Articles with "arginine methyltransferase" as a keyword



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Aflatoxin-induced upregulation of protein arginine methyltransferase 5 is mediated by protein kinase C and extracellular signal-regulated kinase

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Published in 2018 at "Cell Biology and Toxicology"

DOI: 10.1007/s10565-018-9439-8

Abstract: Aflatoxins are fungal metabolites classified into four major groups such as B1, B2, G1, and G2. These natural aflatoxins are designated as group I carcinogen by the International Agency for Research on Cancer. Among these,… read more here.

Keywords: arginine methyltransferase; kinase; extracellular signal; protein arginine ... See more keywords
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A coupled fluorescence-based assay for the detection of protein arginine N-methyltransferase 6 (PRMT6) enzymatic activity.

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Published in 2018 at "Analytical biochemistry"

DOI: 10.1016/j.ab.2018.01.023

Abstract: The protein arginine N-methyltransferase 6 (PRMT6) is overexpressed in a variety of different cancer types and plays a role in human immunodeficiency virus (HIV) infections. Furthermore, the PRMT6 activity might also influence the pathogenesis of… read more here.

Keywords: arginine methyltransferase; fluorescence based; protein arginine; coupled fluorescence ... See more keywords
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Histone arginine methyltransferase CARM1 selective inhibitor TP-064 induces apoptosis in endometrial cancer.

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Published in 2022 at "Biochemical and biophysical research communications"

DOI: 10.1016/j.bbrc.2022.02.086

Abstract: Histone modification is the key epigenetic mechanism that regulates gene expression. Coactivator-associated arginine methyltransferase 1 (CARM1) is an arginine methyltransferase that catalyzes dimethylation of histone H3 (H3R17) at arginine 17. Lately, it has been suggested… read more here.

Keywords: cancer; arginine methyltransferase; methyltransferase carm1; endometrial cancer ... See more keywords
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Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme).

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Published in 2019 at "Journal of molecular biology"

DOI: 10.1016/j.jmb.2019.11.002

Abstract: Prozymes are pseudoenzymes that stimulate the function of weakly active enzymes through complex formation. The major Trypanosoma brucei protein arginine methyltransferase, TbPRMT1 enzyme (ENZ), requires TbPRMT1 prozyme (PRO) to form an active heterotetrameric complex. Here… read more here.

Keywords: structural basis; arginine methyltransferase; methyltransferase; protein arginine ... See more keywords
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A Direct Assay for Measuring the Activity and Inhibition of Coactivator-Associated Arginine Methyltransferase 1

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Published in 2022 at "Biochemistry"

DOI: 10.1021/acs.biochem.2c00075

Abstract: Coactivator-associated arginine methyltransferase 1 (CARM1) is a member of the family of protein arginine methyltransferases. CARM1 catalyzes methyl group transfer from the cofactor S-adenosyl-l-methionine (AdoMet) to both histone and nonhistone protein substrates. CARM1 is involved… read more here.

Keywords: activity inhibition; coactivator associated; arginine methyltransferase; carm1 ... See more keywords
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Identification of Selective, Cell Active Inhibitors of Protein Arginine Methyltransferase 5 through Structure-Based Virtual Screening and Biological Assays

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Published in 2018 at "Journal of chemical information and modeling"

DOI: 10.1021/acs.jcim.8b00050

Abstract: Protein arginine methyltransferase 5 (PRMT5), a type II PRMT enzyme, is reported as an important therapeutic target in leukemia and lymphoma. In the present study, based on the combination of virtual screening and biochemical validations,… read more here.

Keywords: virtual screening; arginine methyltransferase; protein arginine; identification selective ... See more keywords
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Structure-Aided Design, Synthesis, and Biological Evaluation of Potent and Selective Non-Nucleoside Inhibitors Targeting Protein Arginine Methyltransferase 5.

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Published in 2022 at "Journal of medicinal chemistry"

DOI: 10.1021/acs.jmedchem.2c00398

Abstract: PRMT5 is a major type II protein arginine methyltransferase and plays important roles in diverse cellular processes. Overexpression of PRMT5 is implicated in various types of cancer. Many efforts have been made to develop potent… read more here.

Keywords: protein arginine; non nucleoside; arginine methyltransferase; potent selective ... See more keywords
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The LINC01138 drives malignancies via activating arginine methyltransferase 5 in hepatocellular carcinoma

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Published in 2018 at "Nature Communications"

DOI: 10.1038/s41467-018-04006-0

Abstract: Recurrent chromosomal aberrations have led to the discovery of oncogenes or tumour suppressors involved in carcinogenesis. Here we characterized an oncogenic long intergenic non-coding RNA in the frequent DNA-gain regions in hepatocellular carcinoma (HCC), LINC01138… read more here.

Keywords: hepatocellular carcinoma; linc01138; arginine methyltransferase; hcc ... See more keywords
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The arginine methyltransferase PRMT7 promotes extravasation of monocytes resulting in tissue injury in COPD

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Published in 2022 at "Nature Communications"

DOI: 10.1038/s41467-022-28809-4

Abstract: Extravasation of monocytes into tissue and to the site of injury is a fundamental immunological process, which requires rapid responses via post translational modifications (PTM) of proteins. Protein arginine methyltransferase 7 (PRMT7) is an epigenetic… read more here.

Keywords: injury; arginine methyltransferase; extravasation monocytes; methyltransferase prmt7 ... See more keywords
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Protein arginine methyltransferase 1 upregulates matrix metalloproteinase‐2/9 expression via Zeste Homolog 2 to promote human rheumatoid arthritis fibroblast‐like synovial cell survival and metastasis

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Published in 2022 at "International Journal of Rheumatic Diseases"

DOI: 10.1111/1756-185x.14454

Abstract: To explore the role of protein arginine methyltransferase 1 (PRMT1) in the development of rheumatoid arthritis (RA). read more here.

Keywords: methyltransferase upregulates; protein arginine; rheumatoid arthritis; arginine methyltransferase ... See more keywords
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Inhibition of protein arginine methyltransferase 3 activity selectively impairs liver X receptor‐driven transcription of hepatic lipogenic genes in vivo

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Published in 2018 at "British Journal of Pharmacology"

DOI: 10.1111/bph.14361

Abstract: Agonists for the liver X receptor (LXR) are considered promising therapeutic moieties in cholesterol‐driven diseases by promoting cellular cholesterol efflux pathways. However, current clinical application of these agents is hampered by concomitant LXR‐induced activation of… read more here.

Keywords: protein arginine; liver receptor; lxr; arginine methyltransferase ... See more keywords