Brian Schaffhausen focuses on Phosphorylation, Molecular biology, Biochemistry, Cell biology and Signal transduction. His research on Phosphorylation frequently links to adjacent areas such as Kinase. His Molecular biology study combines topics in areas such as Retinoblastoma protein, Nuclear protein, Transcription factor and Kinase activity.
His Kinase activity research includes elements of Tyrosine kinase and Phosphoprotein. His SH2 domain study deals with the bigger picture of Proto-oncogene tyrosine-protein kinase Src. His Peptide sequence study combines topics from a wide range of disciplines, such as Phosphopeptide, Phosphotyrosine-binding domain, Phosphotyrosine binding and Adapter molecule crk.
His main research concerns Molecular biology, Phosphorylation, Mutant, Antigen and Cell biology. His biological study spans a wide range of topics, including Cell culture, DNA, Kinase activity, Wild type and Gene. The Phosphorylation study combines topics in areas such as Tyrosine and Kinase.
In general Cell biology study, his work on Signal transduction, Protein kinase B and Cell signaling often relates to the realm of Platelet-derived growth factor receptor, thereby connecting several areas of interest. His Tyrosine phosphorylation research is multidisciplinary, relying on both Proto-oncogene tyrosine-protein kinase Src and Blot. His research in the fields of SH2 domain and Phosphoinositide 3-kinase overlaps with other disciplines such as IRS2.
Brian Schaffhausen mainly investigates Cell biology, Protein phosphatase 2, Cancer research, Molecular biology and Murine polyomavirus. His Protein kinase B, PI3K/AKT/mTOR pathway, Signal transduction and Cell signaling study in the realm of Cell biology interacts with subjects such as Spindle checkpoint. His PI3K/AKT/mTOR pathway research is multidisciplinary, incorporating perspectives in Phosphatidylinositol and Kinase.
His Protein phosphatase 2 study is concerned with Phosphorylation in general. His Molecular biology research incorporates elements of Cell culture and RAD51, Nucleotide excision repair, DNA repair, DNA mismatch repair. The various areas that Brian Schaffhausen examines in his Virology study include Bovine papillomavirus, SV40 large T antigen, Proto-oncogene tyrosine-protein kinase Src and Tyrosine phosphorylation.
His primary areas of investigation include Cell biology, Cancer research, Signal transduction, Protein kinase B and Phosphorylation. His Cancer research research is multidisciplinary, incorporating elements of Retinoblastoma protein and Senescence, Cell aging. His work deals with themes such as Endothelial stem cell, Cell migration and Protein kinase A, which intersect with Protein kinase B.
Phosphorylation is closely attributed to Viral transformation in his research. He has included themes like Transformation, Cell signaling and Proto-oncogene tyrosine-protein kinase Src in his Viral transformation study. Brian Schaffhausen interconnects Small Molecule Libraries, Small molecule, Phosphatidylinositol, Kinase and Programmed cell death in the investigation of issues within Proto-Oncogene Proteins c-akt.
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SH2 domains recognize specific phosphopeptide sequences
Songyang Zhou;Songyang Zhou;Steven E. Shoelson;Manas Chaudhuri;Gerald Gish.
Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation.
Malcolm Whitman;David R. Kaplan;Brian Schaffhausen;Lewis Cantley.
Regulation of protein kinase C ζ by PI 3-kinase and PDK-1
Margaret M. Chou;Weimin Hou;Joanne Johnson;Lauren K. Graham.
Current Biology (1998)
Purification and characterization of phosphoinositide 3-kinase from rat liver.
C L Carpenter;B C Duckworth;K R Auger;B Cohen.
Journal of Biological Chemistry (1990)
Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity
David R. Kaplan;Malcolm Whitman;Brian Schaffhausen;David C. Pallas.
IRS-1 activates phosphatidylinositol 3'-kinase by associating with src homology 2 domains of p85
Martin G. Myers;Jonathan M. Backer;Xiao Jian Sun;Steven Shoelson.
Proceedings of the National Academy of Sciences of the United States of America (1992)
Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85-kDa subunit.
C. L. Carpenter;K. R. Auger;Manas Chanudhuri;M. Yoakim.
Journal of Biological Chemistry (1993)
A tightly associated serine/threonine protein kinase regulates phosphoinositide 3-kinase activity.
C. L. Carpenter;K. R. Auger;B. C. Duckworth;Wei-Min Hou.
Molecular and Cellular Biology (1993)
DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication.
K S Campbell;K P Mullane;I A Aksoy;H Stubdal.
Genes & Development (1997)
Phosphatidylinositol metabolism and polyoma-mediated transformation.
David R. Kaplan;Malcolm Whitman;Brian Schaffhausen;Leda Raptis.
Proceedings of the National Academy of Sciences of the United States of America (1986)
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