Unrip is a component of SMN complexes active in snRNP assembly (Q28246568)

7

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Jennifer Baccon

Jennifer Baccon

2

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Claudia Carissimi

Claudia Carissimi

1

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Alan Sawyer

Alan Sawyer

6

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Marco Straccia

Marco Straccia

3

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Livio Pellizzoni

Livio Pellizzoni

8

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author name string

Pieranna Chiarella

4

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Alessio Maiolica

Spliceosomal UsnRNP biogenesis, structure and function

5

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language of work or name

English

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publication date

25 April 2005

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published in

FEBS Letters

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volume

579

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page(s)

2348-54

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issue

11

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cites work

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SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets

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The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins

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A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs

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Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs

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Essential role for the SMN complex in the specificity of snRNP assembly

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snRNAs contain specific SMN-binding domains that are essential for snRNP assembly

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Sequence-specific interaction of U1 snRNA with the SMN complex

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The SMN complex, an assemblyosome of ribonucleoproteins

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Identification and characterization of a spinal muscular atrophy-determining gene

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Identification and characterization of Gemin7, a novel component of the survival of motor neuron complex

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Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems

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Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli

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The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins

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Purification of native survival of motor neurons complexes and identification of Gemin6 as a novel component

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Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins

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Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry

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unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA

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SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins.

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Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein

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