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  1. Book ; Online ; E-Book: Discovery of small-molecule modulators of protein-RNA interactions for treating cancer and COVID-19

    Byun, Wan Gi

    (Springer Theses)

    2023  

    Author's details Wan Gi Byun
    Series title Springer Theses
    MeSH term(s) Neoplasms/therapy. ; Neoplasms/genetics. ; RNA ; COVID-19 ; Proteins
    Keywords COVID-19 (Disease) ; Cancer/Molecular aspects
    Subject code 362.1962414
    Language English
    Size 1 online resource (156 pages)
    Publisher Springer
    Publishing place Singapore
    Document type Book ; Online ; E-Book
    Note "Doctoral thesis accepted by Seoul National University, Seoul, Korea (Republic of)"
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 9789811978142 ; 9789811978135 ; 981197814X ; 9811978131
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Discovery of Small-Molecule Modulators of Protein¿RNA Interactions for Treating Cancer and COVID-19

    Byun, Wan Gi

    (Springer Theses)

    2022  

    Author's details Wan Gi Byun received his B.S. degree in Department of Chemistry at Seoul National University, Korea in 2015. In the same year, he joined Prof. Seung Bum Park's group in the Department of Chemistry at the Seoul National University and started to study chemical biology and drug discovery. His research during Ph.D. involved the development of high-throughput screening systems and identification of small-molecule modulators of protein-RNA interactions to overcome human diseases including cancer and COVID-19. After he got his Ph.D. degree in 2022, he is currently a post-doctoral researcher in Department of Chemistry, Seoul National University. His current research focus on the development of broadspectrum, pan-coronavirus antiviral drugs
    Series title Springer Theses
    Keywords Protein¿RNA Interaction ; High-Throughput Screening ; Chemical Biology ; cancer treatment ; Protein–RNA Interaction ; High-throughput Screening ; COVID-19 ; Cancer Treatment
    Language English
    Size 160 p.
    Edition 1
    Publisher Springer Nature Singapore
    Document type Book
    Note PDA Manuell_19
    Format 160 x 241 x 14
    ISBN 9789811978135 ; 9811978131
    Database PDA

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  3. Article ; Online: Small-molecule modulators of protein-RNA interactions.

    Byun, Wan Gi / Lim, Donghyun / Park, Seung Bum

    Current opinion in chemical biology

    2022  Volume 68, Page(s) 102149

    Abstract: Protein-RNA interactions (PRIs) play crucial roles in diverse cellular pathways, from transcription to liquid-liquid phase separation, and its dysregulation is associated with a wide range of human disorders. Therefore, there is great emphasis on ... ...

    Abstract Protein-RNA interactions (PRIs) play crucial roles in diverse cellular pathways, from transcription to liquid-liquid phase separation, and its dysregulation is associated with a wide range of human disorders. Therefore, there is great emphasis on discovering small-molecule modulators that target unexplored PRIs by developing robust PRI assays. In particular, targeting PRIs could offer innovative solutions to expand the druggable genome, as only a small portion of protein-coding genes are currently targeted by drugs. This review describes the therapeutic potential of targeting PRIs using small molecules, biochemical and cell-based experimental tools for observing PRIs, and several PRI modulators. We also highlight emerging technologies and the challenges in developing PRI modulators.
    MeSH term(s) Humans ; RNA-Binding Proteins ; Small Molecule Libraries/pharmacology
    Chemical Substances RNA-Binding Proteins ; Small Molecule Libraries
    Language English
    Publishing date 2022-05-06
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1439176-4
    ISSN 1879-0402 ; 1367-5931
    ISSN (online) 1879-0402
    ISSN 1367-5931
    DOI 10.1016/j.cbpa.2022.102149
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4986: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: Harnessing stress granule formation by small molecules to inhibit the cellular replication of SARS-CoV-2.

    Byun, Wan Gi / Lee, Jihye / Kim, Seungtaek / Park, Seung Bum

    Chemical communications (Cambridge, England)

    2021  Volume 57, Issue 93, Page(s) 12476–12479

    Abstract: We identified small-molecule enhancers of cellular stress granules by observing molecular crowding of proteins and RNAs in a time-dependent manner. Hit molecules sensitized the IRF3-mediated antiviral mechanism in the presence of poly(I:C) and inhibited ... ...

    Abstract We identified small-molecule enhancers of cellular stress granules by observing molecular crowding of proteins and RNAs in a time-dependent manner. Hit molecules sensitized the IRF3-mediated antiviral mechanism in the presence of poly(I:C) and inhibited the replication of SARS-CoV-2 by inducing stress granule formation. Thus, modulating multimolecular crowding can be a promising strategy against SARS-CoV-2.
    MeSH term(s) Animals ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Benzopyrans/chemistry ; Benzopyrans/pharmacology ; Cell Line, Tumor ; Chlorocebus aethiops ; Cytoplasmic Granules/drug effects ; Cytoplasmic Granules/metabolism ; Dose-Response Relationship, Drug ; Drug Combinations ; Humans ; Interferon Regulatory Factor-3/metabolism ; Lopinavir/pharmacology ; Microbial Sensitivity Tests ; Molecular Structure ; Poly I-C/pharmacology ; Pyrazoles/chemistry ; Pyrazoles/pharmacology ; SARS-CoV-2/drug effects ; Structure-Activity Relationship ; Vero Cells ; Virus Replication/drug effects
    Chemical Substances Antiviral Agents ; Benzopyrans ; Drug Combinations ; IRF3 protein, human ; Interferon Regulatory Factor-3 ; Pyrazoles ; Lopinavir (2494G1JF75) ; Poly I-C (O84C90HH2L)
    Language English
    Publishing date 2021-11-23
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d1cc05508a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Harnessing stress granule formation by small molecules to inhibit the cellular replication of SARS-CoV-2

    Byun, Wan Gi / Lee, Jihye / Kim, Seungtaek / Park, Seung Bum

    Chemical communications. 2021 Nov. 23, v. 57, no. 93

    2021  

    Abstract: We identified small-molecule enhancers of cellular stress granules by observing molecular crowding of proteins and RNAs in a time-dependent manner. Hit molecules sensitized the IRF3-mediated antiviral mechanism in the presence of poly(I:C) and inhibited ... ...

    Abstract We identified small-molecule enhancers of cellular stress granules by observing molecular crowding of proteins and RNAs in a time-dependent manner. Hit molecules sensitized the IRF3-mediated antiviral mechanism in the presence of poly(I:C) and inhibited the replication of SARS-CoV-2 by inducing stress granule formation. Thus, modulating multimolecular crowding can be a promising strategy against SARS-CoV-2.
    Keywords RNA ; Severe acute respiratory syndrome coronavirus 2 ; chemical communication ; cytoplasmic granules ; harness ; proteins
    Language English
    Dates of publication 2021-1123
    Size p. 12476-12479.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d1cc05508a
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Discovery of Small-Molecule Modulators of Protein-RNA Interactions by Fluorescence Intensity-Based Binding Assay.

    Byun, Wan Gi / Lim, Donghyun / Park, Seung Bum

    Chembiochem : a European journal of chemical biology

    2019  Volume 21, Issue 6, Page(s) 818–824

    Abstract: Protein-RNA interactions mediate various cellular processes, the dysregulation of which has been associated with a list of diseases. Thus, novel experimental tools for monitoring protein-RNA interactions are highly desirable to identify new chemical ... ...

    Abstract Protein-RNA interactions mediate various cellular processes, the dysregulation of which has been associated with a list of diseases. Thus, novel experimental tools for monitoring protein-RNA interactions are highly desirable to identify new chemical modulators of these therapeutic targets. In this study, we constructed simple fluorescence intensity-based protein-RNA binding assays by testing multiple environment-sensitive organic fluorophores. We selected the oncogenic interaction between Lin28 and the let-7 microRNA and the important immunomodulatory Roquin-Tnf CDE interaction as representative targets. We adapted this assay to high-throughput screening for the identification of pyrazolyl thiazolidinedione-type molecules as potent small-molecule inhibitors of protein-microRNA interactions. We clearly showed the structure-activity relationships of this new class of Lin28-let-7 interaction inhibitors, and confirmed that cellular mature let-7 microRNAs and their target genes could be modulated upon treatment with the pyrazolyl thiazolidinedione-type inhibitor. We expect that our simple and adaptable screening approach can be applied for the development of various assay systems aimed at the identification of bioactive small molecules targeting protein-RNA interactions.
    MeSH term(s) Binding Sites/drug effects ; Drug Discovery ; Fluorescence ; High-Throughput Screening Assays ; Humans ; MicroRNAs/antagonists & inhibitors ; MicroRNAs/chemistry ; RNA-Binding Proteins/antagonists & inhibitors ; RNA-Binding Proteins/chemistry ; Small Molecule Libraries/chemical synthesis ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology ; Thiazolidinediones/chemical synthesis ; Thiazolidinediones/chemistry ; Thiazolidinediones/pharmacology
    Chemical Substances Lin28A protein, human ; MicroRNAs ; RNA-Binding Proteins ; Small Molecule Libraries ; Thiazolidinediones ; mirnlet7 microRNA, human ; 2,4-thiazolidinedione (AA68LXK93C)
    Language English
    Publishing date 2019-11-18
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020469-3
    ISSN 1439-7633 ; 1439-4227
    ISSN (online) 1439-7633
    ISSN 1439-4227
    DOI 10.1002/cbic.201900467
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Restoring Let-7 microRNA Biogenesis Using a Small-Molecule Inhibitor of the Protein-RNA Interaction.

    Lim, Donghyun / Byun, Wan Gi / Park, Seung Bum

    ACS medicinal chemistry letters

    2018  Volume 9, Issue 12, Page(s) 1181–1185

    Abstract: Abnormal function of RNA-binding proteins can lead to dysregulation of RNA function, causing a variety of disease states. Thus, developing small-molecule modulators of protein-RNA interactions is one of the key challenges in chemical biology. Herein, we ... ...

    Abstract Abnormal function of RNA-binding proteins can lead to dysregulation of RNA function, causing a variety of disease states. Thus, developing small-molecule modulators of protein-RNA interactions is one of the key challenges in chemical biology. Herein, we performed a high-throughput screening of chemical libraries using a Förster resonance energy transfer-based Lin28-let-7 interaction assay to identify a potent small-molecule inhibitor of the protein-microRNA interaction, as it is an important target implicated in stem cell-like phenotypes in cancer cells. The new inhibitor KCB3602 selectively restored cellular let-7 microRNA levels, decreased the expression of a panel of oncogenes responsible for cancer stem cell maintenance, and showed potential anticancer activities. We expect that our Lin28-let-7 interaction inhibitor will provide a good starting point for pharmacological eradication of cancer stem cells.
    Language English
    Publishing date 2018-11-08
    Publishing country United States
    Document type Journal Article
    ISSN 1948-5875
    ISSN 1948-5875
    DOI 10.1021/acsmedchemlett.8b00323
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: S-Benproperine, an Active Stereoisomer of Benproperine, Suppresses Cancer Migration and Tumor Metastasis by Targeting ARPC2.

    Jang, Hyun-Jin / Yoon, Yae Jin / Choi, Jiyeon / Lee, Yu-Jin / Lee, Sangku / Cho, Wansang / Byun, Wan Gi / Park, Seung Bum / Han, Dong Cho / Kwon, Byoung-Mog

    Pharmaceuticals (Basel, Switzerland)

    2022  Volume 15, Issue 12

    Abstract: Metastasis, in which cancer cells migrate to other tissues and form new tumors, is a major cause of both cancer death and treatment failure. In a previous study, benproperine (Benp) was identified as a cancer cell migration inhibitor and an inhibitor of ... ...

    Abstract Metastasis, in which cancer cells migrate to other tissues and form new tumors, is a major cause of both cancer death and treatment failure. In a previous study, benproperine (Benp) was identified as a cancer cell migration inhibitor and an inhibitor of actin-related protein 2/3 complex subunit 2 (ARPC2). However, Benp is a racemic mixture, and which stereoisomer is the active isomer remains unclear. In this study, we found that S-Benp is an active isomer and inhibits the migration and invasion of cancer cells much more strongly than R-Benp, with no effect on normal cells. The metastasis inhibitory effect of S-Benp was also verified in an animal model. Validating that inhibitors bind to their targets in cells and tissues has been a very challenging task in drug discovery. The direct interactions between ARPC2 and S-Benp were verified by surface plasmon resonance analysis (SPR), a cellular thermal shift assay (CETSA), and drug affinity responsive target stability (DARTS). In the mutant study with ARPC2
    Language English
    Publishing date 2022-11-25
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2193542-7
    ISSN 1424-8247
    ISSN 1424-8247
    DOI 10.3390/ph15121462
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Discovery of a Small-Molecule Inhibitor of Protein-MicroRNA Interaction Using Binding Assay with a Site-Specifically Labeled Lin28.

    Lim, Donghyun / Byun, Wan Gi / Koo, Ja Young / Park, Hankum / Park, Seung Bum

    Journal of the American Chemical Society

    2016  Volume 138, Issue 41, Page(s) 13630–13638

    Abstract: MicroRNAs (miRNAs) regulate gene expression by targeting protein-coding transcripts that are involved in various cellular processes. Thus, miRNA biogenesis has been recognized as a novel therapeutic target. Especially, the let-7 miRNA family is well- ... ...

    Abstract MicroRNAs (miRNAs) regulate gene expression by targeting protein-coding transcripts that are involved in various cellular processes. Thus, miRNA biogenesis has been recognized as a novel therapeutic target. Especially, the let-7 miRNA family is well-known for its tumor suppressor functions and is downregulated in many cancer cells. Lin28 protein binds to let-7 miRNA precursors to inhibit their maturation. Herein, we developed a FRET-based, high-throughput screening system to identify small-molecule inhibitors of the Lin28-let-7 interaction. We employed unnatural amino acid mutagenesis and bioorthogonal chemistry for the site-specific fluorescent labeling of Lin28, which ensures the robustness and reliability of the FRET-based protein-miRNA binding assay. Using this direct binding assay, we identified an inhibitor of the oncogenic Lin28-let-7 interaction. The inhibitor enhanced the production of let-7 miRNAs in Lin28-expressing cancer cells and reduced the level of let-7 target oncogene products.
    Language English
    Publishing date 2016-10-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3155-0
    ISSN 1520-5126 ; 0002-7863
    ISSN (online) 1520-5126
    ISSN 0002-7863
    DOI 10.1021/jacs.6b06965
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

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  10. Article ; Online: Pattern formation of metal-oxide hybrid nanostructures via the self-assembly of di-block copolymer blends.

    Jung, Dae Soo / Bang, Jiwon / Park, Tae Wan / Lee, Seung Hyup / Jung, Yun Kyung / Byun, Myunghwan / Cho, Young-Rae / Kim, Kwang Ho / Seong, Gi Hun / Park, Woon Ik

    Nanoscale

    2019  Volume 11, Issue 40, Page(s) 18559–18567

    Abstract: The templated self-assembly of block copolymers (BCPs) with a high Flory-Huggins interaction parameter (χ) can effectively create ultrafine, well-ordered nanostructures in the range of 5-30 nm. However, the self-assembled BCP patterns remain limited to ... ...

    Abstract The templated self-assembly of block copolymers (BCPs) with a high Flory-Huggins interaction parameter (χ) can effectively create ultrafine, well-ordered nanostructures in the range of 5-30 nm. However, the self-assembled BCP patterns remain limited to possible morphological geometries and materials. Here, we introduce a novel and useful self-assembly method of di-BCP blends capable of generating diverse hybrid nanostructures consisting of oxide and metal materials through the rapid microphase separation of A-B/B-C BCP blends. We successfully obtained various hybridized BCP morphologies which cannot be acquired from a single di-BCP, such as hexagonally arranged hybrid dot and dot-in-hole patterns by controlling the mixing ratios of the solvents with a binary solvent annealing process. Furthermore, we demonstrate how the binary solvent vapor annealing process can provide a wide range of pattern geometries to di-BCP blends, showing a well-defined spontaneous one-to-one accommodation in dot-in-hole nanostructures. Specifically, we show clearly how the self-assembled BCPs can be functionalized via selective reduction and/or an oxidation process, resulting in the excellent positioning of confined silica nanodots into each nanospace of a Pt mesh. These results suggest a new method to achieve the pattern formation of more diverse and complex hybrid nanostructures using various blended BCPs.
    Language English
    Publishing date 2019-07-25
    Publishing country England
    Document type Journal Article
    ZDB-ID 2515664-0
    ISSN 2040-3372 ; 2040-3364
    ISSN (online) 2040-3372
    ISSN 2040-3364
    DOI 10.1039/c9nr04038b
    Database MEDical Literature Analysis and Retrieval System OnLINE

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