Multi-domain signaling proteins are regulatable switches that mediate signal transduction with high fidelity and selectivity in response to diverse cues. These proteins often harbor disease-associated mutations that disrupt their regulatory properties or interaction specificity to drive pathogenic signaling. Mapping se...
Anne E. van Vlimmeren, Zi-Yuan Jiang, Devon A. Semoy et al.· Biochemical Journal· 0 citations
Cells employ dense networks of transient protein–protein interactions mediated by modular peptide-binding domains and unstructured peptidic motifs for high-fidelity information processing. How these networks physically execute computations through protein interactions governed by complex intra- and intermolecular mecha...
Julia R. Rogers, Loren P. Cardani, Neel H. Shah et al.· bioRxiv· 0 citations
Traditional deep mutational scanning (DMS) encodes every single amino-acid substitution from a wild-type sequence. We hypothesize that combinatorial DMS (CDMS) libraries, incorporating all mutations in all combinations, can enable the discovery of high-affinity protein (super)binders by capturing epistatic, non-linear...
Ming-Xuan Jiang, Mo-Han Sun, Nuo Cheng et al.· Molecules and Cells· 0 citations
The use of site-specific photo-crosslinking to covalently capture the substrates of tyrosine phosphatases in situ reveals previously unknown roles of PTP1B in signaling systems and could be readily extended to other tyrosine phosphatases in the same family.
Andrew C. Johns, Yethmie S. Goonatilleke, David C. Cabanero et al.· bioRxiv· 0 citations
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