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    Nrdc nardilysin convertase [ Mus musculus (house mouse) ]

    Gene ID: 230598, updated on 12-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Nardilysin-regulated scission mechanism activates polo-like kinase 3 to suppress the development of pancreatic cancer.

    Nardilysin-regulated scission mechanism activates polo-like kinase 3 to suppress the development of pancreatic cancer.
    Fu J, Ling J, Li CF, Tsai CL, Yin W, Hou J, Chen P, Cao Y, Kang Y, Sun Y, Xia X, Jiang Z, Furukawa K, Lu Y, Wu M, Huang Q, Yao J, Hawke DH, Pan BF, Zhao J, Huang J, Wang H, Bahassi EIM, Stambrook PJ, Huang P, Fleming JB, Maitra A, Tainer JA, Hung MC, Lin C, Chiao PJ., Free PMC Article

    04/30/2024
    Nardilysin in adipocytes regulates UCP1 expression and body temperature homeostasis.

    Nardilysin in adipocytes regulates UCP1 expression and body temperature homeostasis.
    Saijo S, Ohno M, Iwasaki H, Matsuda S, Nishi K, Hiraoka Y, Ide N, Kimura T, Nishi E., Free PMC Article

    04/23/2022
    Deficiency of Nardilysin in the Liver Reduces Serum Cholesterol Levels.

    Deficiency of Nardilysin in the Liver Reduces Serum Cholesterol Levels.
    Yasuda D, Hiraoka Y, Ohno M, Nishi K, Iwasaki H, Kita T, Nishi E, Kume N.

    10/16/2021
    Nardilysin controls cardiac sympathetic innervation patterning through regulation of p75 neurotrophin receptor.

    Nardilysin controls cardiac sympathetic innervation patterning through regulation of p75 neurotrophin receptor.
    Ohno M, Nishi K, Hiraoka Y, Niizuma S, Matsuda S, Iwasaki H, Kimura T, Nishi E.

    03/27/2021
    integrative studies emphasize the importance of Nrdc for maintaining a proper epigenetic status and cell growth.

    Genome-wide profiling of nardilysin target genes reveals its role in epigenetic regulation and cell cycle progression.
    Morita Y, Ohno M, Nishi K, Hiraoka Y, Saijo S, Matsuda S, Kita T, Kimura T, Nishi E., Free PMC Article

    07/6/2019
    Here, the authors have demonstrated that nardilysin regulates gastric inflammation caused by Helicobacter felis infection or forced expression of prostaglandin. Metaplastic changes following gastric inflammation were suppressed by the deletion of nardilysin. Furthremore, the deletion of nardilysin significantly suppressed N-methyl-N-nitrosourea (MNU)-induced gastric tumorigenesis in the murine stomach.

    Nardilysin regulates inflammation, metaplasia, and tumors in murine stomach.
    Kimura Y, Ikuta K, Kimura T, Chiba T, Oshima H, Oshima M, Nishi E, Seno H., Free PMC Article

    11/3/2018
    Nardilysin Is Required for Maintaining Pancreatic beta-Cell Function

    Nardilysin Is Required for Maintaining Pancreatic β-Cell Function.
    Nishi K, Sato Y, Ohno M, Hiraoka Y, Saijo S, Sakamoto J, Chen PM, Morita Y, Matsuda S, Iwasaki K, Sugizaki K, Harada N, Mukumoto Y, Kiyonari H, Furuyama K, Kawaguchi Y, Uemoto S, Kita T, Inagaki N, Kimura T, Nishi E.

    05/20/2017
    critical regulator of body temperature homoeostasis

    Critical roles of nardilysin in the maintenance of body temperature homoeostasis.
    Hiraoka Y, Matsuoka T, Ohno M, Nakamura K, Saijo S, Matsumura S, Nishi K, Sakamoto J, Chen PM, Inoue K, Fushiki T, Kita T, Kimura T, Nishi E., Free PMC Article

    10/31/2015
    deletion of nardilysin prevents the development of diet-induced steatohepatitis and liver fibrogenesis

    Deletion of nardilysin prevents the development of steatohepatitis and liver fibrotic changes.
    Ishizu-Higashi S, Seno H, Nishi E, Matsumoto Y, Ikuta K, Tsuda M, Kimura Y, Takada Y, Kimura Y, Nakanishi Y, Kanda K, Komekado H, Chiba T., Free PMC Article

    01/17/2015
    It controls Amyloid beta plaque formation through the regulation of a-secretase.

    Nardilysin prevents amyloid plaque formation by enhancing α-secretase activity in an Alzheimer's disease mouse model.
    Ohno M, Hiraoka Y, Lichtenthaler SF, Nishi K, Saijo S, Matsuoka T, Tomimoto H, Araki W, Takahashi R, Kita T, Kimura T, Nishi E.

    04/26/2014
    Identification and characterization of nardilysin as a novel dimethyl H3K4-binding protein involved in transcriptional regulation.

    Identification and characterization of nardilysin as a novel dimethyl H3K4-binding protein involved in transcriptional regulation.
    Li J, Chu M, Wang S, Chan D, Qi S, Wu M, Zhou Z, Li J, Nishi E, Qin J, Wong J., Free PMC Article

    05/19/2012
    It plays a critical role in axonal maturation and myelination. (review)

    [Regulation of protein ectodomain shedding by nardilysin--a critical role of nardilysin in axonal maturation and myelination].
    Nishi E.

    01/29/2011
    NRDc regulates axonal maturation and myelination in the nervous system, in part, through the modulation of NRG1 shedding

    Nardilysin regulates axonal maturation and myelination in the central and peripheral nervous system.
    Ohno M, Hiraoka Y, Matsuoka T, Tomimoto H, Takao K, Miyakawa T, Oshima N, Kiyonari H, Kimura T, Kita T, Nishi E.

    01/21/2010
    role for nardilysin in oocyte meiosis through its dynamic translocation from cytosol to nucleus, and then to the spindle apparatus

    Subcellular localization of nardilysin during mouse oocyte maturation.
    Ma Z, Wang X, Hockman S, Snow EC, Hersh LB.

    01/21/2010
    Studies extend the range of potential substrates for nardilysin and further substantiate that nardilysin is a true peptidase.

    Nardilysin cleaves peptides at monobasic sites.
    Chow KM, Oakley O, Goodman J, Ma Z, Juliano MA, Juliano L, Hersh LB.

    01/21/2010
    miniglucagon-generating endopeptidase is composed of NRDc and aminopeptidase B acting sequentially

    Miniglucagon (MG)-generating endopeptidase, which processes glucagon into MG, is composed of N-arginine dibasic convertase and aminopeptidase B.
    Fontés G, Lajoix AD, Bergeron F, Cadel S, Prat A, Foulon T, Gross R, Dalle S, Le-Nguyen D, Tribillac F, Bataille D.

    01/21/2010
    The use of proteolysis to study the structure of nardilysin.

    The use of proteolysis to study the structure of nardilysin.
    Ma Z, Chow KM, Csuhai E, Hersh LB.

    01/21/2010
    The acidic stretch of nardilysin, expressed as a fusion protein with glutathione S-transferase and compared to the native enzyme with respect to spermine binding, functions as an autonomous domain.

    Expression of the acidic stretch of nardilysin as a functional binding domain.
    Ma Z, Csuhai E, Chow KM, Hersh LB.

    02/14/2003
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