Strobl et al., Vienna, Austria. In Bmc Cell Biol, 2009
Using microarray and RT-qPCR, we furthermore show that Oct-6 is involved in the regulation of transcriptional responses to dsRNA, in particular in the gene regulation of serine/threonine protein kinase 40 (Stk40) and U7 snRNA-associated Sm-like protein Lsm10 (Lsm10).
Stein et al., Worcester, United States. In J Cell Physiol, 2009
The subnuclear organization of histone gene regulatory proteins and 3' end processing factors (NPAT/LSM10) of normal somatic and embryonic stem cells is compromised in selected human cancer cell types.
Stein et al., Worcester, United States. In Proc Natl Acad Sci U S A, 2008
Our results demonstrate that regulatory complexes that mediate transcriptional initiation (e.g., p220(NPAT)) and 3'-end processing (e.g., Lsm10, Lsm11, and SLBP) of histone gene transcripts colocalize at histone gene loci in dedicated subnuclear foci (histone locus bodies) that are distinct from Cajal bodies.
Schümperli et al., Bern, Switzerland. In J Biol Chem, 2005
Lsm10 and Lsm11, which replace the Sm proteins D1 and D2 in the histone RNA processing U7 snRNPs, associate with pICln in vitro and in vivo without receiving sDMA modifications and with PRMT5 and SMN complexes
Pillai et al., Bern, Switzerland. In Cell Mol Life Sci, 2004
In contrast to spliceosomal snRNPs, which contain a ring-shaped assembly of seven so-called Sm proteins, in the U7 snRNP the Sm proteins D1 and D2 are replaced by U7-specific Sm-like proteins, Lsm10 and Lsm11.
Schümperli et al., Bern, Switzerland. In Genes Dev, 2003
The U7 snRNP involved in histone RNA 3' processing contains a structurally similar but biochemically unique Sm core in which two of these proteins, Sm D1 and D2, are replaced by Lsm10 and by another as yet unknown component.