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PCMT1 encodes a member of the type II class of protein carboxyl methyltransferase enzymes. De plus, nous expédions Protein-L-Isoaspartate (D-Aspartate) O-Methyltransferase Anticorps (68) et Protein-L-Isoaspartate (D-Aspartate) O-Methyltransferase Protéines (14) et beaucoup plus de produits pour cette protéine.
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decrease of PCMT1 significantly increased the proportion of D-Asp (Montrer ASIP Kits ELISA) residues in PHB1 (Montrer PHB Kits ELISA) and had significant and fatal impacts on morphology and functions of the mitochondria, such as ATP production and the mitochondrial fusion-fission system
PIMT heterozygosity for R36C, G175R, R17H, or R17S would be detrimental to successful aging, whereas homozygosity (should it ever occur) would produce devastating neuropathology
Strong PIMT expression was a predictive marker of poor prognosis for surgically resected lung adenocarcinoma.
The data of this study indicated that DA-associated PIMT downregulation is an important event contributing to neuronal cell death
ERK2-mediated phosphorylation of transcriptional coactivator binding protein PIMT/NCoA6IP at Ser298 augments hepatic gluconeogenesis.
Overexpression of PCMT1 attentuates Mst1 (Montrer MST1 Kits ELISA) kinase activation and its apoptotic effects in response to hypoxia-induced injury in cardiomyocytes.
Data indicate that human PROTEIN ISOASPARTYL METHYLTRANSFERASE (PIMT) can initiate isoAsp conversion to Asp (Montrer ASIP Kits ELISA), and is able to restore Arabidopsis PRH75 (Montrer DDX46 Kits ELISA)'s complex biochemical activity provided isoAsp formation has not led to conformational alterations.
Data show six differentially expressed proteins were identified as HSP70 (Montrer HSP70 Kits ELISA), PPIA (Montrer PPIA Kits ELISA) and alpha-Enolase (Montrer ENO1 Kits ELISA) (up-regulated) S100-A9, PIMT and beta-5 tubulin (Montrer TUBB Kits ELISA) (down-regulated), most of which had been shown to play a potential role in the pathogenesis of atherosclerosis.
The results implied that maternal polymorphisms in PCMT1 might be a potential genetic risk factor for isolated anencephaly in the Chinese population of Lvliang.
Study provides new insight into the molecular mechanisms by which PIMT suppresses the p53 (Montrer TP53 Kits ELISA) activity through carboxyl methylation, and suggests a therapeutic target for cancers.
Loss of normal CKB (Montrer CHKB Kits ELISA) structure and function contributes to the mechanisms by which isoaspartate accumulation leads to central nervous system dysfunction in the PIMT-Knockout mouse.
PIMT levels may significantly influence the course of age-related central nervous system dysfunction.
PIMT knockout mice have perturbations in glutamate (Montrer GRIN1 Kits ELISA) metabolism in the brain and die prematurely of epileptic seizures.
synuclein is not a major target of PIMT in vivo
Altered levels of S-adenosylmethionine and S-adenosylhomocysteine in the brains of PCMT1 knockout mice
Recombinant adeno (Montrer ADORA2A Kits ELISA)-PIMT improved the symptoms of PIMT-deficient mice in vivo, but only partially repaired IsoAsp in damaged proteins.
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.
Pcmt1-/- mice have altered regulation of the insulin (Montrer INS Kits ELISA) 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.
Protein L-isoaspartyl methyltransferase (PIMT) catalyzes in vivo racemization of Asp (Montrer C3 Kits ELISA)-25 in mammalian histone H2B, suggesting that PIMT functions in the repair, rather than the metabolic turnover, of isoaspartyl proteins in vivo.
This gene encodes a member of the type II class of protein carboxyl methyltransferase enzymes. The encoded enzyme plays a role in protein repair by recognizing and converting D-aspartyl and L-isoaspartyl residues resulting from spontaneous deamidation back to the normal L-aspartyl form. The encoded protein may play a protective role in the pathogenesis of Alzheimer's disease, and single nucleotide polymorphisms in this gene have been associated with spina bifida and premature ovarian failure. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
L-isoaspartyl protein carboxyl methyltransferase
, protein L-isoaspartyl/D-aspartyl methyltransferase
, protein-L-isoaspartate(D-aspartate) O-methyltransferase
, protein-beta-aspartate methyltransferase
, protein carboxyl methyltransferase
, protein carboxyl-o-methyltransferase
, protein-L-isoaspartate (D-aspartate) O-methyltransferase 1
, Protein L-isoaspartyl/D-aspartyl methyltransferase
, Protein-beta-aspartate methyltransferase
, l-isoaspartyl protein carboxyl methyltransferase