<h1>Du, Fangyong</h1>
<h2>Combined from <a href="https://authors.library.caltech.edu">CaltechAUTHORS</a></h2>
<ul>
<li>Xia, Zanxian and Webster, Ailsa, el al. (2008) <a href="https://resolver.caltech.edu/CaltechAUTHORS:XIAjbc08">Substrate-binding sites of UBR1, the ubiquitin ligase of the N-end rule pathway</a>; Journal of Biological Chemistry; Vol. 283; No. 35; 24011-24028; PMCID PMC2527112; <a href="https://doi.org/10.1074/jbc.M802583200">10.1074/jbc.M802583200</a></li>
<li>Du, Fangyong and Navarro-Garcia, Federico, el al. (2002) <a href="https://resolver.caltech.edu/CaltechAUTHORS:DUFpnas02">Pairs of dipeptides synergistically activate the binding of substrate by ubiquitin ligase through dissociation of its autoinhibitory domain</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 22; 14110-14115; PMCID PMC137845; <a href="https://doi.org/10.1073/pnas.172527399">10.1073/pnas.172527399</a></li>
<li>Kwon, Yong Tae and Kashina, Anna S., el al. (2002) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20141114-160435229">An Essential Role of N-Terminal Arginylation in Cardiovascular Development</a>; Science; Vol. 297; No. 5578; 96-99; <a href="https://doi.org/10.1126/science.1069531">10.1126/science.1069531</a></li>
<li>Varshavsky, Alexander and Turner, Glenn, el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180803-074725065">The Ubiquitin System and the N-End Rule Pathway</a>; Biological Chemistry; Vol. 381; No. 9-10; 779-789; <a href="https://doi.org/10.1515/BC.2000.101">10.1515/BC.2000.101</a></li>
<li>Turner, Glenn C. and Du, Fangyong, el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150330-105345474">Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway</a>; Nature; Vol. 405; No. 6786; 579; <a href="https://doi.org/10.1038/35014629">10.1038/35014629</a></li>
<li>Saks, Margaret E. and Sampson, Jeffrey R., el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SAKjbc96">An engineered Tetrahymena tRNA(Gln) for in vivo incorporation of unnatural amino acids into proteins by nonsense suppression</a>; Journal of Biological Chemistry; Vol. 271; No. 38; 23169-23175</li>
</ul>