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  1. Article ; Online: Non-Fullerene Acceptors with Benzodithiophene-Based Fused Planar Ring Cores for Organic Solar Cells.

    Yang, Ning / Ryu, Du Hyeon / Lee, Suha / Bai, Yongqi / Kim, Seo Il / Seo, Ji Hoon / Song, Chang Eun / Hwang, Do-Hoon

    ACS applied materials & interfaces

    2023  Volume 15, Issue 17, Page(s) 21306–21313

    Abstract: Fused aromatic rings are widely employed in organic solar cell (OSC) materials due to their planarity and rigidity. Here, we designed and synthesized four two-dimensional non-fullerene acceptors, D6-4F, D6-4Cl, DTT-4F, and DTT-4Cl, based on two new fused ...

    Abstract Fused aromatic rings are widely employed in organic solar cell (OSC) materials due to their planarity and rigidity. Here, we designed and synthesized four two-dimensional non-fullerene acceptors, D6-4F, D6-4Cl, DTT-4F, and DTT-4Cl, based on two new fused planar ring structures of f-DTBDT-C6 and f-DTTBDT. Owing to the desirable phase separation formed in the blend films and the higher energy levels induced by the extra alkyl groups, PM6:D6-4F-based devices achieved a high
    Language English
    Publishing date 2023-04-20
    Publishing country United States
    Document type Journal Article
    ISSN 1944-8252
    ISSN (online) 1944-8252
    DOI 10.1021/acsami.3c01626
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: N-Glycosylation of secretion enhancer peptide as influencing factor for the secretion of target proteins from Saccharomyces cerevisiae.

    Han, Kyoung Sim / Kim, Seo Il / Choi, Seong Il / Seong, Baik Lin

    Biochemical and biophysical research communications

    2005  Volume 337, Issue 2, Page(s) 557–562

    Abstract: hIL-1beta-derived polypeptide, when fused to the N-terminal end of target proteins, exerts a potent secretion enhancer function in Saccharomyces cerevisiae. We investigated the effect of N-glycosylation of the secretion enhancer peptide on the secretion ... ...

    Abstract hIL-1beta-derived polypeptide, when fused to the N-terminal end of target proteins, exerts a potent secretion enhancer function in Saccharomyces cerevisiae. We investigated the effect of N-glycosylation of the secretion enhancer peptide on the secretion of target proteins. The N-terminal 24 amino acids (Ser5-Ala28) of human interleukin 1beta (hIL-1beta) and interleukin 1 receptor antagonist (IL-1ra) were used as secretion enhancer for synthesizing recombinant human granulocyte-colony stimulating factor (rhG-CSF) from S. cerevisiae. The mutation of potential N-glycosylation site, by substituting Gln for either Asn7 of N-terminal 24 amino acids of hIL-1beta (Asn7Gln) or Asn84 of IL-1ra (Asn84Gln), resulted in a dramatic reduction of rhG-CSF secretion efficiency. In contrast, the mutant containing an additional N-glycosylation site on the N-terminal 24 amino acids of hIL-1beta (Gln15Asn) secreted twice as much rhG-CSF into culture media as wild type hIL-1beta. These results show that N-glycosylation of the secretion enhancer peptide plays an important role in increasing the secretion efficiency of the downstream target proteins. The results also suggest that judicious choice of enhancer peptide and the control of its glycosylation could be of general utility for secretory production of heterologous proteins from S. cerevisiae.
    MeSH term(s) Down-Regulation ; Glycosylation ; Granulocyte Colony-Stimulating Factor/genetics ; Granulocyte Colony-Stimulating Factor/metabolism ; Granulocyte Colony-Stimulating Factor/secretion ; Humans ; Interleukin-1/genetics ; Interleukin-1/metabolism ; Mutation ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Receptors, Interleukin-1/antagonists & inhibitors ; Receptors, Interleukin-1/genetics ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Recombinant Fusion Proteins/secretion ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Time Factors
    Chemical Substances Interleukin-1 ; Peptides ; Receptors, Interleukin-1 ; Recombinant Fusion Proteins ; Granulocyte Colony-Stimulating Factor (143011-72-7)
    Language English
    Publishing date 2005-11-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2005.09.089
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Comparison of the Intraperitoneal, Retroorbital and per Oral Routes for F-18 FDG Administration as Effective Alternatives to Intravenous Administration in Mouse Tumor Models Using Small Animal PET/CT Studies.

    Kim, Chulhan / Kim, In Hye / Kim, Seo-Il / Kim, Young Sang / Kang, Se Hun / Moon, Seung Hwan / Kim, Tae-Sung / Kim, Seok-Ki

    Nuclear medicine and molecular imaging

    2011  Volume 45, Issue 3, Page(s) 169–176

    Abstract: Purpose: We compared alternative routes for (18)F-fluorodeoxyglucose (FDG) administration, such as the retroorbital (RO), intraperitoneal (IP) and per oral (PO) routes, with the intravenous (IV) route in normal tissues and tumors of mice.: Materials ... ...

    Abstract Purpose: We compared alternative routes for (18)F-fluorodeoxyglucose (FDG) administration, such as the retroorbital (RO), intraperitoneal (IP) and per oral (PO) routes, with the intravenous (IV) route in normal tissues and tumors of mice.
    Materials and methods: CRL-1642 (ATCC, Lewis lung carcinoma) cells were inoculated in female BALB/c-nu/nu mice 6 to 10 weeks old. When the tumor grew to about 9 mm in diameter, positron emission tomography (PET) scans were performed after FDG administration via the RO, IP, PO or IV route. Additional serial PET scans were performed using the RO, IV or IP route alternatively from 5 to 29 days after the tumor cell injection.
    Results: There was no significant difference in the FDG uptake in normal tissues at 60 min after FDG administration via RO, IP and IV routes. PO administration, however, showed delayed distribution and unwanted high gastrointestinal uptake. Tumoral uptake of FDG showed a similar temporal pattern and increased until 60 min after FDG administration in the RO, IP and IV injection groups. In the PO administration group, tumoral uptake was delayed and reduced. There was no statistical difference among the RO, IP and IV administration groups for additional serial PET scans.
    Conclusion: RO administration is an effective alternative route to IV administration for mouse FDG PET scans using normal mice and tumor models. In addition, IP administration can be a practical alternative in the late phase, although the initial uptake is lower than those in the IV and RO groups.
    Language English
    Publishing date 2011-05-27
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2541855-5
    ISSN 1869-3482 ; 1869-3474
    ISSN (online) 1869-3482
    ISSN 1869-3474
    DOI 10.1007/s13139-011-0087-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Protein solubility and folding enhancement by interaction with RNA.

    Choi, Seong Il / Han, Kyoung Sim / Kim, Chul Woo / Ryu, Ki-Sun / Kim, Byung Hee / Kim, Kyun-Hwan / Kim, Seo-Il / Kang, Tae Hyun / Shin, Hang-Cheol / Lim, Keo-Heun / Kim, Hyo Kyung / Hyun, Jeong-Min / Seong, Baik L

    PloS one

    2008  Volume 3, Issue 7, Page(s) e2677

    Abstract: While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated ...

    Abstract While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated by interaction with RNA. When an RNA-binding module is placed at the N-terminus of aggregation-prone target proteins, this module, upon binding with RNA, further promotes the solubility of passenger proteins, potentially leading to enhancement of proper protein folding. Studies on in vitro refolding in the presence of RNA, coexpression of RNA molecules in vivo and the mutants with impaired RNA binding ability suggests that RNA can exert chaperoning effect on their bound proteins. The results suggest that RNA binding could affect the overall kinetic network of protein folding pathway in favor of productive folding over off-pathway aggregation. In addition, the RNA binding-mediated solubility enhancement is extremely robust for increasing soluble yield of passenger proteins and could be usefully implemented for high-throughput protein expression for functional and structural genomic research initiatives. The RNA-mediated chaperone type presented here would give new insights into de novo folding in vivo.
    MeSH term(s) Cytosol/metabolism ; DNA/chemistry ; Enhancer Elements, Genetic ; Humans ; Models, Genetic ; Molecular Chaperones/chemistry ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; Protein Binding ; Protein Denaturation ; Protein Folding ; Protein Structure, Tertiary ; Proteins/chemistry ; RNA/chemistry ; Solubility
    Chemical Substances Molecular Chaperones ; Proteins ; RNA (63231-63-0) ; DNA (9007-49-2)
    Language English
    Publishing date 2008-07-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0002677
    Database MEDical Literature Analysis and Retrieval System OnLINE

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