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The Journal of Biological Chemistry|January 2, 2019
TGF-β2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-β and inhibin-αMorkos A Henen, Pardeep Mahlawat, Christian Zwieb, et al.
Nature Communications|August 8, 2023
Cryo-EM structures of Uba7 reveal the molecular basis for ISG15 activation and E1-E2 thioester transferMohammad Afsar, GuanQun Liu, Lijia Jia, et al.
Nature Communications|August 19, 2022
Crystal structures reveal catalytic and regulatory mechanisms of the dual-specificity ubiquitin/FAT10 E1 enzyme Uba6Lingmin Yuan, Fei Gao, Zongyang Lv, et al.
Nature Communications|March 1, 2026
Cryo-EM structures of UBA6 reveal mechanisms of E1-E2 specificity and dual FAT10/ubiquitin thioester transferDigant Nayak, Lijia Jia, Priscila Dos Santos Bury, et al.
The Journal of Biological Chemistry|February 24, 2017
An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signalingSun Kyung Kim, Lindsey Barron, Cynthia S Hinck, et al.
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