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  1. Article ; Online: Reflections on the Basic Manuscript Editors’ Training 2017

    Hakbong Lee

    Science Editing, Vol 4, Iss 2, Pp 93-

    2017  Volume 94

    Keywords Science (General) ; Q1-390
    Language English
    Publishing date 2017-08-01T00:00:00Z
    Publisher Korean Council of Science Editors
    Document type Article ; Online
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  2. Article: Brief Pollination Assessment of a Critically Endangered Food-Deceptive Orchid (

    Lee, Hakbong / Lee, Heung-Sik / Bae, Kee-Hwa

    Plants (Basel, Switzerland)

    2022  Volume 11, Issue 6

    Abstract: The translocation of orchids (Orchidaceae) cannot be successful if one is unaware of their effective pollinators and plant-pollinator interactions. ...

    Abstract The translocation of orchids (Orchidaceae) cannot be successful if one is unaware of their effective pollinators and plant-pollinator interactions.
    Language English
    Publishing date 2022-03-17
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2704341-1
    ISSN 2223-7747
    ISSN 2223-7747
    DOI 10.3390/plants11060798
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  3. Article: Brief Pollination Assessment of a Critically Endangered Food-Deceptive Orchid (Cypripedium guttatum) Using a Network Approach

    Lee, Hakbong / Lee, Heung-Sik / Bae, Kee-Hwa

    Plants. 2022 Mar. 17, v. 11, no. 6

    2022  

    Abstract: The translocation of orchids (Orchidaceae) cannot be successful if one is unaware of their effective pollinators and plant–pollinator interactions. Cypripedium guttatum is a generalized food-deceptive orchid, which is highly threatened in the Republic of ...

    Abstract The translocation of orchids (Orchidaceae) cannot be successful if one is unaware of their effective pollinators and plant–pollinator interactions. Cypripedium guttatum is a generalized food-deceptive orchid, which is highly threatened in the Republic of Korea, thus, requiring immediate translocation actions. Although effective pollinators of the orchid are well known in China, little is known about the pollinators in the Republic of Korea and the ecological context in which the orchid can be successfully pollinated. To briefly assess the pollination of C. guttatum prior to translocation, we conducted a one-month survey of general pollination and the community-wide plant–pollinator network properties. Over 21 h of observation, we found that an effective pollinator of the orchid was the sweat bee Lasioglossum virideglaucum. The network was significantly specialized and modular, but not significantly nested. L. virideglaucum (pollinator) and Arabis gemmifera (plant) were determined to be keystone species, based on network metrics. A total of six network modules were identified and the flower colors of the plant species belonging to the C. guttatum module were purple, white, and yellow. After comparing the daily network patterns, we found that pollination of the orchid was accomplished when various flowering plant species bloom, and the nestedness value was high. This study revealed that high plant and pollinator richness could increase the chance that the deceptive orchid would be pollinated. Our study suggests that the network properties of this food-deceptive orchid community could provide useful insight into understanding the ecologically suitable habitat for the translocation of the highly threatened orchid species C. guttatum.
    Keywords Arabis ; Cypripedium ; Lasioglossum ; flowers ; habitats ; keystone species ; nestedness ; pollination ; pollinators ; surveys ; China ; South Korea
    Language English
    Dates of publication 2022-0317
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2704341-1
    ISSN 2223-7747
    ISSN 2223-7747
    DOI 10.3390/plants11060798
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  4. Article ; Online: Correction to "Mitoquinone Inactivates Mitochondrial Chaperone TRAP1 by Blocking the Client Binding Site".

    Yoon, Nam Gu / Lee, Hakbong / Kim, So-Yeon / Hu, Sung / Kim, Darong / Yang, Sujae / Hong, Ki Bum / Lee, Ji Hoon / Kang, Soosung / Kim, Byung-Gyu / Myung, Kyungjae / Lee, Changwook / Kang, Byoung Heon

    Journal of the American Chemical Society

    2022  Volume 144, Issue 4, Page(s) 2020

    Language English
    Publishing date 2022-01-19
    Publishing country United States
    Document type Published Erratum
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.2c00039
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  5. Article: A chemical tool for blue light-inducible proximity photo-crosslinking in live cells.

    Mishra, Pratyush Kumar / Kang, Myeong-Gyun / Lee, Hakbong / Kim, Seungjoon / Choi, Subin / Sharma, Nirmali / Park, Cheol-Min / Ko, Jaewon / Lee, Changwook / Seo, Jeong Kon / Rhee, Hyun-Woo

    Chemical science

    2021  Volume 13, Issue 4, Page(s) 955–966

    Abstract: We developed a proximity photo-crosslinking method ( ...

    Abstract We developed a proximity photo-crosslinking method (
    Language English
    Publishing date 2021-12-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/d1sc04871f
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  6. Article ; Online: Mitoquinone Inactivates Mitochondrial Chaperone TRAP1 by Blocking the Client Binding Site.

    Yoon, Nam Gu / Lee, Hakbong / Kim, So-Yeon / Hu, Sung / Kim, Darong / Yang, Sujae / Hong, Ki Bum / Lee, Ji Hoon / Kang, Soosung / Kim, Byung-Gyu / Myung, Kyungjae / Lee, Changwook / Kang, Byoung Heon

    Journal of the American Chemical Society

    2021  Volume 143, Issue 47, Page(s) 19684–19696

    Abstract: Heat shock protein 90 (Hsp90) family proteins are molecular chaperones that modulate the functions of various substrate proteins (clients) implicated in pro-tumorigenic pathways. In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) ... ...

    Abstract Heat shock protein 90 (Hsp90) family proteins are molecular chaperones that modulate the functions of various substrate proteins (clients) implicated in pro-tumorigenic pathways. In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) was identified as a potent inhibitor of mitochondrial Hsp90, known as a tumor necrosis factor receptor-associated protein 1 (TRAP1). Structural analyses revealed an asymmetric bipartite interaction between MitoQ and the previously unrecognized drug binding sites located in the middle domain of TRAP1, believed to be a client binding region. MitoQ effectively competed with TRAP1 clients, and MitoQ treatment facilitated the identification of 103 TRAP1-interacting mitochondrial proteins in cancer cells. MitoQ and its redox-crippled SB-U014/SB-U015 exhibited more potent anticancer activity
    MeSH term(s) Animals ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use ; Binding Sites ; HSP90 Heat-Shock Proteins/antagonists & inhibitors ; HSP90 Heat-Shock Proteins/chemistry ; HeLa Cells ; Humans ; Mice, Nude ; Neoplasms/drug therapy ; Organophosphorus Compounds/pharmacology ; Organophosphorus Compounds/therapeutic use ; Ubiquinone/analogs & derivatives ; Ubiquinone/pharmacology ; Ubiquinone/therapeutic use ; Xenograft Model Antitumor Assays ; Mice
    Chemical Substances Antineoplastic Agents ; HSP90 Heat-Shock Proteins ; Organophosphorus Compounds ; TRAP1 protein, human ; Ubiquinone (1339-63-5) ; mitoquinone (47BYS17IY0)
    Language English
    Publishing date 2021-11-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.1c07099
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  7. Article ; Online: The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome

    Hakbong Lee / Hanbin Jeong / Joonho Choe / Youngsoo Jun / Chunghun Lim / Changwook Lee

    Scientific Reports, Vol 7, Iss 1, Pp 1-

    2017  Volume 13

    Abstract: Abstract Kohlschutter-Tönz syndrome (KTS) is a rare autosomal-recessive disorder of childhood onset characterized by global developmental delay, spasticity, epilepsy, and amelogenesis imperfecta. Rogdi, an essential protein, is highly conserved across ... ...

    Abstract Abstract Kohlschutter-Tönz syndrome (KTS) is a rare autosomal-recessive disorder of childhood onset characterized by global developmental delay, spasticity, epilepsy, and amelogenesis imperfecta. Rogdi, an essential protein, is highly conserved across metazoans, and mutations in Rogdi are linked to KTS. However, how certain mutations in Rogdi abolish its physiological functions and cause KTS is not known. In this study, we determined the crystal structure of human Rogdi protein at atomic resolution. Rogdi forms a novel elongated curved structure comprising the α domain, a leucine-zipper-like four-helix bundle, and a characteristic β-sheet domain. Within the α domain, the N-terminal H1 helix (residues 19–45) pairs with the C-terminal H6 helix (residues 252–287) in an antiparallel manner, indicating that the integrity of the four-helix bundle requires both N- and C-terminal residues. The crystal structure, in conjunction with biochemical data, indicates that the α domain might undergo a conformational change and provide a structural platform for protein–protein interactions. Disruption of the four-helix bundle by mutation results in significant destabilization of the structure. This study provides structural insights into how certain mutations in Rogdi affect its structure and cause KTS, which has important implications for the development of pharmaceutical agents against this debilitating neurological disease.
    Keywords Medicine ; R ; Science ; Q
    Subject code 572
    Language English
    Publishing date 2017-06-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
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  8. Article: Mitoquinone Inactivates Mitochondrial Chaperone TRAP1 by Blocking the Client Binding Site

    Yoon, Nam Gu / Lee, Hakbong / Kim, So-Yeon / Hu, Sung / Kim, Darong / Yang, Sujae / Hong, Ki Bum / Lee, Ji Hoon / Kang, Soosung / Kim, Byung-Gyu / Myung, Kyungjae / Lee, Changwook / Kang, Byoung Heon

    Journal of the American Chemical Society. 2021 Nov. 10, v. 143, no. 47

    2021  

    Abstract: Heat shock protein 90 (Hsp90) family proteins are molecular chaperones that modulate the functions of various substrate proteins (clients) implicated in pro-tumorigenic pathways. In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) ... ...

    Abstract Heat shock protein 90 (Hsp90) family proteins are molecular chaperones that modulate the functions of various substrate proteins (clients) implicated in pro-tumorigenic pathways. In this study, the mitochondria-targeted antioxidant mitoquinone (MitoQ) was identified as a potent inhibitor of mitochondrial Hsp90, known as a tumor necrosis factor receptor-associated protein 1 (TRAP1). Structural analyses revealed an asymmetric bipartite interaction between MitoQ and the previously unrecognized drug binding sites located in the middle domain of TRAP1, believed to be a client binding region. MitoQ effectively competed with TRAP1 clients, and MitoQ treatment facilitated the identification of 103 TRAP1-interacting mitochondrial proteins in cancer cells. MitoQ and its redox-crippled SB-U014/SB-U015 exhibited more potent anticancer activity in vitro and in vivo than previously reported mitochondria-targeted TRAP1 inhibitors. The findings indicate that targeting the client binding site of Hsp90 family proteins offers a novel strategy for the development of potent anticancer drugs.
    Keywords antineoplastic activity ; antioxidants ; heat-shock protein 90 ; mitochondria ; tumor necrosis factors
    Language English
    Dates of publication 2021-1110
    Size p. 19684-19696.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.1c07099
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  9. Article ; Online: Crystallization and preliminary X-ray diffraction analysis of the Sel1-like repeats of SEL1L.

    Jeong, Hanbin / Lee, Hakbong / Lee, Changwook

    Acta crystallographica. Section F, Structural biology communications

    2014  Volume 70, Issue Pt 12, Page(s) 1624–1627

    Abstract: Terminally misfolded or unassembled proteins are selectively recognized and cleared by the ER-associated degradation (ERAD) pathway. Suppressor/enhancer of lin-12-like (SEL1L), a component of the dislocation machinery containing the E3 ubiquitin ligase ... ...

    Abstract Terminally misfolded or unassembled proteins are selectively recognized and cleared by the ER-associated degradation (ERAD) pathway. Suppressor/enhancer of lin-12-like (SEL1L), a component of the dislocation machinery containing the E3 ubiquitin ligase Hrd1, plays an important role in selecting and transporting ERAD substrates for degradation in the endoplasmic reticulum. In this study, the purification, crystallization and preliminary X-ray diffraction analysis of recombinant mouse SEL1L (residues 348-533) are reported. The crystals were obtained by the hanging-drop vapour-diffusion method at pH 8.5 and 277 K using 30% 2-propanol as a precipitant. Optimized crystals diffracted to 3.3 Å resolution at a synchrotron-radiation source. Preliminary X-ray diffraction analysis revealed that the crystals belonged to space group P21 and contained four molecules per asymmetric unit, with a solvent content of 44%.
    MeSH term(s) Animals ; Base Sequence ; Crystallization ; Crystallography, X-Ray ; DNA Primers ; Intracellular Signaling Peptides and Proteins ; Mice ; Polymerase Chain Reaction ; Proteins/chemistry
    Chemical Substances DNA Primers ; Intracellular Signaling Peptides and Proteins ; Proteins ; Sel1h protein, mouse
    Language English
    Publishing date 2014-11-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2053-230X
    ISSN (online) 2053-230X
    DOI 10.1107/S2053230X14023115
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  10. Article ; Online: Impaired DNA-binding affinity of novel PAX6 mutations

    Seowhang Lee / Seung-Han Lee / Hwan Heo / Eun Hye Oh / Jin-Hong Shin / Hyang-Sook Kim / Jae-Ho Jung / Seo Young Choi / Kwang-Dong Choi / Hakbong Lee / Changwook Lee / Jae-Hwan Choi

    Scientific Reports, Vol 10, Iss 1, Pp 1-

    2020  Volume 10

    Abstract: Abstract Mutations in human PAX6 gene are associated with various congenital eye malformations including aniridia, foveal hypoplasia, and congenital nystagmus. These various phenotypes may depend on the mutation spectrums that can affect DNA-binding ... ...

    Abstract Abstract Mutations in human PAX6 gene are associated with various congenital eye malformations including aniridia, foveal hypoplasia, and congenital nystagmus. These various phenotypes may depend on the mutation spectrums that can affect DNA-binding affinity, although this hypothesis is debatable. We screened PAX6 mutations in two unrelated patients with congenital nystagmus, and measured DNA-binding affinity through isothermal titration calorimetry (ITC). To elucidate phenotypic differences according to DNA-binding affinity, we also compared DNA-binding affinity among the previously reported PAX6 missense mutations within the linker region between two subdomains of the paired domain (PD). We identified two novel mutations of PAX6 gene: c.214 G > T (p.Gly72Cys) and c.249_250delinsCGC (p.Val84Alafs*8). Both were located within the linker region between the two subdomains of the PD. ITC measurement revealed that the mutation p.Val84Alafs*8 had no DNA-binding affinity, while the p.Gly72Cys mutation showed a decreased binding affinity (Kd = 0.58 μM) by approximately 1.4 times compared to the wild type-PAX6 (Kd = 0.41 μM). We also found that there was no close relationship between DNA-binding affinity and phenotypic differences. Our results suggest that the DNA-binding affinity alone might be insufficient to determine PAX6-related phenotypes, and that other modifier genes or environmental factors might affect phenotypes of the PAX6 gene.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2020-02-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
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