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Molecular Biology

D-Index
119
Citations
64096
World Ranking
264
National Ranking
154

Research.com Recognitions

  • 2018 - Member of the National Academy of Medicine (NAM)
  • 2015 - Fellow of the Royal Society, United Kingdom
  • 2008 - Fellow of the American Academy of Arts and Sciences
  • 2005 - Richard Lounsbery Award, National Academy of Sciences and the French Academy of Sciences for his critical role in revealing the structural mechanisms underlying processivity in DNA replication and the regulation of tyrosine kinases and their interacting target proteins.
  • 2001 - Member of the National Academy of Sciences

Overview

John Kuriyan is affiliated with Vanderbilt University in the United States. Their research primarily spans the fields of biochemistry, genetics, and molecular biology, with a significant focus on molecular biology and genetics. The scientist's work also extends into subfields such as immunology, radiology, nuclear medicine and imaging, and materials chemistry.

The main topics of their research include:

  • Protein kinase regulation and GTPase signaling
  • Monoclonal and polyclonal antibodies research
  • Chronic lymphocytic leukemia research
  • Protein structure and dynamics
  • Enzyme structure and function
  • RNA and protein synthesis mechanisms
  • Ubiquitin and proteasome pathways

John Kuriyan has published extensively in several academic venues. The most frequent publication venues include:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • eLife
  • Proceedings of the National Academy of Sciences
  • Protein Science
  • Science Signaling

Some recent papers authored or co-authored by Kuriyan are:

  • "Structural basis and regulation of the reductive stress response," 2021, published in Cell
  • "CRISPR-Cas12a exploits R-loop asymmetry to form double-strand breaks," 2020, published in eLife
  • "A two-component protein condensate of the EGFR cytoplasmic tail and Grb2 regulates Ras activation by SOS at the membrane," 2022, published in Proceedings of the National Academy of Sciences
  • "Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation," 2020, published in eLife
  • "Structural basis for dimerization quality control," 2020, published in Nature

Frequent co-authors collaborating with Kuriyan include:

  • Jay T. Groves
  • Christine L. Gee
  • Serena Muratcioğlu
  • Timothy J. Eisen
  • Subu Subramanian

Throughout their career, John Kuriyan has received several recognitions and awards, including:

  • Member of the National Academy of Medicine (2018)
  • Fellow of the Royal Society, United Kingdom (2015)
  • Fellow of the American Academy of Arts and Sciences (2008)
  • Richard Lounsbery Award from the National Academy of Sciences and the French Academy of Sciences (2005) for revealing structural mechanisms underlying DNA replication processivity and regulation of tyrosine kinases and their interacting target proteins
  • Member of the National Academy of Sciences (2001)

Best Publications

  • Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

    Thomas Schindler;William Bornmann;Patricia Pellicena;W. Todd Miller

  • The Conformational Plasticity of Protein Kinases

    Morgan Huse;John Kuriyan;John Kuriyan

  • Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia

    Neil P. Shah;John M. Nicoll;Bhushan Nagar;Mercedes E. Gorre

  • An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor

    Xuewu Zhang;Jodi Gureasko;Kui Shen;Philip A. Cole

  • Crystal structure of the Src family tyrosine kinase Hck

    Frank Sicheri;Ismail Moarefi;Ismail Moarefi;John Kuriyan;John Kuriyan

  • Molecular dynamics and protein function

    M. Karplus;J. Kuriyan

  • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)

    Bhushan Nagar;William G. Bornmann;Patricia Pellicena;Thomas Schindler

  • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA

    Talluru S.R. Krishna;Xiang-Peng Kong;Sonja Gary;Peter M. Burgers

  • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.

    Jonathan Goldberg;Hsien Bin Huang;Young Guen Kwon;Paul Greengard

  • Structural basis for the autoinhibition of c-Abl tyrosine kinase

    Bhushan Nagar;Oliver Hantschel;Matthew A. Young;Klaus Scheffzek

  • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.

    Elena Conti;Marc Uy;Marc Uy;Lore Leighton;Lore Leighton;Günter Blobel;Günter Blobel

  • The structural basis of the activation of Ras by Sos

    P.A Boriack-Sjodin;S.M Margarit;D Bar-Sagi;J. Kuriyan

  • Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free forms

    Gabriel Waksman;Steven E. Shoelson;Nalin Pant;David Cowburn

  • Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA

    Jacqueline M Gulbis;Zvi Kelman;Jerard Hurwitz;Mike O'Donnell;Mike O'Donnell

  • Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp

    Xiang-Peng Kong;Rene Onrust;Mike O'Donnell;John Kuriyan;John Kuriyan

  • Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.

    Xiaomin Chen;Uwe Vinkemeier;Yanxiang Zhao;David Jeruzalmi

  • CRYSTAL-STRUCTURE OF THE PHOSPHOTYROSINE RECOGNITION DOMAIN SH2 OF V-SRC COMPLEXED WITH TYROSINE-PHOSPHORYLATED PEPTIDES

    Gabriel Waksman;Dorothea Kominos;Scott C. Robertson;Scott C. Robertson;Nalin Pant

  • Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia

    Catherine C. Smith;Qi Wang;Chen Shan Chin;Sara Salerno

  • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement

    I Moarefi;M LaFevre-Bernt;F Sicheri;M Huse

  • Modular peptide recognition domains in eukaryotic signaling.

    John Kuriyan;David Cowburn

Frequent Co-Authors

Mike O'Donnell
Mike O'Donnell Rockefeller University
Jay T. Groves
Jay T. Groves University of California, Berkeley
David E. Wemmer
David E. Wemmer University of California, Berkeley
Arthur Weiss
Arthur Weiss University of California, San Francisco
Holger Sondermann
Holger Sondermann Kiel University
Howard Schulman
Howard Schulman Stanford University
Dafna Bar-Sagi
Dafna Bar-Sagi New York University
Evan R. Williams
Evan R. Williams University of California, Berkeley
Martin Karplus
Martin Karplus Harvard University
David E. Shaw
David E. Shaw D. E. Shaw Research

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