia Pellicena et al. profile →
  9. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    1995 715 citations John Kuriyan et al. profile →
  10. Crystallographic Analysis of the Recognition of a Nuclear Localization Signal by the Nuclear Import Factor Karyopherin α
    1998 674 citations John Kuriyan et al. profile →
  11. Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA
    1996 668 citations Mike O’Donnell, John Kuriyan et al. profile →
  12. Structural Basis for the Autoinhibition of c-Abl Tyrosine Kinase
    2003 654 citations Bhushan Nagar, John Kuriyan et al. profile →
  13. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    1992 651 citations Mike O’Donnell, John Kuriyan et al. profile →
  14. The structural basis of the activation of Ras by Sos
    1998 649 citations Dafna Bar‐Sagi, John Kuriyan et al. profile →
  15. Crystal Structure of a Tyrosine Phosphorylated STAT-1 Dimer Bound to DNA
    1998 571 citations Yanxiang Zhao, John Kuriyan et al. profile →
  16. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    1992 551 citations Dorothea Kominos, John Kuriyan et al. profile →
  17. Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia
    2012 542 citations Qi Wang, John Kuriyan et al. profile →
  18. Activation of the Sire-family tyrosine kinase Hck by SH3 domain displacement
    1997 530 citations John Kuriyan et al. profile →
  19. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution
    1986 460 citations John Kuriyan et al. profile →
  20. Oncogenic Mutations Counteract Intrinsic Disorder in the EGFR Kinase and Promote Receptor Dimerization
    2012 276 citations Yibing Shan, Michael P. Eastwood et al. profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
John Kuriyan 28.8k 7.0k 4.9k 4.5k 3.9k 235 38.8k
Robert Huber 46.8k 1.6× 9.2k 1.3× 6.8k 1.4× 11.3k 2.5× 5.6k 1.4× 600 66.7k
Piet Gros 19.8k 0.7× 7.7k 1.1× 2.2k 0.5× 4.5k 1.0× 2.3k 0.6× 251 34.7k
Tony Pawson 49.8k 1.7× 10.9k 1.6× 13.1k 2.7× 2.1k 0.5× 3.2k 0.8× 447 68.5k
Wolfram Bode 15.0k 0.5× 5.5k 0.8× 2.2k 0.4× 2.3k 0.5× 7.1k 1.8× 282 28.0k
Frank McCormick 42.8k 1.5× 14.4k 2.0× 9.3k 1.9× 1.5k 0.3× 2.5k 0.6× 381 57.5k
Albert J. R. Heck 33.6k 1.2× 4.8k 0.7× 4.7k 1.0× 2.6k 0.6× 855 0.2× 815 50.5k
Matthew G. Vander Heiden 37.2k 1.3× 7.3k 1.0× 2.8k 0.6× 1.0k 0.2× 1.4k 0.4× 225 54.5k
Stefan Knapp 21.6k 0.8× 5.6k 0.8× 2.3k 0.5× 1.8k 0.4× 3.9k 1.0× 516 29.0k
Stephen W. Fesik 24.8k 0.9× 5.3k 0.8× 2.2k 0.4× 2.5k 0.6× 1.0k 0.3× 267 31.1k
Airlie J. McCoy 43.0k 1.5× 4.9k 0.7× 6.2k 1.3× 12.2k 2.7× 899 0.2× 96 60.1k

Countries citing papers authored by John Kuriyan

Since Specialization
Citations

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

Fields of papers citing papers by John Kuriyan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of John Kuriyan

This figure shows the co-authorship network connecting the top 25 collaborators of John Kuriyan. A scholar is included among the top collaborators of John Kuriyan 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 John Kuriyan. John Kuriyan 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.
Huang, Yongjian, Subu Subramanian, Christine L. Gee, et al.. (2024). Autoinhibition of a clamp-loader ATPase revealed by deep mutagenesis and cryo-EM. Nature Structural & Molecular Biology. 31(3). 424–435. 1 indexed citations
2.
Yang, Kailu, Chuchu Wang, Alex J.B. Kreutzberger, et al.. (2022). Nanomolar inhibition of SARS-CoV-2 infection by an unmodified peptide targeting the prehairpin intermediate of the spike protein. Proceedings of the National Academy of Sciences. 119(40). e2210990119–e2210990119. 27 indexed citations
3.
Huang, William Y. C., Steven Alvarez, Yasushi Kondo, John Kuriyan, & Jay T. Groves. (2021). Relating cellular signaling timescales to single-molecule kinetics: A first-passage time analysis of Ras activation by SOS. Proceedings of the National Academy of Sciences. 118(45). 12 indexed citations
4.
Cofsky, Joshua C., et al.. (2020). CRISPR-Cas12a exploits R-loop asymmetry to form double-strand breaks. eLife. 9. 79 indexed citations
5.
Chung, Jean K., Laura M. Nocka, Qi Wang, et al.. (2019). Switch-like activation of Bruton’s tyrosine kinase by membrane-mediated dimerization. Proceedings of the National Academy of Sciences. 116(22). 10798–10803. 37 indexed citations
6.
Huang, William Y. C., Steven Alvarez, Yasushi Kondo, et al.. (2019). A molecular assembly phase transition and kinetic proofreading modulate Ras activation by SOS. Science. 363(6431). 1098–1103. 255 indexed citations
7.
Kondo, Yasushi, Jana Ognjenović, Saikat Banerjee, et al.. (2019). Cryo-EM structure of a dimeric B-Raf:14-3-3 complex reveals asymmetry in the active sites of B-Raf kinases. Science. 366(6461). 109–115. 118 indexed citations
8.
Cantor, Aaron J., Neel H. Shah, & John Kuriyan. (2018). Deep mutational analysis reveals functional trade-offs in the sequences of EGFR autophosphorylation sites. Proceedings of the National Academy of Sciences. 115(31). E7303–E7312. 29 indexed citations
9.
Vercoulen, Yvonne, Yasushi Kondo, Jeffrey S. Iwig, et al.. (2017). A Histidine pH sensor regulates activation of the Ras-specific guanine nucleotide exchange factor RasGRP1. eLife. 6. 29 indexed citations
10.
Bandaru, Pradeep, Neel H. Shah, Moitrayee Bhattacharyya, et al.. (2017). Deconstruction of the Ras switching cycle through saturation mutagenesis. eLife. 6. 70 indexed citations
11.
Chan, Alice, Divya Punwani, Theresa A. Kadlecek, et al.. (2016). A novel human autoimmune syndrome caused by combined hypomorphic and activating mutations in ZAP-70. The Journal of Experimental Medicine. 213(2). 155–165. 54 indexed citations
12.
Herzik, Mark A., et al.. (2014). Structural insights into the role of iron–histidine bond cleavage in nitric oxide-induced activation of H-NOX gas sensor proteins. Proceedings of the National Academy of Sciences. 111(40). E4156–64. 81 indexed citations
13.
Iversen, Lars, Hsiung‐Lin Tu, Wan‐Chen Lin, et al.. (2014). Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics. Science. 345(6192). 50–54. 110 indexed citations
14.
Seeliger, Markus A., Pratistha Ranjitkar, Corynn Kasap, et al.. (2009). Equally Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase Conformations. Cancer Research. 69(6). 2384–2392. 127 indexed citations
15.
Shan, Yibing, Markus A. Seeliger, Michael P. Eastwood, et al.. (2008). A conserved protonation-dependent switch controls drug binding in the Abl kinase. Proceedings of the National Academy of Sciences. 106(1). 139–144. 216 indexed citations
16.
Freedman, Tanya S., Holger Sondermann, Gregory D. Friedland, et al.. (2006). A Ras-induced conformational switch in the Ras activator Son of sevenless. Proceedings of the National Academy of Sciences. 103(45). 16692–16697. 116 indexed citations
17.
Sondermann, Holger, Bhushan Nagar, Dafna Bar‐Sagi, & John Kuriyan. (2005). Computational docking and solution x-ray scattering predict a membrane-interacting role for the histone domain of the Ras activator son of sevenless. Proceedings of the National Academy of Sciences. 102(46). 16632–16637. 52 indexed citations
18.
Kazmirski, Steven L., Yanxiang Zhao, Gregory D. Bowman, Mike O’Donnell, & John Kuriyan. (2005). Out-of-plane motions in open sliding clamps: Molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen. Proceedings of the National Academy of Sciences. 102(39). 13801–13806. 54 indexed citations
19.
Pellicena, Patricia, David S. Karow, Elizabeth M. Boon, Michael A. Marletta, & John Kuriyan. (2004). Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. Proceedings of the National Academy of Sciences. 101(35). 12854–12859. 216 indexed citations
20.
Waksman, Gilles, et al.. (1993). CRYSTAL-STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN (SH2) OF THE V-SRC TYROSINE KINASE COMPLEXED WITH TYROSINE PHOSPHORYLATED PEPTIDES. UCL Discovery (University College London). 9 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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