Hyun Lee

Prof. Hyun Lee

Department of Pharmaceutical Science, College of Pharmacy, University of Illinois at Chicago, Chicago, IL, USA
orcid

Research Focus & Metrics

Academic Career Length

32Years (1995-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 September 2000 in Journal of Biological Chemistry
Verified
Journal Article
Open access
PDF file
HLHyun Lee
Hyun Lee
KMK. H. Mok
K. H. Mok
RMRanjith Muhandiram
Ranjith Muhandiram
KPKyu-Hwan Park
Kyu-Hwan Park
JSJae-Eun Suk
Jae-Eun Suk
KHKyou-Hoon Han
Kyou-Hoon Han
DNA transcription is initiated by a small regulatory region of transactivators known as the transactivation domain. In contrast to the rapid progress made on the functional aspect of this promiscuous domain, its structural feature is still poorly characterized. Here, our multidimensional NMR study reveals that an unbound full-length p53 transactivation domain, although similar to the recently discovered group of loosely folded proteins in that it does not have tertiary structure, is nevertheless populated by an amphipathic helix and two nascent turns. The helix is formed by residues Thr18–Leu26(Thr-Phe-Ser-Asp-Leu-Trp-Lys-Leu-Leu), whereas the two turns are formed by residues Met40–Met44 and Asp48–Trp53, respectively. It is remarkable that these local secondary structures are selectively formed by functionally critical and positionally conserved hydrophobic residues present in several acidic transactivation domains. This observation suggests that such local structures are general features of acidic transactivation domains and may represent “specificity determinants” (Ptashne, M., and Gann, A. A. F. (1997),Nature 386, 569–577) that are important for transcriptional activity.

20 July 2021 in Science
Verified
Journal Article
Open access
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NDNir Drayman
Nir Drayman
JDJennifer K. DeMarco
Jennifer K. DeMarco
KJKrysten A. Jones
Krysten A. Jones
SASaara-Anne Azizi
Saara-Anne Azizi
HFHeather M. Froggatt
Heather M. Froggatt
STSavas Tay
Savas Tay
Targeting the main protease of SARS-CoV-2: Inside host cells, the RNA genome of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is translated into two polyproteins that are cleaved to give the individual viral proteins. The main viral protease, known as Mpro or 3CLpro, plays a key role in these cleavages, making it an important drug target. Drayman et al . identified eight drugs that target 3CLpro from a library of 1900 clinically safe drugs. Because of the challenge of working with SARS-CoV-2, they started by screening for drugs that inhibit the replication of a human coronavirus that causes the common cold. They then evaluated the top hits for inhibiting SARS-CoV-2 replication and for inhibiting 3CLpro. Masitinib, a broad antiviral, inhibited the main proteases of coronaviruses and picornaviruses and was effective in reducing SARS-CoV-2 replication in mice. —VV

19 October 2021 in Journal of Medicinal Chemistry
Verified
Journal Article
Closed access
ZSZhengnan Shen
Zhengnan Shen
KRKiira Ratia
Kiira Ratia
LCLaura Cooper
Laura Cooper
DKDeyu Kong
Deyu Kong
HLHyun Lee
Hyun Lee
RXRui Xiong
Rui Xiong

26 June 2017 in Nature Medicine
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Journal Article
Closed access
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SHSalim S Hayek
Salim S Hayek
KKKwi Hye Koh
Kwi Hye Koh
MGMorgan E Grams
Morgan E Grams
CWChangli Wei
Changli Wei
YKYi-An Ko
Yi-An Ko
JRJochen Reiser
Jochen Reiser

23 December 2008 in Science Signaling
Verified
Journal Article
Closed access
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AMAnjali Mahajan
Anjali Mahajan
CYChunhua Yuan
Chunhua Yuan
HLHyun Lee
Hyun Lee
ECEric S.-W. Chen
Eric S.-W. Chen
PWPei-Yu Wu
Pei-Yu Wu
MTMing-Daw Tsai
Ming-Daw Tsai
The forkhead-associated (FHA) domain binds specifically to phosphothreonine residues and possesses unique structural and functional features.

9 June 2010 in Journal of Medicinal Chemistry
Verified
Journal Article
Closed access
AGArun K. Ghosh
Arun K. Ghosh
JTJun Takayama
Jun Takayama
KRKalapala Venkateswara Rao
Kalapala Venkateswara Rao
KRKiira Ratia
Kiira Ratia
RCRima Chaudhuri
Rima Chaudhuri
AMAndrew D. David Mesecar
Andrew D. David Mesecar