Showing 1-8 of 8 results for "hpa018976"
Joyce Sayegh et al.
The Journal of biological chemistry, 282(50), 36444-36453 (2007-10-11)
Human protein arginine methyltransferase PRMT8 has been recently described as a type I enzyme in brain that is localized to the plasma membrane by N-terminal myristoylation. The amino acid sequence of human PRMT8 is almost 80% identical to human PRMT1...
Rene Meyer et al.
The Journal of steroid biochemistry and molecular biology, 107(1-2), 1-14 (2007-06-26)
The basal transcriptional activity of nuclear receptors (NRs) is regulated by interactions with additional comodulator proteins (coactivator/corepressor). Here, we describe a new androgen receptor (AR)-associated coactivator, PRMT2, which belongs to the arginine methyltransferase protein family. To search for AR-interacting proteins...
Chao Qi et al.
The Journal of biological chemistry, 277(32), 28624-28630 (2002-06-01)
In an attempt to isolate cofactors capable of influencing estrogen receptor alpha (ERalpha) transcriptional activity, we used yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ERalpha-binding protein. PRMT2 interacted directly with three ERalpha regions including...
Lakshmanan Ganesh et al.
Molecular and cellular biology, 26(10), 3864-3874 (2006-05-02)
The protein arginine methyltransferases (PRMTs) include a family of proteins with related putative methyltransferase domains that modify chromatin and regulate cellular transcription. Although some family members, PRMT1 and PRMT4, have been implicated in transcriptional modulation or intracellular signaling, the roles...
Soo Jung Lee et al.
PloS one, 15(1), e0227672-e0227672 (2020-01-17)
A large number of pre-clinical and developmental investigations involve experimental vertebrate animals, of which mice have emerged as a favored organism. Recognition of the differences between humans and mice is essential for assessment of the relevance of animal studies to...
Ted M Lakowski et al.
The Biochemical journal, 421(2), 253-261 (2009-05-02)
Protein arginine N-methyltransferases (PRMTs) methylate arginine residues within proteins using S-adenosyl-L-methionine (AdoMet) to form S-adenosyl-L-homocysteine and methylarginine residues. All PRMTs produce omega-NG-monomethylarginine (MMA) residues and either asymmetric omega-N(G),N(G)-dimethylarginine (aDMA) or symmetric omega-N(G),N'(G)-dimethylarginine (sDMA) residues, referred to as Type I or...
Magnolia L Pak et al.
Biochemistry, 50(38), 8226-8240 (2011-08-20)
Protein arginine N-methyltransferases (PRMTs) act in signaling pathways and gene expression by methylating arginine residues within target proteins. PRMT1 is responsible for most cellular arginine methylation activity and can work independently or in collaboration with other PRMTs. In this study...
G Poelmans et al.
American journal of medical genetics. Part B, Neuropsychiatric genetics : the official publication of the International Society of Psychiatric Genetics, 150B(1), 140-147 (2008-06-04)
Dyslexia is the most common childhood learning disorder and it is a significantly heritable trait. At least nine chromosomal loci have been linked to dyslexia, and additional susceptibility loci on other chromosomes have been suggested. Within two of these loci...

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