Log in

Relevant bibliographies by topics / Protein arginine methyltransferase

Contents

Journal articles

Academic literature on the topic 'Protein arginine methyltransferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Protein arginine methyltransferase.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Protein arginine methyltransferase"

1

Yan, Dongsheng, Yong Zhang, Lifang Niu, Yi Yuan, and Xiaofeng Cao. "Identification and characterization of two closely related histone H4 arginine 3 methyltransferases in Arabidopsis thaliana." Biochemical Journal 408, no. 1 (2007): 113–21. http://dx.doi.org/10.1042/bj20070786.

Full text

Abstract:

Arginine methylation of histone H3 and H4 plays important roles in transcriptional regulation in eukaryotes such as yeasts, fruitflies, nematode worms, fish and mammals; however, less is known in plants. In the present paper, we report the identification and characterization of two Arabidopsis thaliana protein arginine N-methyltransferases, AtPRMT1a and AtPRMT1b, which exhibit high homology with human PRMT1. Both AtPRMT1a and AtPRMT1b methylated histone H4, H2A, and myelin basic protein in vitro. Site-directed mutagenesis of the third arginine (R3) on the N-terminus of histone H4 to lysine (H4

APA, Harvard, Vancouver, ISO, and other styles

2

BOULANGER, Marie-Chloé, Tina Branscombe MIRANDA, Steven CLARKE, et al. "Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4." Biochemical Journal 379, no. 2 (2004): 283–89. http://dx.doi.org/10.1042/bj20031176.

Full text

Abstract:

The role of arginine methylation in Drosophila melanogaster is unknown. We identified a family of nine PRMTs (protein arginine methyltransferases) by sequence homology with mammalian arginine methyltransferases, which we have named DART1 to DART9 (Drosophilaarginine methyltransferases 1–9). In keeping with the mammalian PRMT nomenclature, DART1, DART4, DART5 and DART7 are the putative homologues of PRMT1, PRMT4, PRMT5 and PRMT7. Other DART family members have a closer resemblance to PRMT1, but do not have identifiable homologues. All nine genes are expressed in Drosophila at various developmen

APA, Harvard, Vancouver, ISO, and other styles

3

Cheung, Ngai, Li Chong Chan, Alex Thompson, Michael L. Cleary, and Chi Wai Eric So. "Protein arginine-methyltransferase-dependent oncogenesis." Nature Cell Biology 9, no. 10 (2007): 1208–15. http://dx.doi.org/10.1038/ncb1642.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Mowen, K. A., and M. David. "Analysis of Protein Arginine Methylation and Protein Arginine-Methyltransferase Activity." Science Signaling 2001, no. 93 (2001): pl1. http://dx.doi.org/10.1126/stke.2001.93.pl1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Gou, Qing, ShuJiao He, and ZeJian Zhou. "Protein arginine N-methyltransferase 1 promotes the proliferation and metastasis of hepatocellular carcinoma cells." Tumor Biology 39, no. 2 (2017): 101042831769141. http://dx.doi.org/10.1177/1010428317691419.

Full text

Abstract:

Hepatocellular carcinoma is the most common subtype of liver cancer. Protein arginine N-methyltransferase 1 was shown to be upregulated in various cancers. However, the role of protein arginine N-methyltransferase 1 in hepatocellular carcinoma progression remains incompletely understood. We investigated the clinical and functional significance of protein arginine N-methyltransferase 1 in a series of clinical hepatocellular carcinoma samples and a panel of hepatocellular carcinoma cell lines. We performed suppression analysis of protein arginine N-methyltransferase 1 using small interfering RNA

APA, Harvard, Vancouver, ISO, and other styles

6

Al-Hamashi, Ayad A., Krystal Diaz, and Rong Huang. "Non-Histone Arginine Methylation by Protein Arginine Methyltransferases." Current Protein & Peptide Science 21, no. 7 (2020): 699–712. http://dx.doi.org/10.2174/1389203721666200507091952.

Full text

Abstract:

Protein arginine methyltransferase (PRMT) enzymes play a crucial role in RNA splicing, DNA damage repair, cell signaling, and differentiation. Arginine methylation is a prominent posttransitional modification of histones and various non-histone proteins that can either activate or repress gene expression. The aberrant expression of PRMTs has been linked to multiple abnormalities, notably cancer. Herein, we review a number of non-histone protein substrates for all nine members of human PRMTs and how PRMT-mediated non-histone arginine methylation modulates various diseases. Additionally, we high

APA, Harvard, Vancouver, ISO, and other styles

7

Côté, Jocelyn, Franc˛ois-Michel Boisvert, Marie-Chloé Boulanger, Mark T. Bedford, and Stéphane Richard. "Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1." Molecular Biology of the Cell 14, no. 1 (2003): 274–87. http://dx.doi.org/10.1091/mbc.e02-08-0484.

Full text

Abstract:

RNA binding proteins often contain multiple arginine glycine repeats, a sequence that is frequently methylated by protein arginine methyltransferases. The role of this posttranslational modification in the life cycle of RNA binding proteins is not well understood. Herein, we report that Sam68, a heteronuclear ribonucleoprotein K homology domain containing RNA binding protein, associates with and is methylated in vivo by the protein arginineN-methyltransferase 1 (PRMT1). Sam68 contains asymmetrical dimethylarginines near its proline motif P3 as assessed by using a novel asymmetrical dimethylarg

APA, Harvard, Vancouver, ISO, and other styles

8

van Haren, Matthijs J., Nils Marechal, Nathalie Troffer-Charlier, et al. "Transition state mimics are valuable mechanistic probes for structural studies with the arginine methyltransferase CARM1." Proceedings of the National Academy of Sciences 114, no. 14 (2017): 3625–30. http://dx.doi.org/10.1073/pnas.1618401114.

Full text

Abstract:

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. These constructs were found to be potent CARM1 inhibitors and also formed stable comple

APA, Harvard, Vancouver, ISO, and other styles

9

Gupta, Somlee, Rajashekar Varma Kadumuri, Anjali Kumari Singh, Sreenivas Chavali, and Arunkumar Dhayalan. "Structure, Activity and Function of the Protein Arginine Methyltransferase 6." Life 11, no. 9 (2021): 951. http://dx.doi.org/10.3390/life11090951.

Full text

Abstract:

Members of the protein arginine methyltransferase (PRMT) family methylate the arginine residue(s) of several proteins and regulate a broad spectrum of cellular functions. Protein arginine methyltransferase 6 (PRMT6) is a type I PRMT that asymmetrically dimethylates the arginine residues of numerous substrate proteins. PRMT6 introduces asymmetric dimethylation modification in the histone 3 at arginine 2 (H3R2me2a) and facilitates epigenetic regulation of global gene expression. In addition to histones, PRMT6 methylates a wide range of cellular proteins and regulates their functions. Here, we di

APA, Harvard, Vancouver, ISO, and other styles

10

Cha, Boksik, Yaerin Park, Byul Nim Hwang, So-young Kim, and Eek-hoon Jho. "Protein Arginine Methyltransferase 1 Methylates Smurf2." Molecules and Cells 38, no. 8 (2015): 723–28. http://dx.doi.org/10.14348/molcells.2015.0113.

Full text

APA, Harvard, Vancouver, ISO, and other styles

More sources

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!