2011 - Fellow of the Royal Society of Canada Academy of Science
His primary areas of investigation include Biochemistry, Cell biology, Phosphorylation, Ubiquitin ligase and Ubiquitin. Kinase, SH2 domain, Receptor tyrosine kinase, Proto-oncogene tyrosine-protein kinase Src and SH3 domain are subfields of Biochemistry in which his conducts study. His biological study spans a wide range of topics, including RNA and Protein biosynthesis.
His Cell biology research incorporates themes from Protein structure and Protein kinase domain. His Ubiquitin ligase research is multidisciplinary, incorporating elements of DNA ligase and Sic1. His study focuses on the intersection of Ubiquitin and fields such as Enzyme with connections in the field of Mutagenesis, Receptor complex and Ubiquitin ligase activity.
Frank Sicheri mainly focuses on Cell biology, Biochemistry, Ubiquitin, Kinase and Ubiquitin ligase. His work in Cell biology covers topics such as Protein kinase domain which are related to areas like Kinase activity and Receptor tyrosine kinase. His research on Biochemistry often connects related areas such as Biophysics.
He has included themes like DNA ligase and Enzyme in his Ubiquitin study. Frank Sicheri interconnects Cyclin-dependent kinase and Allosteric regulation in the investigation of issues within Ubiquitin ligase. His Cell division control protein 4 research includes themes of Sic1 and F-box protein.
Frank Sicheri spends much of his time researching Cell biology, Ubiquitin, Kinase, Deubiquitinating enzyme and Plasma protein binding. His work focuses on many connections between Cell biology and other disciplines, such as Binding site, that overlap with his field of interest in Enzyme kinetics. His work deals with themes such as Active site, Enzyme, Phage display and Function, which intersect with Ubiquitin.
His Phage display study introduces a deeper knowledge of Biochemistry. His Kinase research is multidisciplinary, incorporating perspectives in Cancer research, Signal transduction, Protein kinase domain and Effector. The various areas that he examines in his Plasma protein binding study include Catalytic cycle, Gene, Archaea and Transfer RNA, TRNA modification.
His primary scientific interests are in Kinase, Cell biology, Antibody response, Immunology and Antibody. His Kinase study incorporates themes from Cell culture, Cancer research and Signal transduction. His Signal transduction research incorporates elements of Plasma protein binding, Cell growth, V600E, Mutant and Regulation of gene expression.
Frank Sicheri combines subjects such as Ubiquitin, Protein kinase domain and Pyrazolopyrimidine, Pyrimidine with his study of Cell biology. The Ubiquitin study combines topics in areas such as Function, Phosphorylation and Active site. His research investigates the connection between Immunology and topics such as Enzyme that intersect with problems in Ubiquitin-conjugating enzyme, NEDD8, Chemical biology and F-box protein.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Crystal structure of the Src family tyrosine kinase Hck
Frank Sicheri;Ismail Moarefi;Ismail Moarefi;John Kuriyan;John Kuriyan.
Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
Piers Nash;Xiaojing Tang;Stephen Orlicky;Qinghua Chen.
Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
I Moarefi;M LaFevre-Bernt;F Sicheri;M Huse.
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Amélie Fradet-Turcotte;Marella D. Canny;Cristina Escribano-Díaz;Alexandre Orthwein.
Bone recognition mechanism of porcine osteocalcin from crystal structure.
Quyen Q. Hoang;Frank Sicheri;Frank Sicheri;Andrew J. Howard;Daniel S. C. Yang.
Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase
Stephen Orlicky;Xiaojing Tang;Andrew Willems;Mike Tyers;Mike Tyers.
Crystal Structure of Hck in Complex with a Src Family–Selective Tyrosine Kinase Inhibitor
Thomas Schindler;Frank Sicheri;Alexander Pico;Aviv Gazit.
Molecular Cell (1999)
Structures of Src-family tyrosine kinases.
Frank Sicheri;John Kuriyan.
Current Opinion in Structural Biology (1997)
Ice-binding structure and mechanism of an antifreeze protein from winter flounder
F. Sicheri;D. S. C. Yang;D. S. C. Yang.
A dimerization-dependent mechanism drives RAF catalytic activation
Thanashan Rajakulendran;Malha Sahmi;Martin Lefrançois;Frank Sicheri.
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: