Gary W Zieve
Affiliation: Stony Brook University
- The anti-Sm immune response in autoimmunity and cell biologyGary W Zieve
Department of Pathology, SUNY Stony Brook, Stony Brook, NY 11794 8691, USA
Autoimmun Rev 2:235-40. 2003..Current work on the snRNP particles is attempting to identify the features that predispose the common core proteins to become autoantigens in vulnerable individuals...
- The symmetrical dimethylarginine post-translational modification of the SmD3 protein is not required for snRNP assembly and nuclear transportPermanan R Khusial
Department of Pathology, Health Sciences Center, Stony Brook University, Stony Brook, NY 11794 8691, USA
Biochem Biophys Res Commun 337:1119-24. 2005..This suggests this modification is not essential for maturation of the SmD3 protein...
- LSm proteins form heptameric rings that bind to RNA via repeating motifsPermanan Khusial
Department of Pathology, Stony Brook University, Stony Brook, NY 11794 8691, USA
Trends Biochem Sci 30:522-8. 2005..The two different rings that transiently bind to RNAs and, thereby, assist in the degradation of mRNA in the cytoplasm and the maturation of a wide spectrum of RNAs in the nucleus are called LSm rings...
- Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleusTina Branscombe Miranda
Department of Chemistry and Biochemistry, Molecular Biology Institute, UCLA, Los Angeles, CA 90095 1569, USA
Biochem Biophys Res Commun 323:382-7. 2004..These results suggest that the activity responsible for the formation of asymmetric dimethylated arginine residues in Sm proteins is either PRMT5 or a protein associated with it in the immunoprecipitated complex...