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https://www.readbyqxmd.com/read/28330993/transition-state-mimics-are-valuable-mechanistic-probes-for-structural-studies-with-the-arginine-methyltransferase-carm1
#1
Matthijs J van Haren, Nils Marechal, Nathalie Troffer-Charlier, Agostino Cianciulli, Gianluca Sbardella, Jean Cavarelli, Nathaniel I Martin
Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics...
March 22, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28301308/regenerating-muscle-with-arginine-methylation
#2
Roméo S Blanc, Stéphane Richard
Protein arginine methyltransferase (PRMT) is a family of nine proteins catalyzing the methylation of arginine residues. They were recently shown to be essential for proper regeneration of skeletal muscles. However, the mechanisms triggering the methylation event, as well as how the methylated substrates regulate muscle stem cell function and fate decision remain to be determined. This point-of-view will discuss the recent findings on the specific role of PRMT1, CARM1/PRMT4, PRMT5, and PRMT7 in muscle stem cell fate guidance, and shed light on the future challenges which could help defining the therapeutic potential of PRMT inhibitors against muscular disorders and aging...
February 17, 2017: Transcription
https://www.readbyqxmd.com/read/28285332/the-role-of-l-arginine-l-homoarginine-nitric-oxide-pathway-for-aortic-distensibility-and-intima-media-thickness-in-stroke-patients
#3
Arash Haghikia, Georgi Radoslavov Yanchev, Arslan Arinc Kayacelebi, Erik Hanff, Nils Bledau, Christian Widera, Kristina Sonnenschein, Aiden Haghikia, Karin Weissenborn, Johann Bauersachs, Udo Bavendiek, Dimitrios Tsikas
Asymmetric dimethylarginine (ADMA) and L-homoarginine (hArg) are L-arginine (Arg) metabolites derived from different pathways. Protein arginine N-methyltransferase (PRMT) and subsequent proteolysis of proteins containing methylarginine residues release ADMA. Arginine:glycine amidinotransferase (AGAT) converts Arg to hArg and guanidinoacetate (GAA). While high concentrations of ADMA and low concentrations of hArg in the blood have been established as cardiovascular risk markers, the cardiovascular relevance of GAA is still unexplored...
March 11, 2017: Amino Acids
https://www.readbyqxmd.com/read/28279165/root-morphogenic-pathways-in-eucalyptus-grandis-are-modified-by-the-activity-of-protein-arginine-methyltransferases
#4
Krista L Plett, Anita E Raposo, Stephen Bullivant, Ian C Anderson, Sabine C Piller, Jonathan M Plett
BACKGROUND: Methylation of proteins at arginine residues, catalysed by members of the protein arginine methyltransferase (PRMT) family, is crucial for the regulation of gene transcription and for protein function in eukaryotic organisms. Inhibition of the activity of PRMTs in annual model plants has demonstrated wide-ranging involvement of PRMTs in key plant developmental processes, however, PRMTs have not been characterised or studied in long-lived tree species. RESULTS: Taking advantage of the recently available genome for Eucalyptus grandis, we demonstrate that most of the major plant PRMTs are conserved in E...
March 9, 2017: BMC Plant Biology
https://www.readbyqxmd.com/read/28173048/prmt-5-converts-monomethylarginines-into-symmetrical-dimethylarginines-in-caenorhabditis-elegans
#5
Akihiko Kanou, Koichiro Kako, Keiko Hirota, Akiyoshi Fukamizu
No abstract text is available yet for this article.
February 1, 2017: Journal of Biochemistry
https://www.readbyqxmd.com/read/28158808/simultaneous-ablation-of-prmt-1-and-prmt-5-abolishes-asymmetric-and-symmetric-arginine-dimethylations-in-caenorhabditis-elegans
#6
Keiko Hirota, Chihiro Shigekawa, Sho Araoi, Liang Sha, Takayuki Inagawa, Akihiko Kanou, Koichiro Kako, Hiroaki Daitoku, Akiyoshi Fukamizu
No abstract text is available yet for this article.
February 2, 2017: Journal of Biochemistry
https://www.readbyqxmd.com/read/28143887/comparative-monomethylarginine-proteomics-suggests-that-prmt1-is-a-significant-contributor-to-arginine-monomethylation-in-toxoplasma-gondii
#7
Rama R Yakubu, Natalie C Silmon de Monerri, Edward Nieves, Kami Kim, Louis M Weiss
Arginine methylation is a common posttranslational modification found on nuclear and cytoplasmic proteins that has roles in transcriptional regulation, RNA metabolism and DNA repair. The protozoan parasite Toxoplasma gondii has a complex life cycle requiring transcriptional plasticity and has unique transcriptional regulatory pathways. Arginine methylation may play an important part in transcriptional regulation and splicing biology in this organism. The T. gondii genome contains five putative protein arginine methyltransferases (PRMTs), of which PRMT1 is important for cell division and growth...
January 31, 2017: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/28087667/prmt5-selective-inhibitors-suppress-inflammatory-t-cell-responses-and-experimental-autoimmune-encephalomyelitis
#8
Lindsay M Webb, Stephanie A Amici, Kyle A Jablonski, Himanshu Savardekar, Amanda R Panfil, Linsen Li, Wei Zhou, Kevin Peine, Vrajesh Karkhanis, Eric M Bachelder, Kristy M Ainslie, Patrick L Green, Chenglong Li, Robert A Baiocchi, Mireia Guerau-de-Arellano
In the autoimmune disease multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis (EAE), expansion of pathogenic, myelin-specific Th1 cell populations drives active disease; selectively targeting this process may be the basis for a new therapeutic approach. Previous studies have hinted at a role for protein arginine methylation in immune responses, including T cell-mediated autoimmunity and EAE. However, a conclusive role for the protein arginine methyltransferase (PRMT) enzymes that catalyze these reactions has been lacking...
February 15, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/28061334/arginine-methylation-the-coming-of-age
#9
REVIEW
Roméo S Blanc, Stéphane Richard
Arginine methylation is a common post-translational modification functioning as an epigenetic regulator of transcription and playing key roles in pre-mRNA splicing, DNA damage signaling, mRNA translation, cell signaling, and cell fate decision. Recently, a wealth of studies using transgenic mouse models and selective PRMT inhibitors helped define physiological roles for protein arginine methyltransferases (PRMTs) linking them to diseases such as cancer and metabolic, neurodegenerative, and muscular disorders...
January 5, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28042453/design-and-synthesis-of-selective-small-molecule-inhibitors-of-coactivator-associated-arginine-methyltransferase-1-carm1
#10
H Ü Kaniskan, M S Eram, J Liu, D Smil, M L Martini, Y Shen, V Santhakumar, P J Brown, C Arrowsmith, M Vedadi, J Jin
Coactivator-associated arginine methyltransferase 1 (CARM1) is a type I protein arginine methyltransferase (PRMT) that catalyzes the conversion of arginine into monomethylarginine (MMA) and further into asymmetric dimethylarginine (ADMA). CARM1 methylates histone 3 arginines 17 and 26, as well as numerous non-histone proteins including CBP/p300, SRC-3, NCOA2, PABP1, and SAP49, while also functioning as a coactivator for various proteins that have been linked to cancer such as p53, NF-κβ, β-catenin, E2F1 and steroid hormone receptor ERα...
September 1, 2016: MedChemComm
https://www.readbyqxmd.com/read/27998975/the-major-protein-arginine-methyltransferase-in-trypanosoma-brucei-functions-as-an-enzyme-prozyme-complex
#11
Lucie Kafková, Erik W Debler, John C Fisk, Kanishk Jain, Steven G Clarke, Laurie K Read
Prozymes are catalytically inactive enzyme paralogs that dramatically stimulate the function of weakly active enzymes through complex formation. The two prozymes described to date reside in the polyamine biosynthesis pathway of the human parasite Trypanosoma brucei, an early branching eukaryote that lacks transcriptional regulation and regulates its proteome through posttranscriptional and posttranslational means. Arginine methylation is a common posttranslational modification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs) that are typically thought to function as homodimers...
February 10, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27994012/asymmetric-arginine-dimethylation-modulates-mitochondrial-energy-metabolism-and-homeostasis-in-caenorhabditis-elegans
#12
Liang Sha, Hiroaki Daitoku, Sho Araoi, Yuta Kaneko, Yuta Takahashi, Koichiro Kako, Akiyoshi Fukamizu
Protein arginine methyltransferase 1 (PRMT-1) catalyzes asymmetric arginine dimethylation on cellular proteins and modulates various aspects of biological processes, such as signal transduction, DNA repair, and transcriptional regulation. We have previously reported that the null mutant of prmt-1 in Caenorhabditis elegans exhibits a slightly shortened life span, but the physiological significance of PRMT-1 remains largely unclear. Here we explored the role of PRMT-1 in mitochondrial function as hinted by a two-dimensional Western blot-based proteomic study...
March 15, 2017: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/27935040/network-based-characterization-of-the-synaptic-proteome-reveals-that-removal-of-epigenetic-regulator-prmt8-restricts-proteins-associated-with-synaptic-maturation
#13
Patrick Kia Ming Lee, Wilson Wen Bin Goh, Judy Chia Ghee Sng
The brain adapts to dynamic environmental conditions by altering its epigenetic state, thereby influencing neuronal transcriptional programs. An example of an epigenetic modification is protein methylation, catalyzed by protein arginine methyltransferases (PRMT). One member, Prmt8, is selectively expressed in the central nervous system during a crucial phase of early development, but little else is known regarding its function. We hypothesize Prmt8 plays a role in synaptic maturation during development. To evaluate this, we used a proteome-wide approach to characterize the synaptic proteome of Prmt8 knockout versus wild-type mice...
December 9, 2016: Journal of Neurochemistry
https://www.readbyqxmd.com/read/27897114/ureas-applications-in-drug-design-and-development
#14
Ajit Dhananjay Jagtap, Nagendra Bharatrao Kondekar, Amit A Sadani, Ji-Wang Chern
The unique hydrogen binding capabilities of ureas make them an important functional group to make drug-target interactions and thus incorporated in small molecules displaying broad range of bioactivities. The related research and numerous excellent achievements of ureas applicability in drug design for the modulation of selectivity, stability, toxicity and pharmacokinetic profile of lead molecules have become active topic. This review aims to provide insights in to the significance of urea in drug design by summarizing successful studies of various urea derivatives as modulators biological targets (viz...
November 29, 2016: Current Medicinal Chemistry
https://www.readbyqxmd.com/read/27872854/identification-of-novel-inhibitors-against-coactivator-associated-arginine-methyltransferase-1-based-on-virtual-screening-and-biological-assays
#15
Fei Ye, Weiyao Zhang, Wenchao Lu, Yiqian Xie, Hao Jiang, Jia Jin, Cheng Luo
Overexpression of coactivator associated arginine methyltransferase 1 (CARM1), a protein arginine N-methyltransferase (PRMT) family enzyme, is associated with various diseases including cancers. Consequently, the development of small-molecule inhibitors targeting PRMTs has significant value for both research and therapeutic purposes. In this study, together with structure-based virtual screening with biochemical assays, two compounds DC_C11 and DC_C66 were identified as novel inhibitors of CARM1. Cellular studies revealed that the two inhibitors are cell membrane permeable and effectively blocked proliferation of cancer cells including HELA, K562, and MCF7...
2016: BioMed Research International
https://www.readbyqxmd.com/read/27834681/transient-kinetics-define-a-complete-kinetic-model-for-protein-arginine-methyltransferase-1
#16
Hao Hu, Cheng Luo, Y George Zheng
Protein arginine methyltransferases (PRMTs) are the enzymes responsible for posttranslational methylation of protein arginine residues in eukaryotic cells, particularly within the histone tails. A detailed mechanistic model of PRMT-catalyzed methylation is currently lacking, but it is essential for understanding the functions of PRMTs in various cellular pathways and for efficient design of PRMT inhibitors as potential treatments for a range of human diseases. In this work, we used stopped-flow fluorescence in combination with global kinetic simulation to dissect the transient kinetics of PRMT1, the predominant type I arginine methyltransferase...
December 23, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27780782/atprmt5-regulates-shoot-regeneration-through-mediating-histone-h4r3-dimethylation-on-krps-and-pre-mrna-splicing-of-rkp-in-arabidopsis
#17
Hui Liu, Xu Ma, Hua Nan Han, Yu Jin Hao, Xian Sheng Zhang
Protein arginine methylation plays important roles in diverse biological processes, but its role in regulating shoot regeneration remains elusive. In this study, we characterized the function of the protein arginine methyltransferase AtPRMT5 during de novo shoot regeneration in Arabidopsis. AtPRMT5 encodes a type II protein arginine methyltransferase that methylates proteins, including histones and RNA splicing factors. The frequency of shoot regeneration and the number of shoots per callus were decreased in the atprmt5 mutant compared with those in the wild type...
December 5, 2016: Molecular Plant
https://www.readbyqxmd.com/read/27604291/intracerebral-administration-of-s-adenosylhomocysteine-or-s-adenosylmethionine-attenuates-the-increases-in-the-cortical-extracellular-levels-of-dimethylarginines-without-affecting-cgmp-level-in-rats-with-acute-liver-failure
#18
Anna Czarnecka, Krzysztof Milewski, Radosław Jaźwiec, Magdalena Zielińska
Alterations in brain nitric oxide (NO)/cGMP synthesis contribute to the pathogenesis of hepatic encephalopathy (HE). An increased asymmetrically dimethylated derivative of L-arginine (ADMA), an endogenous inhibitor of NO synthases, was observed in plasma of HE patients and animal models. It is not clear whether changes in brain ADMA reflect its increased local synthesis therefore affecting NO/cGMP pathway, or are a consequence of its increased peripheral blood content. We measured extracellular concentration of ADMA and symmetrically dimethylated isoform (SDMA) in the prefrontal cortex of control and thioacetamide (TAA)-induced HE rats...
January 2017: Neurotoxicity Research
https://www.readbyqxmd.com/read/27601476/arginine-demethylation-of-g3bp1-promotes-stress-granule-assembly
#19
Wei-Chih Tsai, Sitaram Gayatri, Lucas C Reineke, Gianluca Sbardella, Mark T Bedford, Richard E Lloyd
Stress granules (SGs) are cytoplasmic condensates of stalled messenger ribonucleoprotein complexes (mRNPs) that form when eukaryotic cells encounter environmental stress. RNA-binding proteins are enriched for arginine methylation and facilitate SG assembly through interactions involving regions of low amino acid complexity. How methylation of specific RNA-binding proteins regulates RNA granule assembly has not been characterized. Here, we examined the potent SG-nucleating protein Ras-GAP SH3-binding protein 1 (G3BP1), and found that G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain...
October 21, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27577262/proteome-wide-analysis-of-arginine-monomethylation-reveals-widespread-occurrence-in-human-cells
#20
Sara C Larsen, Kathrine B Sylvestersen, Andreas Mund, David Lyon, Meeli Mullari, Maria V Madsen, Jeremy A Daniel, Lars J Jensen, Michael L Nielsen
The posttranslational modification of proteins by arginine methylation is functionally important, yet the breadth of this modification is not well characterized. Using high-resolution mass spectrometry, we identified 8030 arginine methylation sites within 3300 human proteins in human embryonic kidney 293 cells, indicating that the occurrence of this modification is comparable to phosphorylation and ubiquitylation. A site-level conservation analysis revealed that arginine methylation sites are less evolutionarily conserved compared to arginines that were not identified as modified by methylation...
2016: Science Signaling
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