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    NEU4 neuraminidase 4 [ Homo sapiens (human) ]

    Gene ID: 129807, updated on 19-Sep-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Neuraminidase 4 (NEU4): new biological and physiological player.

    Neuraminidase 4 (NEU4): new biological and physiological player.
    Okun S, Peek A, Igdoura SA.

    10/28/2023
    Biomarkers of ulcerative colitis disease activity CXCL1, CYP2R1, LPCAT1, and NEU4 and their relationship to immune infiltrates.

    Biomarkers of ulcerative colitis disease activity CXCL1, CYP2R1, LPCAT1, and NEU4 and their relationship to immune infiltrates.
    Huo A, Wang F., Free PMC Article

    07/31/2023
    Synergistic activation of the NEU4 promoter by p73 and AP2 in colon cancer cells.

    Synergistic activation of the NEU4 promoter by p73 and AP2 in colon cancer cells.
    Cai BH, Wu PH, Chou CK, Huang HC, Chao CC, Chung HY, Lee HY, Chen JY, Kannagi R., Free PMC Article

    08/15/2020
    The most potent compound tested targeted the human Neu4 isoenzyme, and was able to substantially reduce the rate of cell migration. We found that the lateral mobility of integrins was reduced by treatment of cells with Neu3, suggesting that Neu3 enzyme activity resulted in changes to integrin-co-receptor or integrin-cytoskeleton interactions

    Integrin-mediated cell migration is blocked by inhibitors of human neuraminidase.
    Jia F, Howlader MA, Cairo CW.

    06/3/2017
    The silencing or chemical inhibition of NEU4 changes the entire glycosylation pattern of proteins and lipids, making it more similar to that of differentiated GBM cells and drastically reduces GSCs survival.

    Sialidase NEU4 is involved in glioblastoma stem cell survival.
    Silvestri I, Testa F, Zappasodi R, Cairo CW, Zhang Y, Lupo B, Galli R, Di Nicola M, Venerando B, Tringali C., Free PMC Article

    03/12/2016
    The results demonstrate that the proline-rich region can also enhance cell proliferation and retinoic acid (RA)-induced neuronal differentiation and it is also involved in NEU4 interaction with Akt.

    A proline-rich loop mediates specific functions of human sialidase NEU4 in SK-N-BE neuronal differentiation.
    Bigi A, Tringali C, Forcella M, Mozzi A, Venerando B, Monti E, Fusi P.

    12/20/2014
    Overexpression of NEU4 is associated with neuroblastoma.

    NEU4L sialidase overexpression promotes β-catenin signaling in neuroblastoma cells, enhancing stem-like malignant cell growth.
    Tringali C, Cirillo F, Lamorte G, Papini N, Anastasia L, Lupo B, Silvestri I, Tettamanti G, Venerando B.

    11/3/2012
    NEU4 is involved in regulation of neuronal function by polySia degradation in mammals.

    Sialidase NEU4 hydrolyzes polysialic acids of neural cell adhesion molecules and negatively regulates neurite formation by hippocampal neurons.
    Takahashi K, Mitoma J, Hosono M, Shiozaki K, Sato C, Yamaguchi K, Kitajima K, Higashi H, Nitta K, Shima H, Miyagi T., Free PMC Article

    07/7/2012
    NEU4 plays an important role in control of sialyl Lewis antigen expression and its impairment in colon cancer

    Regulation of sialyl Lewis antigen expression in colon cancer cells by sialidase NEU4.
    Shiozaki K, Yamaguchi K, Takahashi K, Moriya S, Miyagi T., Free PMC Article

    09/3/2011
    The NEU4 long form localizes in mitochondria, while the short form is also associated with the endoplasmic reticulum.

    Human sialidase NEU4 long and short are extrinsic proteins bound to outer mitochondrial membrane and the endoplasmic reticulum, respectively.
    Bigi A, Morosi L, Pozzi C, Forcella M, Tettamanti G, Venerando B, Monti E, Fusi P.

    03/8/2010
    related to malignancy and may be potential targets for cancer diagnosis and therapy

    Human sialidase as a cancer marker.
    Miyagi T, Wada T, Yamaguchi K, Shiozaki K, Sato I, Kakugawa Y, Yamanami H, Fujiya T.

    01/21/2010
    Neu4 is a novel human lysosomal lumen sialidase

    Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells.
    Seyrantepe V, Landry K, Trudel S, Hassan JA, Morales CR, Pshezhetsky AV.

    01/21/2010
    The NEU4 gene, identified by searching sequence databases for entries showing homologies to the human cytosolic sialidase NEU2, maps in 2q37 and encodes a 484-residue protein.

    Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family.
    Monti E, Bassi MT, Bresciani R, Civini S, Croci GL, Papini N, Riboni M, Zanchetti G, Ballabio A, Preti A, Tettamanti G, Venerando B, Borsani G.

    01/21/2010
    Data show that the differentiation of monocytes into macrophages is associated with regulation of the expression of at least three distinct cellular sialidases, Neu1, 3, and 4, with specific up-regulation of the enzyme activity of only Neu1.

    Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages.
    Stamatos NM, Liang F, Nan X, Landry K, Cross AS, Wang LX, Pshezhetsky AV.

    01/21/2010
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