LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 4 of total 4

Search options

  1. Article ; Online: Pneumoviral Phosphoprotein, a Multidomain Adaptor-Like Protein of Apparent Low Structural Complexity and High Conformational Versatility.

    Cardone, Christophe / Caseau, Claire-Marie / Pereira, Nelson / Sizun, Christina

    International journal of molecular sciences

    2021  Volume 22, Issue 4

    Abstract: ... ...

    Abstract Mononegavirales
    MeSH term(s) Amino Acid Sequence ; Animals ; Binding Sites ; Gene Expression Regulation, Viral ; Humans ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Models, Molecular ; Mononegavirales ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Pneumovirus/genetics ; Pneumovirus/metabolism ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Interaction Domains and Motifs ; Respiratory Syncytial Virus, Human ; Structure-Activity Relationship ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism
    Chemical Substances Intrinsically Disordered Proteins ; Phosphoproteins ; Viral Proteins
    Language English
    Publishing date 2021-02-03
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms22041537
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  2. Article ; Online: A Structural and Dynamic Analysis of the Partially Disordered Polymerase-Binding Domain in RSV Phosphoprotein.

    Cardone, Christophe / Caseau, Claire-Marie / Bardiaux, Benjamin / Thureaux, Aurélien / Galloux, Marie / Bajorek, Monika / Eléouët, Jean-François / Litaudon, Marc / Bontems, François / Sizun, Christina

    Biomolecules

    2021  Volume 11, Issue 8

    Abstract: The phosphoprotein P ... ...

    Abstract The phosphoprotein P of
    MeSH term(s) Hydrogen Bonding ; Light ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Nucleoproteins/metabolism ; Phosphoproteins/chemistry ; Protein Binding ; Protein Conformation ; Protein Domains ; Respiratory Syncytial Virus, Human/chemistry ; Respiratory Syncytial Virus, Human/genetics ; Scattering, Radiation ; Terpenes/chemistry ; Viral Proteins/chemistry ; X-Rays
    Chemical Substances Nucleoproteins ; Phosphoproteins ; Terpenes ; Viral Proteins ; garcinol (TR1VR1V71B)
    Language English
    Publishing date 2021-08-17
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom11081225
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  3. Article ; Online: RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription.

    Richard, Charles-Adrien / Rincheval, Vincent / Lassoued, Safa / Fix, Jenna / Cardone, Christophe / Esneau, Camille / Nekhai, Sergei / Galloux, Marie / Rameix-Welti, Marie-Anne / Sizun, Christina / Eléouët, Jean-François

    PLoS pathogens

    2018  Volume 14, Issue 3, Page(s) e1006920

    Abstract: Respiratory syncytial virus (RSV) RNA synthesis occurs in cytoplasmic inclusion bodies (IBs) in which all the components of the viral RNA polymerase are concentrated. In this work, we show that RSV P protein recruits the essential RSV transcription ... ...

    Abstract Respiratory syncytial virus (RSV) RNA synthesis occurs in cytoplasmic inclusion bodies (IBs) in which all the components of the viral RNA polymerase are concentrated. In this work, we show that RSV P protein recruits the essential RSV transcription factor M2-1 to IBs independently of the phosphorylation state of M2-1. We also show that M2-1 dephosphorylation is achieved by a complex formed between P and the cellular phosphatase PP1. We identified the PP1 binding site of P, which is an RVxF-like motif located nearby and upstream of the M2-1 binding region. NMR confirmed both P-M2-1 and P-PP1 interaction regions in P. When the P-PP1 interaction was disrupted, M2-1 remained phosphorylated and viral transcription was impaired, showing that M2-1 dephosphorylation is required, in a cyclic manner, for efficient viral transcription. IBs contain substructures called inclusion bodies associated granules (IBAGs), where M2-1 and neo-synthesized viral mRNAs concentrate. Disruption of the P-PP1 interaction was correlated with M2-1 exclusion from IBAGs, indicating that only dephosphorylated M2-1 is competent for viral mRNA binding and hence for a previously proposed post-transcriptional function.
    MeSH term(s) Amino Acid Sequence ; Binding Sites ; Cytoplasmic Granules/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Humans ; Inclusion Bodies/metabolism ; Phosphorylation ; Protein Phosphatase 1/metabolism ; Proteolysis ; RNA, Viral ; Respiratory Syncytial Virus Infections/metabolism ; Respiratory Syncytial Virus Infections/virology ; Respiratory Syncytial Virus, Human/genetics ; Respiratory Syncytial Virus, Human/pathogenicity ; Sequence Homology ; Transcription, Genetic ; Viral Proteins/metabolism
    Chemical Substances RNA, Viral ; Viral Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Protein Phosphatase 1 (EC 3.1.3.16)
    Language English
    Publishing date 2018-02-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1006920
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    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.

  4. Article ; Online: New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein Partners.

    Pereira, Nelson / Cardone, Christophe / Lassoued, Safa / Galloux, Marie / Fix, Jenna / Assrir, Nadine / Lescop, Ewen / Bontems, François / Eléouët, Jean-François / Sizun, Christina

    The Journal of biological chemistry

    2016  Volume 292, Issue 6, Page(s) 2120–2131

    Abstract: Phosphoprotein is the main cofactor of the viral RNA polymerase ... ...

    Abstract Phosphoprotein is the main cofactor of the viral RNA polymerase of
    MeSH term(s) Amino Acid Sequence ; Electron Spin Resonance Spectroscopy ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Protein Binding ; Protein Structure, Secondary ; Respiratory Syncytial Virus, Human/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances Intrinsically Disordered Proteins ; Phosphoproteins
    Language English
    Publishing date 2016-12-28
    Publishing country United States
    Document type Journal Article ; 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.M116.765958
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    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.

To top