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Min Zhang

Researcher at University of Utah

Publications -  16
Citations -  416

Min Zhang is an academic researcher from University of Utah. The author has contributed to research in topics: Protein–protein interaction & Wnt signaling pathway. The author has an hindex of 9, co-authored 16 publications receiving 292 citations. Previous affiliations of Min Zhang include Moffitt Cancer Center.

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Rational design of selective small-molecule inhibitors for β-catenin/B-cell lymphoma 9 protein-protein interactions.

TL;DR: A series of small-molecule inhibitors selective for β-catenin/B-cell lymphoma 9 (BCL9) over β-catsin/cadherin PPIs was designed and synthesized, and the binding mode of new inhibitors was characterized by site-directed mutagenesis and structure-activity relationship studies.
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Inhibition of β-catenin/B cell lymphoma 9 protein−protein interaction using α-helix–mimicking sulfono-γ-AApeptide inhibitors

TL;DR: A series of unprecedented helical sulfono-γ-AApeptides that mimic the binding mode of the α-helical HD2 domain of B Cell Lymphoma 9 (BCL9) and disrupt cancer-related β-catenin/ BCL9 protein–protein interaction in cells with excellent potency and specificity are designed.
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Discovery of Selective Small-Molecule Inhibitors for the β-Catenin/T-Cell Factor Protein-Protein Interaction through the Optimization of the Acyl Hydrazone Moiety.

TL;DR: A new small-molecule inhibitor for the β-catenin/Tcf protein-protein interaction (PPI) was identified through AlphaScreen and FP assays and contains an acyl hydrazone group and exhibits higher inhibitory activities in cell-based assays than biochemical assays.
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Targeting the Tcf4 G13ANDE17 binding site to selectively disrupt β-catenin/T-cell factor protein-protein interactions.

TL;DR: A new peptidomimetic strategy that incorporates SiteMap and multiple-copy simultaneous search was used to design selective small-molecule inhibitors for β-catenin/Tcf interactions.
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Rational design of small-molecule inhibitors for β-catenin/T-cell factor protein-protein interactions by bioisostere replacement.

TL;DR: A new hot spot-based design strategy using bioisostere replacement is reported to rationally design nonpeptidic small-molecule inhibitors for protein-protein interactions and validated by the site-directed mutagenesis and structure-activity relationship (SAR) studies.