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Yun-Beom Choi
Researcher at Brigham and Women's Hospital
Publications - 12
Citations - 4077
Yun-Beom Choi is an academic researcher from Brigham and Women's Hospital. The author has contributed to research in topics: Cysteine & Redox. The author has an hindex of 9, co-authored 11 publications receiving 3987 citations. Previous affiliations of Yun-Beom Choi include Boston Children's Hospital & Sanford-Burnham Institute for Medical Research.
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Journal ArticleDOI
A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds
Stuart A. Lipton,Yun-Beom Choi,Yun-Beom Choi,Zhuo Hua Pan,Zhuo Hua Pan,Sizheng Z. Lei,Sizheng Z. Lei,Huei-Sheng Vincent Chen,Huei-Sheng Vincent Chen,Nikolaus J. Sucher,Nikolaus J. Sucher,Joseph Loscalzo,Joseph Loscalzo,David J. Singel,Jonathan S. Stamler,Jonathan S. Stamler +15 more
TL;DR: It is reported that NO.-mediated neurotoxicity is engendered, at least in part, by reaction with superoxide anion (O.-2), apparently leading to formation of peroxynitrite (ONOO−), and not by NO.
Journal ArticleDOI
Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation.
Yun-Beom Choi,Lalitha Tenneti,Dean A. Le,Justin Ortiz,Guang Bai,Huei-Sheng Vincent Chen,Stuart A. Lipton,Stuart A. Lipton +7 more
TL;DR: It is shown that the NMDA receptor (NMDAR)-associated ion channel was modulated not only by exogenous NO but also by endogenous NO, and endogenous S-nitrosylation can regulate ion channel activity.
Journal ArticleDOI
Cysteine regulation of protein function--as exemplified by NMDA-receptor modulation.
Stuart A. Lipton,Yun-Beom Choi,Hiroto Takahashi,Dongxian Zhang,Weizhong Li,Adam Godzik,Laurie A. Bankston +6 more
TL;DR: The basis for these molecular cysteine switches is reviewed, drawing on the NMDA receptor as an exemplary protein, and a molecular model for the action of S-nitrosylation based on recently derived crystal structures is proposed.
Journal ArticleDOI
NMDA receptors: from genes to channels
TL;DR: Sucher et al. as mentioned in this paper showed that the pharmacological properties of recombinant NMDA receptors are not comparable to those of native NMDA receptor subunits, and they also pointed out that it is difficult to reconcile disparate effects obtained with recombinant versus native N-methyl-D-aspartate receptors.
Journal ArticleDOI
Identification and mechanism of action of two histidine residues underlying high-affinity Zn2+ inhibition of the NMDA receptor.
Yun-Beom Choi,Stuart A. Lipton +1 more
TL;DR: Two neighboring histidine residues on NR2A represent the critical determinant (termed the "short spacer") for high-affinity, voltage-independent Zn2+ inhibition using the Xenopus oocyte expression system and site-directed mutagenesis to suggest that the mechanism of high-Affinity Zn 2+ inhibition on the NMDAR involves enhancement of proton inhibition.