ArticleACS chemical biology2014
Resurfaced shape complementary proteins that selectively bind the oncoprotein gankyrin.
Article in ACS chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Gankyrin-Protein Interactions in GI Cancers: A Novel Target of New Therapeutics.Chronic diseases and translational medicine · 2025Review
- Gankyrin as a potential target for tumor therapy: evidence and perspectives.American journal of translational research · 2018Review
- Scratching the Surface: Resurfacing Proteins to Endow New Properties and Function.Cell chemical biology · 2016Review
- Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell.Scientific reports · 2016Article
- Synthetic Proteins Potently and Selectively Bind the Oncoprotein Gankyrin, Modulate Its Interaction with S6 ATPase, and Suppress Gankyrin/MDM2-Dependent Ubiquitination of p53.ACS chemical biology · 2015Article
- Characterization of the binding interaction between the oncoprotein gankyrin and a grafted S6 ATPase.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Increased cellular levels of protein-protein interactions involving the ankyrin repeat oncoprotein gankyrin are directly linked to aberrant cellular events and numerous cancers. Inhibition of these protein-protein interactions is thus an attractive therapeutic strategy. However, the relatively featureless topology of gankyrin's putative binding face and large surface areas involved in gankyrin-dependent protein-protein interactions present a dramatic challenge to small molecule discovery. The size, high folding energies, and well-defined surfaces present in many proteins overcome some of the challenges faced by small molecule discovery. We used split-superpositive Green Fluorescent Protein (split-spGFP) reassembly to screen a 5×10(9) library of resurfaced proteins that are shape complementary to the putative binding face of gankyrin and identified mutants that potently and selectively bind this oncoprotein in vitro and in living cells. Collectively, our findings represent the first synthetic proteins that bind gankyrin and may represent a general strategy for developing protein basic research tools and drug leads that bind disease-relevant ankyrin repeats.
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Registered trials
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