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Xiangying Cheng

As seen in: Nature, The Journal of Biological Chemistry
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Articles

Comprehensive multi-omic dissection and AI-prioritized target identification in inverted papilloma–associated sinonasal squamous cell carcinoma

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By Alka Singh, Viktoria A. Sarkisova, Ekaterina Vergasova, Ari Rosenberg, Karthik Suresh, Vasudha Mishra, Yuxuan Miao, Le Shen, Alexander Veviorskiy, Frank W. Pun, Xiangying Cheng, Jayant M. Pinto, Christopher Low, Mark W. Lingen, Lisa M. Rooper, Alexander Pearson, Everett E Vokes, Xuanyao Liu, Nyall R. London, Alex Zhavoronkov, Nishant Agrawal, Evgeny Izumchenko, Michael Korzinkin, Julia Smolik, Claudia Wing
| Nature Verified
Abstract Sinonasal squamous cell carcinoma (SNSCC) is a rare malignancy arising de novo or from inverted papilloma (IP), a benign neoplasm with malignant potential. The molecular drivers of IP-associated SNSCC (IP-SNSCC) remain poorly defined, and no effective therapies are available. Progress is hindered by limited preclinical studies and prospective clinical investigations.
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Allostery between two binding sites in the ion channel subunit TRIP8b confers binding specificity to HCN channels

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By Kyle A. Lyman, Clinical Neurosciences, Robert J. Heuermann, Xiangying Cheng
| The Journal of Biological Chemistry Verified
Tetratricopeptide repeat (TPR) domains are ubiquitous structural motifs that mediate protein–protein interactions. For example, the TPR domains in the peroxisomal import receptor PEX5 enable binding to a range of type 1 peroxisomal targeting signal motifs. A homolog of PEX5, tetratricopeptide repeat–containing Rab8b-interacting protein (TRIP8b), binds to and functions as an auxiliary subunit of hyperpolarization-activated cyclic nucleotide (HCN)–gated channels.
Open in Who Shared Issue with article?

Allostery between two binding sites in the ion channel subunit TRIP8b confers binding specificity to HCN channels

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By Kyle A. Lyman, Robert J. Heuermann, Xiangying Cheng, Jonathan E. Kurz
| The Journal of Biological Chemistry Verified
Tetratricopeptide repeat (TPR) domains are ubiquitous structural motifs that mediate protein-protein interactions. For example, the TPR domains in the peroxisomal import receptor PEX5 enable binding to a range of type 1 peroxisomal targeting signal (PTS1) motifs. A homolog of PEX5, tetratricopeptide repeat-containing Rab8b interacting protein (TRIP8b), binds to and functions as an auxiliary subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels.
Open in Who Shared Issue with article?
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