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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

LSM10, U7 small nuclear RNA associated

Lsm10
Top mentioned proteins: Histone, SLBP, SmaI, CAN, CDK2
Papers on Lsm10
U7 small nuclear ribonucleoprotein represses histone gene transcription in cell cycle-arrested cells.
Hirose et al., Tokyo, Japan. In Proc Natl Acad Sci U S A, 2012
An analogous effect was observed upon depletion of Lsm10, a component of the U7 snRNP-specific Sm ring, with siRNA.
Interaction between FLASH and Lsm11 is essential for histone pre-mRNA processing in vivo in Drosophila.
Dominski et al., Chapel Hill, United States. In Rna, 2011
Formation of the histone mRNA 3' end requires the U7 snRNP, which contains Lsm10 and Lsm11, and FLASH, a processing factor that binds Lsm11.
Octamer-binding factor 6 (Oct-6/Pou3f1) is induced by interferon and contributes to dsRNA-mediated transcriptional responses.
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).
The Drosophila U7 snRNP proteins Lsm10 and Lsm11 are required for histone pre-mRNA processing and play an essential role in development.
Duronio et al., Chapel Hill, United States. In Rna, 2009
U7 snRNP contains two like-Sm proteins, Lsm10 and Lsm11, which replace SmD1 and SmD2 in the canonical heptameric Sm protein ring that binds spliceosomal snRNAs.
Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA.
Dominski et al., Chapel Hill, United States. In Mol Cell Biol, 2009
The region between the cleavage site and the U7-binding site interacts with three low-molecular-weight proteins, which were identified as components of the U7-specific Sm core: SmB, SmD3, and Lsm10.
The subnuclear organization of histone gene regulatory proteins and 3' end processing factors of normal somatic and embryonic stem cells is compromised in selected human cancer cell types.
GeneRIF
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.
Staged assembly of histone gene expression machinery at subnuclear foci in the abbreviated cell cycle of human embryonic stem cells.
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.
ZFP100, a component of the active U7 snRNP limiting for histone pre-mRNA processing, is required for entry into S phase.
GeneRIF
Marzluff et al., Chapel Hill, United States. In Mol Cell Biol, 2006
The overexpression of Lsm10 and Lsm11 increases the cellular levels of U7 snRNP but has no effect on histone pre-mRNA processing.
Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes.
GeneRIF
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
The special Sm core structure of the U7 snRNP: far-reaching significance of a small nuclear ribonucleoprotein.
Review
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.
Evolutionary conservation of the U7 small nuclear ribonucleoprotein in Drosophila melanogaster.
Schumperli et al., Bern, Switzerland. In Rna, 2003
The missing Sm D1 and D2 subunits are replaced by U7-specific Sm-like proteins Lsm10 and Lsm11, at least the latter of which is important for histone RNA processing.
Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing.
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.
Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein.
GeneRIF
Müller et al., Bern, Switzerland. In Embo J, 2001
Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein.
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