Associated Papers
Phosphatase SHP2 pathogenic mutations enhance activity by altering conformational sampling.
Glaser AW et al.
Biorxiv : the Preprint Server for Biology, 2025
Deep mutational scanning of a multi-domain signaling protein reveals mechanisms of regulation and pathogenicity.
Jiang Z et al.
Biorxiv : the Preprint Server for Biology, 2024
39091798 (PubMed )
Supplement: media-3.xlsx › SHP2-FL_cSrc-KD_column
An allosteric interaction controls the activation mechanism of SHP2 tyrosine phosphatase.
Anselmi M et al.
Scientific Reports, 2020
Understanding the Mechanism of Recognition of Gab2 by the N-SH2 Domain of SHP2.
Visconti L et al.
Life (basel, Switzerland), 2020
Unveiling the Molecular Basis of the Noonan Syndrome-Causing Mutation T42A of SHP2.
Toto A et al.
International Journal of Molecular Sciences, 2020
Structural characterization of an on-pathway intermediate and transition state in the folding of the N-terminal SH2 domain from SHP2.
Visconti L et al.
The Febs Journal, 2019
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