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    Pcmt1 protein-L-isoaspartate (D-aspartate) O-methyltransferase 1 [ Mus musculus (house mouse) ]

    Gene ID: 18537, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PIMT is a novel and potent suppressor of endothelial activation.

    PIMT is a novel and potent suppressor of endothelial activation.
    Zhang C, Guo ZF, Liu W, Kazama K, Hu L, Sun X, Wang L, Lee H, Lu L, Yang XF, Summer R, Sun J., Free PMC Article

    04/26/2023
    Loss of normal CKB structure and function contributes to the mechanisms by which isoaspartate accumulation leads to central nervous system dysfunction in the PIMT-Knockout mouse.

    Isoaspartyl formation in creatine kinase B is associated with loss of enzymatic activity; implications for the linkage of isoaspartate accumulation and neurological dysfunction in the PIMT knockout mouse.
    Dimitrijevic A, Qin Z, Aswad DW., Free PMC Article

    10/17/2015
    PIMT levels may significantly influence the course of age-related central nervous system dysfunction.

    Accelerated protein damage in brains of PIMT+/- mice; a possible model for the variability of cognitive decline in human aging.
    Qin Z, Dimitrijevic A, Aswad DW., Free PMC Article

    09/26/2015
    ERK2-mediated phosphorylation of transcriptional coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic gluconeogenesis.

    ERK2-mediated phosphorylation of transcriptional coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic gluconeogenesis.
    Kapadia B, Viswakarma N, Parsa KV, Kain V, Behera S, Suraj SK, Babu PP, Kar A, Panda S, Zhu YJ, Jia Y, Thimmapaya B, Reddy JK, Misra P., Free PMC Article

    09/20/2014
    PIMT knockout mice have perturbations in glutamate metabolism in the brain and die prematurely of epileptic seizures.

    Brain proteomics supports the role of glutamate metabolism and suggests other metabolic alterations in protein l-isoaspartyl methyltransferase (PIMT)-knockout mice.
    Yang H, Lowenson JD, Clarke S, Zubarev RA., Free PMC Article

    05/10/2014
    synuclein is not a major target of PIMT in vivo

    Considerations in the identification of endogenous substrates for protein L-isoaspartyl methyltransferase: the case of synuclein.
    Morrison GJ, Ganesan R, Qin Z, Aswad DW., Free PMC Article

    02/16/2013
    Pcmt1-/- mice have an increased number of granule cells in the granule cell layer and hilus of the dentate gyrus.

    Increased cell proliferation and granule cell number in the dentate gyrus of protein repair-deficient mice.
    Farrar CE, Huang CS, Clarke SG, Houser CR.

    01/21/2010
    An accumulation of isoaspartyl residues in cells of mice lacking the isoaspartyl repair enzyme PCMT alters the effector function of T lymphocytes leading to autoantibody production.

    A failure to repair self-proteins leads to T cell hyperproliferation and autoantibody production.
    Doyle HA, Gee RJ, Mamula MJ.

    01/21/2010
    Recombinant adeno-PIMT improved the symptoms of PIMT-deficient mice in vivo, but only partially repaired IsoAsp in damaged proteins.

    Adenoviral expression of protein-L-isoaspartyl methyltransferase (PIMT) partially attenuates the biochemical changes in PIMT-deficient mice.
    Ogawara M, Takahashi M, Shimizu T, Nakajima M, Setoguchi Y, Shirasawa T.

    01/21/2010
    Synapsin I is a major endogenous substrate for Pcmt1 in the mouse brain.

    Synapsin I is a major endogenous substrate for protein L-isoaspartyl methyltransferase in mammalian brain.
    Reissner KJ, Paranandi MV, Luc TM, Doyle HA, Mamula MJ, Lowenson JD, Aswad DW.

    01/21/2010
    Altered levels of S-adenosylmethionine and S-adenosylhomocysteine in the brains of PCMT1 knockout mice

    Altered levels of S-adenosylmethionine and S-adenosylhomocysteine in the brains of L-isoaspartyl (D-Aspartyl) O-methyltransferase-deficient mice.
    Farrar C, Clarke S.

    01/21/2010
    Pcmt1-/- mice have altered regulation of the insulin pathway, possibly as a compensatory response to altered glucose uptake or metabolism or as an adaptive response to a general accumulation of isoaspartyl protein damage in the brain and other tissues.

    Activation of the PI3K/Akt signal transduction pathway and increased levels of insulin receptor in protein repair-deficient mice.
    Farrar C, Houser CR, Clarke S.

    01/21/2010
    PIMT-KO phenotype results from the cumulative effect of isoaspartate-related damage to a number of the neuron-rich proteins detected in this study

    Protein repair in the brain, proteomic analysis of endogenous substrates for protein L-isoaspartyl methyltransferase in mouse brain.
    Zhu JX, Doyle HA, Mamula MJ, Aswad DW.

    01/21/2010
    Protein L-isoaspartyl methyltransferase (PIMT) catalyzes in vivo racemization of Asp-25 in mammalian histone H2B, suggesting that PIMT functions in the repair, rather than the metabolic turnover, of isoaspartyl proteins in vivo.

    Protein L-isoaspartyl methyltransferase catalyzes in vivo racemization of Aspartate-25 in mammalian histone H2B.
    Young GW, Hoofring SA, Mamula MJ, Doyle HA, Bunick GJ, Hu Y, Aswad DW.

    01/21/2010
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