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    RPL13A ribosomal protein L13a [ Homo sapiens (human) ]

    Gene ID: 23521, updated on 3-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Moonlight human ribosomal protein L13a downregulation is associated with p53 and HER2/neu expression in breast cancer.

    Moonlight human ribosomal protein L13a downregulation is associated with p53 and HER2/neu expression in breast cancer.
    Molavi G, Samadi N, Hashemzadeh S, Halimi M, Hosseingholi EZ.

    05/21/2022
    show through cellular immunofluorescence experiments that nuclear but not nucleolar localization of L13a is resistant to extensive amino acid alterations, suggesting that multiple complex nuclear import signals are present within this protein

    Mutually exclusive amino acid residues of L13a are responsible for its ribosomal incorporation and translational silencing leading to resolution of inflammation.
    Kour R, Komar AA, Mazumder B., Free PMC Article

    01/11/2020
    The expression of RPL13A and EEF1A1 was not affected by differentiation, thus being these genes the most stable candidates as reference genes for RT-PCR.

    RPL13A and EEF1A1 Are Suitable Reference Genes for qPCR during Adipocyte Differentiation of Vascular Stromal Cells from Patients with Different BMI and HOMA-IR.
    Gentile AM, Lhamyani S, Coín-Aragüez L, Oliva-Olivera W, Zayed H, Vega-Rioja A, Monteseirin J, Romero-Zerbo SY, Tinahones FJ, Bermúdez-Silva FJ, El Bekay R., Free PMC Article

    07/22/2017
    This work identified the arginine residue at position 68 of L13A as being essential for L13A binding to rRNA and incorporation into ribosomes.

    Insights into the mechanism of ribosomal incorporation of mammalian L13a protein during ribosome biogenesis.
    Das P, Basu A, Biswas A, Poddar D, Andrews J, Barik S, Komar AA, Mazumder B., Free PMC Article

    09/21/2013
    Ribosomal protein l13a is a reference gene for human bone marrow-derived mesenchymal stromal cells during expansion, adipo-, chondro-, and osteogenesis

    Ribosomal protein l13a as a reference gene for human bone marrow-derived mesenchymal stromal cells during expansion, adipo-, chondro-, and osteogenesis.
    Studer D, Lischer S, Jochum W, Ehrbar M, Zenobi-Wong M, Maniura-Weber K., Free PMC Article

    08/3/2013
    GAPDH functions as a chaperone, shielding newly released RPL13a from proteasomal degradation.

    Protection of extraribosomal RPL13a by GAPDH and dysregulation by S-nitrosylation.
    Jia J, Arif A, Willard B, Smith JD, Stuehr DJ, Hazen SL, Fox PL., Free PMC Article

    02/2/2013
    The study found two ribosomal proteins, RPS7 and RPL13A that interact with the HMG (high-mobility group) box domain of SRY.

    SRY interacts with ribosomal proteins S7 and L13a in nuclear speckles.
    Sato Y, Yano S, Ewis AA, Nakahori Y.

    07/30/2011
    Data show that EF1alpha, RPL13a and YWHAZ are suitable genes for the RT-qPCR analysis and comparison of several sources of human MSC during in vitro characterization and differentiation as well as in an ex vivo animal model of global cerebral ischemia.

    EF1alpha and RPL13a represent normalization genes suitable for RT-qPCR analysis of bone marrow derived mesenchymal stem cells.
    Curtis KM, Gomez LA, Rios C, Garbayo E, Raval AP, Perez-Pinzon MA, Schiller PC., Free PMC Article

    01/1/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article

    09/15/2010
    L13a may have evolved from an essential ribosomal protein in lower eukaryotes to having a role as a dispensable extra-ribosomal function in higher eukaryotes.

    Human ribosomal protein L13a is dispensable for canonical ribosome function but indispensable for efficient rRNA methylation.
    Chaudhuri S, Vyas K, Kapasi P, Komar AA, Dinman JD, Barik S, Mazumder B., Free PMC Article

    01/21/2010
    A translational silencing mechanism involving regulated release of RPL13a and subsequent binding to its target mRNA was elucidated.

    Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control.
    Mazumder B, Sampath P, Seshadri V, Maitra RK, DiCorleto PE, Fox PL.

    01/21/2010
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