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anti-Human PRMT5 Antikörper:
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Human Polyclonal PRMT5 Primary Antibody für IHC (p), ELISA - ABIN543137
Rho, Choi, Seong, Cho, Kim, Im: Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. in The Journal of biological chemistry 2001
Show all 3 Pubmed References
Human Polyclonal PRMT5 Primary Antibody für IHC (p), IHC - ABIN258206
Pak, Lee, Roh: High nuclear expression of protein arginine methyltransferase-5 is a potentially useful marker to estimate submucosal invasion in endoscopically resected early colorectal carcinoma. in Pathology international 2015
Human Polyclonal PRMT5 Primary Antibody für WB - ABIN4347350
Guo, Zheng, Xu, Dai, Zhou, Pascua, Chen, Shen: Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding. in Nature chemical biology 2010
High PRMT5 expression is associated with glioblastoma.
Expression of PRMT5 was significantly increased in human gastric cancer (GC) tissues compared with normal gastric mucosa. Multiple evidences suggested that PRMT5 repressed transcription of tumor suppressor IRX1 via recruitment of DNMT3A on promoter.
PRMT5 may play a role from early oncogenesis through to the progression of oral squamous cell carcinoma , particularly in the aggressive mode of stromal invasion
he phosphorylation of the MP inhibitory MYPT1(T850) and the regulatory PRMT5(T80) residues as well as the symmetric dimethylation of H2A/4 were elevated in human hepatocellular carcinoma and in other types of cancers.
The polymerase-associated factor complex regulates Prmt5 to facilitate leukemic progression and is a potential therapeutic target for acute myeloid leukemias.
our results indicated that PRMT5 overexpression in hepatocellular carcinoma (HCC)and colon cancer cells contributed to their acquisition of aggressive characteristics, such as invasiveness, thus presenting a promising therapeutic target for the treatment of these diseases
PRMT5 as a key in vitro and in vivo regulator of breast cancer stem cells proliferation. PRMT5 epigenetically regulates FOXP1.
Protein arginine methyltransferase 5 (PRMT5) was identified to be responsible for Eno-1 methylation. Overexpression of PRMT5 and caveolin-1 enhanced levels of membrane-bound extracellular Eno-1 and, conversely, pharmacological inhibition of PRMT5 attenuated Eno-1 cell-surface localization.
A 3.7 A structure of PRMT5, solved in complex with regulatory binding subunit MEP50 (methylosome associated protein 50, WDR77, p44), by single particle (SP) cryo-Electron Microscopy (cryo-EM) using micrographs of particles that are visibly crowded and aggregated. The catalytic PRMT5 subunits form a core tetramer and the MEP50 subunits are arranged peripherally in complex with the PRMT5 N-terminal domain.
These kinetic studies suggest a biochemical explanation for the interplay between PRMT5- and PRMT7-mediated methylation of the same substrate at different residues and also suggest a general model for regulation of PRMTs.
Data indicate the significant potential of PRMT5 as a therapeutic target in pancreatic ductal adenocarcinoma (PDAC) and colorectal cancer (CRC).
PRMT5 inhibited the interaction between CDK4 and CDKN2A and then activated the CDK4-RB-E2F pathway in hepatocellular carcinoma cells under glucose induction.
Data suggest that the protein arginine methyltransferase 5 (PRMT5)-E2F1 transcription factor (E2F-1) pathway may act as a common target for exogenous lectins including Anguilla japonica lectin 1 (AJL1), and the cellular response to exogenous AJL1 may suggest a novel agent for cancer gene therapy.
These results could be helpful in discovering new potent and specific inhibitors of PRMT5, as well as in designing mutant residue assay to modulate the catalytic activity of PRMT5.
PRMT1 inhibition prevents gastric cancer progression by downregulating eIF4E and targeting type II PRMT5.
Data indicate that ZNF326 is an interaction partner and substrate of the PRMT5/WDR77 complex.
ERG signaling in prostate cancer is driven through PRMT5-dependent methylation of the androgen receptor.
SFN treatment of tumors results in reduced MEP50 level and H4R3me2s formation, confirming that that SFN impacts this complex in vivo. These studies suggest that the PRMT5/MEP50 is required for tumor growth and that reduced expression of this complex is a part of the mechanism of SFN suppression of tumor formation.
High nuclear PRMT5 expression is associated with oropharyngeal squamous cell carcinoma.
High PRMT5 expression is associated with prostate cancer.
Results indicate protein arginine N-methyltransferase 5 (PRMT5) as critical for oligodendrocyte differentiation and developmental myelination.
Targeting PRMT5 using small-molecule inhibitors in the treatment of leukemias harboring MLL rearrangements.
PRMT activity is selectively augmented during the initial activation of exercise-induced skeletal muscle remodeling in vivo.
OGG1 affects PRMT5 binding on histone H4 and the formation of dimethylation of histone H4 arginine-3 via PRMT5.
observed the progressive decrease in PRMT5 during oligodendrocyte differentiation
the present study increases our understanding of PRMT1, -4, and -5 biology during the plasticity of skeletal muscle development. Our results provide evidence for a role of PRMT1, via a mitochondrially mediated mechanism, in driving the muscle differentiation program.
the nuclear localized CA-VI B selectively promotes IL-12 expression by interaction with protein arginine N-methyltransferase 5 (PRMT5), which reduces symmetric dimethylation of histone H3 arginine 8 modification (H3R8me2s) at Il12 promoters to facilitate chromatin accessibility, selectively enhancing c-Rel binding to the Il12b promoter.
this study demonstrates for the first time that oncogenic stress orchestrates a p53-dependent response that is controlled by PRMT5-mediated arginine methylation and identifies the Fanconi anemia pathway as an integral part of this versatile cellular mechanism
PRMT5 is an osteoclastogenesis activator and PRMT5 inhibition suppresses osteoclast differentiation via downregulation of CXCL10 and RSAD2.
PRMT5 regulates internal ribosome entry site-dependent translation via methylation of hnRNP A1.
PRMT5 maintains progenitor cells through its regulation of Bmp4; adult and embryonic stem cells also require PRMT5 for maintaining pluripotency, suggesting that similar mechanisms might regulate lineage-restricted progenitor cells during organogenesis.
Menin and PRMT5 suppress GLP1R transcript levels and PKA-mediated phosphorylation of FOXO1 and CREB.
findings show that PRMT5 is an important modulator of CD4(+) T cell expansion; PRMT5 was transiently upregulated during maximal proliferation of mouse and human memory Th cells; data implicate PRMT5 in the regulation of adaptive memory Th cell responses
Prmt5 facilitates promoter-enhancer looping and gene expression at the PPARgamma2 locus, which encodes a critical lineage-determining factor that drives the differentiation of adipose tissue.
Taken together, our data reveal a pathophysiologically relevant role for PRMT5 in MHC II transactivation in macrophages
Prmt5 is required for germ cell survival during spermatogenesis in mice.
Prmt5 controls proliferation of adult muscle stem cells by direct epigenetic silencing of the cell cycle inhibitor p21.
Prmt5 plays critical roles in germ cell development that are required for germ cell survival during embryonic stages
results demonstrate that PRMT5 plays distinct roles in the behavior of HSCs compared with HPCs and is essential for the maintenance of adult hematopoietic cells.
a combinatorial role of PRMT4/CARM1 and PRMT5 for proper myogenesis in zebrafish
Data indicate that MEP50 WD repeat protein is essential for methylation of histones H4 and H2A by PRMT5 arginine methyltransferase.
data support a mechanism in which MEP50 binds substrate and stimulates PRMT5 activity modulated by substrate post-translational modifications
Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs
The results suggested that medaka Mep50 could be a partner of Prmt5 and might play major roles in a variety of tissues in medaka.
It show the morphological and functional phenotypes of single or double null alleles of prmt-5 in Caenorhabditis elegans. The prmt-1;prmt-5 double mutants are viable, and exhibit short body length and small brood size compared to N2 and each of the single mutants.
The PRMT-5 catalyzes the symmetric dimethylation of substrates containing monomethylarginine residues in vivo.
Analysis of prmt-5-deficient worms indicated that methylation promoted the dopamine-mediated modulation of chemosensory and locomotory behaviors through the DOP-3 receptor.
data confirm that MEP50 plays a key role in substrate recognition and activates PRMT5 activity by increasing its affinity for protein substrates.
the substrate specificity, processivity, and kinetic mechanism of bacterially expressed Caenorhabditis elegans PRMT5 (cPRMT5).
analysis of structural insights into protein arginine symmetric dimethylation by PRMT5
PRMT-5 represses CEP-1 transcriptional activity through CBP-1, which represents a novel regulatory mechanism of p53-dependent apoptosis.
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3)\; such methylation being required for the assembly and biogenesis of snRNP core particles. Methylates SUPT5H. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. Methylates histone H2A and H4 'Arg-3' during germ cell development. Methylates histone H3 'Arg-8', which may repress transcription. Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR\; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (By similarity). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation (By similarity). Methylates HOXA9 (By similarity).
72 kDa ICln-binding protein
, HMT1 hnRNP methyltransferase-like 5
, SKB1 homolog
, histone-arginine N-methyltransferase PRMT5
, jak-binding protein 1
, protein arginine N-methyltransferase 5
, shk1 kinase-binding protein 1 homolog
, protein arginine methyltransferase 5
, Jak-binding protein 1
, putative arginine N-methyltransferase, type II
, protein arginine methyltransferase
, protein arginine N-methyltransferase 5-like