An orthosteric inhibitor of the Ras-Sos interaction. Academic Article

abstract

• Mimics of -helices on protein surfaces have emerged as powerful reagents for antagonizing protein-protein interactions, which are difficult to target with small molecules. Here we describe the design of a cell-permeable synthetic -helix, based on the guanine nucleotide exchange factor Sos, that interferes with Ras-Sos interaction and downregulates Ras signaling in response to receptor tyrosine kinase activation.

authors

• Yadav, Kamlesh

published proceedings

• Nat Chem Biol

altmetric score

• 13.85

author list (cited authors)

• Patgiri, A., Yadav, K. K., Arora, P. S., & Bar-Sagi, D.

citation count

• 251

complete list of authors

• Patgiri, Anupam||Yadav, Kamlesh K||Arora, Paramjit S||Bar-Sagi, Dafna

publication date

• January 2011

publisher

• Springer Nature  Publisher

published in

• Nature Chemical Biology  Journal

keywords

• Amino Acid Sequence
• Biomimetic Materials
• Biomimetics
• Cell Line
• Down-Regulation
• Drug Design
• Humans
• Molecular Sequence Data
• Oligopeptides
• Protein Interaction Domains And Motifs
• Protein Structure, Secondary
• Protein-Tyrosine Kinases
• Ras Guanine Nucleotide Exchange Factors
• Signal Transduction
• Son Of Sevenless Protein, Drosophila

Digital Object Identifier (DOI)

• 10.1038/nchembio.612

start page

• 585

end page

• 587

volume

• 7

issue

• 9

URL

• http://dx.doi.org/10.1038/nchembio.612