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  1. Article ; Online: IL9 Polarizes Macrophages to M1 and Induces the Infiltration of Antitumor Immune Cells via MIP-1 and CXCR3 Chemokines.

    Do-Thi, Van Anh / Park, Sang Min / Park, Song Mi / Jeong, Hye Jin / Cho, Geunyoung / An, Hyun-Jung / Kim, Young Sang / Lee, Hayyoung / Lee, Jie-Oh

    Cancer research communications

    2023  Volume 3, Issue 1, Page(s) 80–96

    Abstract: Tumor-associated macrophages (TAM) are involved in tumor progression, metastasis, and immunosuppression. Because TAMs are highly plastic and could alter their phenotypes to proinflammatory M1 in response to environmental stimuli, reeducating TAMs has ... ...

    Abstract Tumor-associated macrophages (TAM) are involved in tumor progression, metastasis, and immunosuppression. Because TAMs are highly plastic and could alter their phenotypes to proinflammatory M1 in response to environmental stimuli, reeducating TAMs has emerged as a promising approach to overcoming the challenges of solid cancer treatment. This study investigated the effect of IL9 on macrophage M1 polarization and verified its antitumor potential to retrain TAMs and promote chemokine secretion. We demonstrated that IL9 stimulated macrophage proliferation and polarized them toward the proinflammatory M1 phenotype in an IFNγ-dependent manner. Tumor-localized IL9 also polarized TAMs toward M1
    Significance: These findings clarified the effect of IL9 on macrophage M1 polarization and verified its antitumor potential through retraining TAMs and chemokine secretion.
    MeSH term(s) Mice ; Animals ; Interleukin-9/pharmacology ; Macrophages ; Melanoma/pathology ; Macrophage Activation ; Chemokines/pharmacology ; Tumor Microenvironment
    Chemical Substances Interleukin-9 ; Chemokines
    Language English
    Publishing date 2023-01-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2767-9764
    ISSN (online) 2767-9764
    DOI 10.1158/2767-9764.CRC-22-0246
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Application of antihelix antibodies in protein structure determination.

    Kim, Ji Won / Kim, Songwon / Lee, Haerim / Cho, Geunyoung / Kim, Sun Chang / Lee, Hayyoung / Jin, Mi Sun / Lee, Jie-Oh

    Proceedings of the National Academy of Sciences of the United States of America

    2019  Volume 116, Issue 36, Page(s) 17786–17791

    Abstract: Antibodies are indispensable tools in protein engineering and structural biology. Antibodies suitable for structural studies should recognize the 3-dimensional (3D) conformations of target proteins. Generating such antibodies and characterizing their ... ...

    Abstract Antibodies are indispensable tools in protein engineering and structural biology. Antibodies suitable for structural studies should recognize the 3-dimensional (3D) conformations of target proteins. Generating such antibodies and characterizing their complexes with antigens take a significant amount of time and effort. Here, we show that we can expand the application of well-characterized antibodies by "transplanting" the epitopes that they recognize to proteins with completely different structures and sequences. Previously, several antibodies have been shown to recognize the alpha-helical conformation of antigenic peptides. We demonstrate that these antibodies can be made to bind to a variety of unrelated "off-target" proteins by modifying amino acids in the preexisting alpha helices of such proteins. Using X-ray crystallography, we determined the structures of the engineered protein-antibody complexes. All of the antibodies bound to the epitope-transplanted proteins, forming accurately predictable structures. Furthermore, we showed that binding of these antihelix antibodies to the engineered target proteins can modulate their catalytic activities by trapping them in selected functional states. Our method is simple and efficient, and it will have applications in protein X-ray crystallography, electron microscopy, and nanotechnology.
    MeSH term(s) Crystallography, X-Ray ; Epitopes/chemistry ; Humans ; Protein Conformation, alpha-Helical ; Proteins/chemistry ; Single-Chain Antibodies/chemistry
    Chemical Substances Epitopes ; Proteins ; Single-Chain Antibodies
    Language English
    Publishing date 2019-08-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1910080116
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Attachment of flagellin enhances the immunostimulatory activity of a hemagglutinin-ferritin nano-cage.

    Lee, Emerson B / Jeon, Hyung-Min / Kim, Chang-Ung / Park, Sang M / Cho, Geunyoung / Kim, Hyun-Jin / Kim, Youngjin / Kim, Doo-Jin / Kim, Young S / Lee, Hayyoung / Lee, Jie-Oh

    Nanomedicine : nanotechnology, biology, and medicine

    2019  Volume 17, Page(s) 223–235

    Abstract: Hemagglutinin (HA) displayed on a ferritin nano-cage has been shown to be effective in generating a potent immune response against a broad range of influenza infections. Here, we showed that conjugation of flagellin together with HA to the exterior ... ...

    Abstract Hemagglutinin (HA) displayed on a ferritin nano-cage has been shown to be effective in generating a potent immune response against a broad range of influenza infections. Here, we showed that conjugation of flagellin together with HA to the exterior surface of the ferritin cage greatly enhanced not only the humoral immune response in mice but also antigen-specific T cell responses that include Th1 cytokine secretion. The effect of flagellin remained essentially unchanged when the molar ratio of flagellin to HA was reduced from 1:1 to 1:3. Injection of the ferritin-HA-flagellin cage provided protection against lethal virus challenge in mice. We used a small immunoglobulin fragment V
    MeSH term(s) Adjuvants, Immunologic/chemistry ; Adjuvants, Immunologic/pharmacology ; Animals ; Cell Line ; Female ; Ferritins/chemistry ; Ferritins/pharmacology ; Flagellin/chemistry ; Flagellin/pharmacology ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus/pharmacology ; Humans ; Immunity, Cellular/drug effects ; Immunity, Humoral/drug effects ; Influenza A virus/chemistry ; Mice ; Mice, Inbred BALB C ; Nanostructures/chemistry ; Salmonella typhimurium/chemistry
    Chemical Substances Adjuvants, Immunologic ; Hemagglutinin Glycoproteins, Influenza Virus ; Flagellin (12777-81-0) ; Ferritins (9007-73-2)
    Language English
    Publishing date 2019-01-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2183417-9
    ISSN 1549-9642 ; 1549-9634
    ISSN (online) 1549-9642
    ISSN 1549-9634
    DOI 10.1016/j.nano.2019.01.012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Higd-1a interacts with Opa1 and is required for the morphological and functional integrity of mitochondria.

    An, Hyun-Jung / Cho, Geunyoung / Lee, Jie-Oh / Paik, Sang-Gi / Kim, Young Sang / Lee, Hayyoung

    Proceedings of the National Academy of Sciences of the United States of America

    2013  Volume 110, Issue 32, Page(s) 13014–13019

    Abstract: The activity and morphology of mitochondria are maintained by dynamic fusion and fission processes regulated by a group of proteins residing in, or attached to, their inner and outer membranes. Hypoxia-induced gene domain protein-1a (Higd-1a)/HIMP1-a/ ... ...

    Abstract The activity and morphology of mitochondria are maintained by dynamic fusion and fission processes regulated by a group of proteins residing in, or attached to, their inner and outer membranes. Hypoxia-induced gene domain protein-1a (Higd-1a)/HIMP1-a/HIG1, a mitochondrial inner membrane protein, plays a role in cell survival under hypoxic conditions. In the present study, we showed that Higd-1a depletion resulted in mitochondrial fission, depletion of mtDNA, disorganization of cristae, and growth retardation. We demonstrated that Higd-1a functions by specifically binding to Optic atrophy 1 (Opa1), a key element in fusion of the inner membrane. In the absence of Higd-1a, Opa1 was cleaved, resulting in the loss of its long isoforms and accumulation of small soluble forms. The small forms of Opa1 do not interact with Higd-1a, suggesting that a part of Opa1 in or proximal to the membrane is required for that interaction. Opa1 cleavage, mitochondrial fission, and cell death induced by dissipation of the mitochondrial membrane potential were significantly inhibited by ectopic expression of Higd-1a. Furthermore, growth inhibition due to Higd-1a depletion could be overcome by overexpression of a noncleavable form of Opa1. Collectively, our observations demonstrate that Higd-1a inhibits Opa1 cleavage and is required for mitochondrial fusion by virtue of its interaction with Opa1.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Blotting, Western ; GTP Phosphohydrolases/genetics ; GTP Phosphohydrolases/metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Membrane Potential, Mitochondrial/genetics ; Membrane Potential, Mitochondrial/physiology ; Microscopy, Electron, Transmission ; Microscopy, Fluorescence ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Protein Binding ; RNA Interference
    Chemical Substances HIGD1A protein, human ; Intracellular Signaling Peptides and Proteins ; Mitochondrial Proteins ; Neoplasm Proteins ; Adenosine Triphosphate (8L70Q75FXE) ; GTP Phosphohydrolases (EC 3.6.1.-) ; OPA1 protein, human (EC 3.6.1.-)
    Language English
    Publishing date 2013-07-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1307170110
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article ; Online: Crystal structures of mono- and bi-specific diabodies and reduction of their structural flexibility by introduction of disulfide bridges at the Fv interface.

    Kim, Jin Hong / Song, Dong Hyun / Youn, Suk-Jun / Kim, Ji Won / Cho, Geunyoung / Kim, Sun Chang / Lee, Hayyoung / Jin, Mi Sun / Lee, Jie-Oh

    Scientific reports

    2016  Volume 6, Page(s) 34515

    Abstract: Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Diabodies are engineered antibody fragments that are composed of two Fv domains connected by short peptide linkers. ... ...

    Abstract Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Diabodies are engineered antibody fragments that are composed of two Fv domains connected by short peptide linkers. They are attractive candidates for mediators in assembling protein nano-structures because they can simultaneously bind to two different proteins and are rigid enough to be crystallized. However, comparison of previous crystal structures demonstrates that there is substantial structural diversity in the Fv interface region of diabodies and, therefore, reliable prediction of its structure is not trivial. Here, we present the crystal structures of ten mono- and bi-specific diabodies. We found that changing an arginine residue in the Fv interface to threonine greatly reduced the structural diversity of diabodies. We also found that one of the bispecific diabodies underwent an unexpected process of chain swapping yielding a non-functional monospecific diabody. In order to further reduce structural flexibility and prevent chain shuffling, we introduced disulfide bridges in the Fv interface regions. The disulfide-bridged diabodies have rigid and predictable structures and may have applications in crystallizing proteins, analyzing cryo-electron microscopic images and building protein nano-assemblies.
    Language English
    Publishing date 2016-09-29
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/srep34515
    Database MEDical Literature Analysis and Retrieval System OnLINE

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