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  1. AU="Abdullahi, Akilu"
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  1. Article: Visualisation of ribosomes in

    Singh, Anand K / Abdullahi, Akilu / Soller, Matthias / David, Alexandre / Brogna, Saverio

    Biology open

    2020  Volume 8, Issue 12

    Abstract: The distribution of assembled, and potentially translating, ribosomes within cells can be visualised ... ...

    Abstract The distribution of assembled, and potentially translating, ribosomes within cells can be visualised in
    MeSH term(s) Animals ; Axons/metabolism ; Drosophila/genetics ; Drosophila/metabolism ; Fluorescent Antibody Technique ; Humans ; Molecular Imaging/methods ; Molecular Structure ; Neurons/metabolism ; Photoreceptor Cells/metabolism ; Ribosomal Proteins/metabolism ; Ribosomes/chemistry ; Ribosomes/metabolism
    Chemical Substances Ribosomal Proteins
    Language English
    Publishing date 2020-01-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2632264-X
    ISSN 2046-6390
    ISSN 2046-6390
    DOI 10.1242/bio.047233
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Recent studies implicate the nucleolus as the major site of nuclear translation.

    McLeod, Tina / Abdullahi, Akilu / Li, Min / Brogna, Saverio

    Biochemical Society transactions

    2014  Volume 42, Issue 4, Page(s) 1224–1228

    Abstract: The nucleolus is the most prominent morphological feature within the nucleus of eukaryotic cells and is best known for its role in ribosome biogenesis. It forms around highly transcribed ribosomal RNA gene repeats which yield precursor rRNAs that are co- ... ...

    Abstract The nucleolus is the most prominent morphological feature within the nucleus of eukaryotic cells and is best known for its role in ribosome biogenesis. It forms around highly transcribed ribosomal RNA gene repeats which yield precursor rRNAs that are co-transcriptionally processed, folded and, while still within the nucleolus, associate with most of the ribosomal proteins. The nucleolus is therefore often thought of as a factory for making ribosomal subunits, which are exported as inactive precursors to the cytoplasm where late maturation makes them capable of mRNA binding and translation initiation. However, recent studies have shown substantial evidence for the presence of functional, translation competent ribosomal subunits within the nucleus, particularly in the nucleolus. These observations raise the intriguing possibility that the nucleolus, as well as being a ribosome factory, is also an important nuclear protein-synthesis plant.
    MeSH term(s) Animals ; Cell Nucleolus/metabolism ; Cell Nucleus/metabolism ; Humans ; Ribosomal Proteins/metabolism ; Ribosome Subunits/metabolism ; Ribosomes/metabolism
    Chemical Substances Ribosomal Proteins
    Language English
    Publishing date 2014-08
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/BST20140062
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 944: 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: Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus.

    Al-Jubran, Khalid / Wen, Jikai / Abdullahi, Akilu / Roy Chaudhury, Subhendu / Li, Min / Ramanathan, Preethi / Matina, Annunziata / De, Sandip / Piechocki, Kim / Rugjee, Kushal Nivriti / Brogna, Saverio

    RNA (New York, N.Y.)

    2013  Volume 19, Issue 12, Page(s) 1669–1683

    Abstract: In eukaryotes the 40S and 60S ribosomal subunits are assembled in the nucleolus, but there appear to be mechanisms preventing mRNA binding, 80S formation, and initiation of translation in the nucleus. To visualize association between ribosomal subunits, ... ...

    Abstract In eukaryotes the 40S and 60S ribosomal subunits are assembled in the nucleolus, but there appear to be mechanisms preventing mRNA binding, 80S formation, and initiation of translation in the nucleus. To visualize association between ribosomal subunits, we tagged pairs of Drosophila ribosomal proteins (RPs) located in different subunits with mutually complementing halves of fluorescent proteins. Pairs of tagged RPs expected to interact, or be adjacent in the 80S structure, showed strong fluorescence, while pairs that were not in close proximity did not. Moreover, the complementation signal is found in ribosomal fractions and it was enhanced by translation elongation inhibitors and reduced by initiation inhibitors. Our technique achieved 80S visualization both in cultured cells and in fly tissues in vivo. Notably, while the main 80S signal was in the cytoplasm, clear signals were also seen in the nucleolus and at other nuclear sites. Furthermore, we detected rapid puromycin incorporation in the nucleolus and at transcription sites, providing an independent indication of functional 80S in the nucleolus and 80S association with nascent transcripts.
    MeSH term(s) Animals ; Bacterial Proteins/biosynthesis ; Cell Line ; Cell Nucleolus/metabolism ; Cell Nucleus/metabolism ; Drosophila Proteins/metabolism ; Drosophila melanogaster/cytology ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Luminescent Proteins/biosynthesis ; Microscopy, Fluorescence ; Peptidyl Transferases/metabolism ; Polytene Chromosomes/metabolism ; Protein Binding ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/biosynthesis ; Ribosomal Proteins/metabolism ; Ribosomes/metabolism ; Transcription, Genetic
    Chemical Substances Bacterial Proteins ; Drosophila Proteins ; Luminescent Proteins ; RNA, Messenger ; Recombinant Fusion Proteins ; Ribosomal Proteins ; yellow fluorescent protein, Bacteria ; Peptidyl Transferases (EC 2.3.2.12)
    Language English
    Publishing date 2013-10-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1241540-6
    ISSN 1469-9001 ; 1355-8382
    ISSN (online) 1469-9001
    ISSN 1355-8382
    DOI 10.1261/rna.038356.113
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4777: 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)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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