H
Ho-Jin Lee
Researcher at St. Jude Children's Research Hospital
Publications - 53
Citations - 2543
Ho-Jin Lee is an academic researcher from St. Jude Children's Research Hospital. The author has contributed to research in topics: Wnt signaling pathway & Dishevelled. The author has an hindex of 22, co-authored 50 publications receiving 2254 citations. Previous affiliations of Ho-Jin Lee include Southwest Tennessee Community College & Kigali Institute of Science and Technology.
Papers
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Journal ArticleDOI
Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled.
Hing-C. Wong,Audrey Bourdelas,Anke Krauss,Ho-Jin Lee,Youming Shao,Dianqing Wu,Marek Mlodzik,De-Li Shi,Jie Zheng,Jie Zheng +9 more
TL;DR: Differences in the binding affinity of the Dvl PDZ domain and its binding partners may be important in regulating signal transduction by Dvl, and these results identify a missing molecular connection within the Wnt pathway.
Journal ArticleDOI
PDZ domains and their binding partners: structure, specificity, and modification
Ho-Jin Lee,Jie Zheng +1 more
TL;DR: The structural characterization of PDZ domains is discussed and the use of recently emerging technologies such as proteomic arrays and peptide libraries to study the binding properties ofPDZ-mediated interactions are discussed.
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Electrochemical cues regulate assembly of the Frizzled/Dishevelled complex at the plasma membrane during planar epithelial polarization
Matias Simons,William J. Gault,Daniel Gotthardt,Rajeev Rohatgi,Thomas J. Klein,Youming Shao,Ho-Jin Lee,Ai Luen Wu,Yimin Fang,Lisa M. Satlin,J. Dow,Jie Chen,Jie Zheng,Michael Boutros,Marek Mlodzik +14 more
TL;DR: Results suggest that direct interaction between Fz and Dsh is stabilized by a pH and charge-dependent interaction of the DEP domain with phospholipids, which is particularly important for the PCP signalling branch and, thus, promotes specific pathway selection in Wnt signalling.
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Hydrogen Bonding Abilities of Thioamide
TL;DR: In this paper, the strengths of hydrogen bonding interaction between formamide (FA) and thioformamide (TFA) were investigated at the B3LYP level with the 6-311G(d,p), 6-31+G(m,p) and 6311++G(2d,2p) basis sets.
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Sulindac inhibits canonical Wnt signaling by blocking the PDZ domain of the protein Dishevelled.
TL;DR: The results suggest that the anticancer protective effect of sulindac (and its metabolite) reflect not only COX-1/2 inhibition but also the inhibition of abnormal canonical Wnt signaling via blockade of the Dvl PDZ domain.