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  1. Article ; Online: Repeated Low-level Red-light Therapy: The Next Wave in Myopia Management?

    Salzano, Aaron D / Khanal, Safal / Cheung, Nathan L / Weise, Katherine K / Jenewein, Erin C / Horn, Darryl M / Mutti, Donald O / Gawne, Timothy J

    Optometry and vision science : official publication of the American Academy of Optometry

    2023  Volume 100, Issue 12, Page(s) 812–822

    Abstract: Significance: Exposure to long-wavelength light has been proposed as a potential intervention to slow myopia progression in children. This article provides an evidence-based review of the safety and myopia control efficacy of red light and discusses the ...

    Abstract Significance: Exposure to long-wavelength light has been proposed as a potential intervention to slow myopia progression in children. This article provides an evidence-based review of the safety and myopia control efficacy of red light and discusses the potential mechanisms by which red light may work to slow childhood myopia progression.The spectral composition of the ambient light in the visual environment has powerful effects on eye growth and refractive development. Studies in mammalian and primate animal models (macaque monkeys and tree shrews) have shown that daily exposure to long-wavelength (red or amber) light promotes slower eye growth and hyperopia development and inhibits myopia induced by form deprivation or minus lens wear. Consistent with these results, several recent randomized controlled clinical trials in Chinese children have demonstrated that exposure to red light for 3 minutes twice a day significantly reduces myopia progression and axial elongation. These findings have collectively provided strong evidence for the potential of using red light as a myopia control intervention in clinical practice. However, several questions remain unanswered. In this article, we review the current evidence on the safety and efficacy of red light as a myopia control intervention, describe potential mechanisms, and discuss some key unresolved issues that require consideration before red light can be broadly translated into myopia control in children.
    MeSH term(s) Animals ; Child ; Humans ; Eye ; Myopia/prevention & control ; Refraction, Ocular ; Hyperopia ; Tupaiidae ; Phototherapy
    Language English
    Publishing date 2023-10-25
    Publishing country United States
    Document type Review ; Journal Article
    ZDB-ID 1001706-9
    ISSN 1538-9235 ; 1040-5488
    ISSN (online) 1538-9235
    ISSN 1040-5488
    DOI 10.1097/OPX.0000000000002083
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Rcl1 protein, a novel nuclease for 18 S ribosomal RNA production.

    Horn, Darryl M / Mason, Saundra L / Karbstein, Katrin

    The Journal of biological chemistry

    2011  Volume 286, Issue 39, Page(s) 34082–34087

    Abstract: In all forms of life, rRNAs for the small and large ribosomal subunit are co-transcribed as a single transcript. Although this ensures the equimolar production of rRNAs, it requires the endonucleolytic separation of pre-rRNAs to initiate rRNA production. ...

    Abstract In all forms of life, rRNAs for the small and large ribosomal subunit are co-transcribed as a single transcript. Although this ensures the equimolar production of rRNAs, it requires the endonucleolytic separation of pre-rRNAs to initiate rRNA production. In yeast, processing of the primary transcript encoding 18 S, 5.8 S, and 25 S rRNAs has been studied extensively. Nevertheless, most nucleases remain to be identified. Here, we show that Rcl1, conserved in all eukaryotes, cleaves pre-rRNA at so-called site A(2), a co-transcriptional cleavage step that separates rRNAs destined for the small and large subunit. Recombinant Rcl1 cleaves pre-rRNA mimics at site A(2) in a reaction that is sensitive to nearby RNA mutations that inhibit cleavage in vivo. Furthermore, mutations in Rcl1 disrupt rRNA processing at site A(2) in vivo and in vitro. Together, these results demonstrate that the role of Rcl1 in eukaryotic pre-rRNA processing is identical to that of RNase III in bacteria: to co-transcriptionally separate the pre-rRNAs destined for the small and large subunit. Furthermore, because Rcl1 has no homology to other known endonucleases, these data also establish a novel class of nucleases.
    MeSH term(s) Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; RNA Precursors/genetics ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional/physiology ; RNA, Fungal/genetics ; RNA, Fungal/metabolism ; RNA, Ribosomal, 18S/genetics ; RNA, Ribosomal, 18S/metabolism ; Ribonucleases/genetics ; Ribonucleases/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Nuclear Proteins ; RCL1 protein, S cerevisiae ; RNA Precursors ; RNA, Fungal ; RNA, Ribosomal, 18S ; Saccharomyces cerevisiae Proteins ; Ribonucleases (EC 3.1.-)
    Language English
    Publishing date 2011-08-17
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M111.268649
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mia40 Protein Serves as an Electron Sink in the Mia40-Erv1 Import Pathway.

    Neal, Sonya E / Dabir, Deepa V / Tienson, Heather L / Horn, Darryl M / Glaeser, Kathrin / Ogozalek Loo, Rachel R / Barrientos, Antoni / Koehler, Carla M

    The Journal of biological chemistry

    2015  Volume 290, Issue 34, Page(s) 20804–20814

    Abstract: A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. ... ...

    Abstract A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously. However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation. In this study, we have addressed the oxidation of Tim13 in vitro and in organello. Reductants such as glutathione and ascorbate inhibited both the oxidation of the substrate Tim13 in vitro and the import of Tim13 and Cmc1 into isolated mitochondria. In addition, a ternary complex consisting of Erv1, Mia40, and substrate, linked by disulfide bonds, was not detected in vitro. Instead, Mia40 accepted six electrons from substrates, and this fully reduced Mia40 was sensitive to protease, indicative of conformational changes in the structure. Mia40 in mitochondria from the erv1-101 mutant was also trapped in a completely reduced state, demonstrating that Mia40 can accept up to six electrons as substrates are imported. Therefore, these studies support that Mia40 functions as an electron sink to facilitate the insertion of two disulfide bonds into substrates.
    MeSH term(s) Ascorbic Acid/pharmacology ; Disulfides/chemistry ; Disulfides/metabolism ; Electrons ; Gene Expression Regulation, Fungal ; Glutathione/pharmacology ; Metallochaperones/genetics ; Metallochaperones/metabolism ; Mitochondria/drug effects ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mutation ; Oxidation-Reduction ; Oxidoreductases Acting on Sulfur Group Donors/genetics ; Oxidoreductases Acting on Sulfur Group Donors/metabolism ; Plasmids/chemistry ; Plasmids/metabolism ; Protein Transport ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Reducing Agents/pharmacology ; Saccharomyces cerevisiae/drug effects ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
    Chemical Substances CMC1 protein, S cerevisiae ; Disulfides ; MIA40 protein, S cerevisiae ; Metallochaperones ; Mitochondrial Membrane Transport Proteins ; Mitochondrial Proteins ; Recombinant Proteins ; Reducing Agents ; Saccharomyces cerevisiae Proteins ; TIM13 protein, S cerevisiae ; Oxidoreductases Acting on Sulfur Group Donors (EC 1.8.-) ; ERV1 protein, S cerevisiae (EC 1.8.3.2) ; Glutathione (GAN16C9B8O) ; Ascorbic Acid (PQ6CK8PD0R)
    Language English
    Publishing date 2015-06-17
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M115.669440
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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