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  1. Article: De novo

    Kang, Sang-Ho / Lee, Woo-Haeng / Sim, Joon-Soo / Thaku, Niha / Chang, Saemin / Hong, Jong-Pil / Oh, Tae-Jin

    Frontiers in plant science

    2022  Volume 12, Page(s) 773553

    Abstract: ... Senna ... ...

    Abstract Senna occidentalis
    Language English
    Publishing date 2022-01-03
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2613694-6
    ISSN 1664-462X
    ISSN 1664-462X
    DOI 10.3389/fpls.2021.773553
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Systemic Expression of Genes Involved in the Plant Defense Response Induced by Wounding in

    Kang, Ji-Nam / Lee, Woo-Haeng / Won, So Youn / Chang, Saemin / Hong, Jong-Pil / Oh, Tae-Jin / Lee, Si Myung / Kang, Sang-Ho

    International journal of molecular sciences

    2021  Volume 22, Issue 18

    Abstract: Wounds in tissues provide a pathway of entry for pathogenic fungi and bacteria in plants. Plants respond to wounding by regulating the expression of genes involved in their defense mechanisms. To analyze this response, we investigated the defense-related ...

    Abstract Wounds in tissues provide a pathway of entry for pathogenic fungi and bacteria in plants. Plants respond to wounding by regulating the expression of genes involved in their defense mechanisms. To analyze this response, we investigated the defense-related genes induced by wounding in the leaves of
    MeSH term(s) Acetates/pharmacology ; Cyclopentanes/pharmacology ; Ethylenes/chemistry ; Fabaceae/genetics ; Gene Expression Profiling ; Gene Expression Regulation, Plant/drug effects ; Genes, Plant ; Kaempferols/pharmacology ; Oxylipins/pharmacology ; Plant Diseases ; Plant Growth Regulators/pharmacology ; Plant Immunity ; Plant Leaves/metabolism ; Plant Proteins/genetics ; Plants/drug effects ; Quercetin/pharmacology ; RNA-Seq
    Chemical Substances Acetates ; Cyclopentanes ; Ethylenes ; Kaempferols ; Oxylipins ; Plant Growth Regulators ; Plant Proteins ; jasmonic acid (6RI5N05OWW) ; kaempferol (731P2LE49E) ; ethylene (91GW059KN7) ; Quercetin (9IKM0I5T1E)
    Language English
    Publishing date 2021-09-17
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms221810073
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Non-redox-active small-molecules can accelerate oxidative protein folding by novel mechanisms.

    Fink, Matthew / Nieves, Paul / Chang, Saemin / Narayan, Mahesh

    Biophysical chemistry

    2008  Volume 132, Issue 2-3, Page(s) 104–109

    Abstract: Multi-disulfide-bond-containing proteins acquire their native structures through an oxidative folding reaction which involves formation of native disulfide bonds through thiol-disulfide exchange reactions between cysteines and disulfides coupled to a ... ...

    Abstract Multi-disulfide-bond-containing proteins acquire their native structures through an oxidative folding reaction which involves formation of native disulfide bonds through thiol-disulfide exchange reactions between cysteines and disulfides coupled to a conformational folding event. Oxidative folding rates of the four-disulfide-bond-containing protein bovine pancreatic ribonuclease A (RNase A) in the presence of the synthetic redox-active molecule, (+/-)-trans-1,2-bis(2-mercaptoacetamido)cyclohexane (BMC), and in combination with non-redox-active trimethylamine-N-oxide (TMAO), and trifluorethanol were determined by HPLC analysis. The data indicate that regeneration of RNase A is enhanced 2-fold by BMC (50 microM) and 3-fold upon addition of TMAO (0.2 M) and TFE (3% v/v) relative to control experiments performed in the absence of small-molecules. Examination of the native tendency of the fully-reduced polypeptide and the stability of key folding intermediates suggests that the increased oxidative folding rate can be attributed to native-like elements induced within the fully-reduced polypeptide and the stabilization of native-like species by added non-redox-active molecules.
    MeSH term(s) Animals ; Cattle ; Disulfides ; Enzyme Stability ; Kinetics ; Organic Chemicals ; Oxidation-Reduction ; Protein Folding ; Ribonuclease, Pancreatic/chemistry
    Chemical Substances Disulfides ; Organic Chemicals ; Ribonuclease, Pancreatic (EC 3.1.27.5)
    Language English
    Publishing date 2008-02
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 185052-0
    ISSN 1873-4200 ; 0301-4622
    ISSN (online) 1873-4200
    ISSN 0301-4622
    DOI 10.1016/j.bpc.2007.10.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1147: 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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  4. Article: Relationship between sequence determinants of stability for two natural homologous proteins with different folds.

    Van Dorn, Laura O / Newlove, Tracey / Chang, Saemin / Ingram, Wendy M / Cordes, Matthew H J

    Biochemistry

    2006  Volume 45, Issue 35, Page(s) 10542–10553

    Abstract: In the Cro protein family, an evolutionary change in secondary structure has converted an alpha-helical fold to a mixture of alpha-helix and beta-sheet. P22 Cro and lambda Cro represent the ancestral all-alpha and descendant alpha+beta folds, ... ...

    Abstract In the Cro protein family, an evolutionary change in secondary structure has converted an alpha-helical fold to a mixture of alpha-helix and beta-sheet. P22 Cro and lambda Cro represent the ancestral all-alpha and descendant alpha+beta folds, respectively. The major structural differences between these proteins are at the C-terminal end of the domain (residues 34-56), where two alpha-helices in P22 Cro align with two beta-strands in lambda Cro. We sought to assess the possibility that smooth evolutionary transitions could have converted the all-alpha structure to the alpha+beta structure through sequences that could adopt both folds. First, we used scanning mutagenesis to identify and compare patterns of key stabilizing residues in the C-terminal regions of both P22 Cro and lambda Cro. These patterns exhibited little similarity to each other, with structurally important residues in the two proteins most often occurring at different sequence positions. Second, "hybrid scanning" studies, involving replacement of each wild-type residue in P22 Cro with the aligned wild-type residue in lambda Cro and vice versa, revealed five or six residues in each protein that strongly destabilized the other. These results suggest that key stability determinants for each Cro fold are quite different and that the P22 Cro sequence strongly favors the all-alpha structure while the lambda Cro sequence strongly favors the alpha+beta structure. Nonetheless, we were able to design a "structurally ambivalent" sequence fragment (SASF1), which corresponded to residues 39-56 and simultaneously incorporated most key stabilizing residues for both P22 Cro and lambda Cro. NMR experiments showed SASF1 to stably fold as a beta-hairpin when incorporated into the lambda Cro sequence but as a pair of alpha-helices when incorporated into P22 Cro.
    MeSH term(s) Alanine/genetics ; Amino Acid Motifs ; Amino Acid Sequence ; DNA-Binding Proteins/genetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis ; Protein Folding ; Protein Structure, Tertiary ; Proteins/chemistry ; Repressor Proteins/genetics ; Sequence Homology, Amino Acid ; Structural Homology, Protein ; Viral Proteins/genetics ; Viral Regulatory and Accessory Proteins
    Chemical Substances DNA-Binding Proteins ; Proteins ; Repressor Proteins ; Viral Proteins ; Viral Regulatory and Accessory Proteins ; phage repressor proteins ; Alanine (OF5P57N2ZX)
    Language English
    Publishing date 2006-09-05
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/bi060853p
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 217: 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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