What is he best known for?
The fields of study he is best known for:
John Kuriyan mainly investigates Biochemistry, Cell biology, Protein structure, Proto-oncogene tyrosine-protein kinase Src and SH3 domain.
His Biochemistry study frequently draws connections between related disciplines such as Biophysics.
John Kuriyan has researched Biophysics in several fields, including Processivity, dnaN, DNA clamp, DNA polymerase delta and Proliferating cell nuclear antigen.
His studies in Cell biology integrate themes in fields like Protein kinase domain and Cell membrane.
His Protein structure research incorporates elements of Peptide, Kinase, Binding site and Stereochemistry.
John Kuriyan has included themes like EVH1 domain, Polyproline helix and Proto-Oncogene Proteins c-abl in his SH3 domain study.
His most cited work include:
- Crystallographic R Factor Refinement by Molecular Dynamics (1779 citations)
- Structural mechanism for STI-571 inhibition of abelson tyrosine kinase (1571 citations)
- 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 (1512 citations)
What are the main themes of his work throughout his whole career to date?
Biochemistry, Cell biology, Biophysics, Protein structure and DNA clamp are his primary areas of study.
His work in Proto-oncogene tyrosine-protein kinase Src, SH3 domain, Tyrosine kinase, SH2 domain and Kinase are all subfields of Biochemistry research.
In his study, ABL and Imatinib is inextricably linked to Protein kinase domain, which falls within the broad field of Cell biology.
His Biophysics study combines topics in areas such as Ca2+/calmodulin-dependent protein kinase, DNA, Guanine nucleotide exchange factor, Calmodulin and Allosteric regulation.
His Protein structure study incorporates themes from Crystallography, Stereochemistry and Binding site.
His DNA clamp research is multidisciplinary, relying on both Processivity, dnaN, DNA polymerase, DNA polymerase delta and Molecular biology.
He most often published in these fields:
- Biochemistry (50.26%)
- Cell biology (47.41%)
- Biophysics (40.67%)
What were the highlights of his more recent work (between 2014-2021)?
- Cell biology (47.41%)
- Biophysics (40.67%)
- Phosphorylation (20.98%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Cell biology, Biophysics, Phosphorylation, Kinase and Tyrosine kinase.
The concepts of his Cell biology study are interwoven with issues in Allosteric regulation, Protein kinase domain and T-cell receptor.
His research investigates the connection between Allosteric regulation and topics such as DNA polymerase that intersect with issues in Mutagenesis and DNA clamp.
John Kuriyan interconnects Kinetic proofreading, Ca2+/calmodulin-dependent protein kinase, DNA, Enzyme and Membrane in the investigation of issues within Biophysics.
His Kinase research is multidisciplinary, incorporating elements of Chemical biology and Active site.
His research on Tyrosine kinase concerns the broader Biochemistry.
Between 2014 and 2021, his most popular works were:
- A Structural Perspective on the Regulation of the Epidermal Growth Factor Receptor (159 citations)
- Molecular basis for multimerization in the activation of the epidermal growth factor receptor (85 citations)
- A molecular assembly phase transition and kinetic proofreading modulate Ras activation by SOS. (84 citations)
In his most recent research, the most cited papers focused on:
John Kuriyan mainly investigates Cell biology, Phosphorylation, Kinase, Biochemistry and Biophysics.
His study in SH2 domain and Tyrosine kinase is done as part of Cell biology.
His study in Phosphorylation is interdisciplinary in nature, drawing from both Transferase and Protein kinase domain.
As a member of one scientific family, he mostly works in the field of Kinase, focusing on Active site and, on occasion, Cell culture, Chemical biology and Peptide.
His is doing research in Receptor tyrosine kinase and ERBB3, both of which are found in Biochemistry.
His research in Biophysics intersects with topics in Guanine nucleotide exchange factor, Structural biology, Kinetic proofreading and Protein structure.
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