395 related articles for article (PubMed ID: 22241471)
1. Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.
Zurita-Lopez CI; Sandberg T; Kelly R; Clarke SG
J Biol Chem; 2012 Mar; 287(11):7859-70. PubMed ID: 22241471
[TBL] [Abstract][Full Text] [Related]
2. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins.
Branscombe TL; Frankel A; Lee JH; Cook JR; Yang Z; Pestka S; Clarke S
J Biol Chem; 2001 Aug; 276(35):32971-6. PubMed ID: 11413150
[TBL] [Abstract][Full Text] [Related]
3. Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.
Miranda TB; Sayegh J; Frankel A; Katz JE; Miranda M; Clarke S
Biochem J; 2006 May; 395(3):563-70. PubMed ID: 16426232
[TBL] [Abstract][Full Text] [Related]
4. Mammalian protein arginine methyltransferase 7 (PRMT7) specifically targets RXR sites in lysine- and arginine-rich regions.
Feng Y; Maity R; Whitelegge JP; Hadjikyriacou A; Li Z; Zurita-Lopez C; Al-Hadid Q; Clark AT; Bedford MT; Masson JY; Clarke SG
J Biol Chem; 2013 Dec; 288(52):37010-25. PubMed ID: 24247247
[TBL] [Abstract][Full Text] [Related]
5. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity.
Miranda TB; Miranda M; Frankel A; Clarke S
J Biol Chem; 2004 May; 279(22):22902-7. PubMed ID: 15044439
[TBL] [Abstract][Full Text] [Related]
6. PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine.
Lee JH; Cook JR; Yang ZH; Mirochnitchenko O; Gunderson SI; Felix AM; Herth N; Hoffmann R; Pestka S
J Biol Chem; 2005 Feb; 280(5):3656-64. PubMed ID: 15494416
[TBL] [Abstract][Full Text] [Related]
7. Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.
Feng Y; Hadjikyriacou A; Clarke SG
J Biol Chem; 2014 Nov; 289(47):32604-16. PubMed ID: 25294873
[TBL] [Abstract][Full Text] [Related]
8. Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases.
Jain K; Jin CY; Clarke SG
Proc Natl Acad Sci U S A; 2017 Sep; 114(38):10101-10106. PubMed ID: 28874563
[TBL] [Abstract][Full Text] [Related]
9. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4.
Lakowski TM; Frankel A
Biochem J; 2009 Jun; 421(2):253-61. PubMed ID: 19405910
[TBL] [Abstract][Full Text] [Related]
10. Histone H2A and H4 N-terminal tails are positioned by the MEP50 WD repeat protein for efficient methylation by the PRMT5 arginine methyltransferase.
Burgos ES; Wilczek C; Onikubo T; Bonanno JB; Jansong J; Reimer U; Shechter D
J Biol Chem; 2015 Apr; 290(15):9674-89. PubMed ID: 25713080
[TBL] [Abstract][Full Text] [Related]
11. PRMT7 as a unique member of the protein arginine methyltransferase family: A review.
Jain K; Clarke SG
Arch Biochem Biophys; 2019 Apr; 665():36-45. PubMed ID: 30802433
[TBL] [Abstract][Full Text] [Related]
12. The macromolecular complexes of histones affect protein arginine methyltransferase activities.
Fulton MD; Cao M; Ho MC; Zhao X; Zheng YG
J Biol Chem; 2021 Oct; 297(4):101123. PubMed ID: 34492270
[TBL] [Abstract][Full Text] [Related]
13. Hsl7 is a substrate-specific type II protein arginine methyltransferase in yeast.
Sayegh J; Clarke SG
Biochem Biophys Res Commun; 2008 Aug; 372(4):811-5. PubMed ID: 18515076
[TBL] [Abstract][Full Text] [Related]
14. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation.
Tang J; Gary JD; Clarke S; Herschman HR
J Biol Chem; 1998 Jul; 273(27):16935-45. PubMed ID: 9642256
[TBL] [Abstract][Full Text] [Related]
15. A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism.
Lakowski TM; Frankel A
J Biol Chem; 2008 Apr; 283(15):10015-25. PubMed ID: 18263580
[TBL] [Abstract][Full Text] [Related]
16. Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-site Architectures.
Jain K; Warmack RA; Debler EW; Hadjikyriacou A; Stavropoulos P; Clarke SG
J Biol Chem; 2016 Aug; 291(35):18299-308. PubMed ID: 27387499
[TBL] [Abstract][Full Text] [Related]
17. PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain.
Frankel A; Clarke S
J Biol Chem; 2000 Oct; 275(42):32974-82. PubMed ID: 10931850
[TBL] [Abstract][Full Text] [Related]
18. The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites.
Bondoc TJ; Lowe TL; Clarke SG
PLoS One; 2023; 18(5):e0285812. PubMed ID: 37216364
[TBL] [Abstract][Full Text] [Related]
19. Computational Study of Symmetric Methylation on Histone Arginine Catalyzed by Protein Arginine Methyltransferase PRMT5 through QM/MM MD and Free Energy Simulations.
Yue Y; Chu Y; Guo H
Molecules; 2015 May; 20(6):10032-46. PubMed ID: 26035101
[TBL] [Abstract][Full Text] [Related]
20. Unique Features of Human Protein Arginine Methyltransferase 9 (PRMT9) and Its Substrate RNA Splicing Factor SF3B2.
Hadjikyriacou A; Yang Y; Espejo A; Bedford MT; Clarke SG
J Biol Chem; 2015 Jul; 290(27):16723-43. PubMed ID: 25979344
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
