4.6 Article

Role of pICLn in Methylation of Sm Proteins by PRMT5

Related references

Note: Only part of the references are listed.
Review Biochemistry & Molecular Biology

Protein Arginine Methylation in Mammals: Who, What, and Why

Mark T. Bedford et al.

MOLECULAR CELL (2009)

Article Biochemistry & Molecular Biology

An Assembly Chaperone Collaborates with the SMN Complex to Generate Spliceosomal SnRNPs

Ashwin Chari et al.

Article Biochemistry & Molecular Biology

The protein arginine methyltransferase Prmt5 is required for myogenesis because it facilitates ATP-dependent chromatin remodeling

Caroline S. Dacwag et al.

MOLECULAR AND CELLULAR BIOLOGY (2007)

Article Biochemistry & Molecular Biology

The Sm-protein methyltransferase, dart5, is essential for germ-cell specification and maintenance

Graydon B. Gonsalvez et al.

CURRENT BIOLOGY (2006)

Article Biochemistry & Molecular Biology

MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties

X Le Guezennec et al.

MOLECULAR AND CELLULAR BIOLOGY (2006)

Article Biochemistry & Molecular Biology

ICln159 folds into a pleckstrin homology domain-like structure

J Fürst et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2005)

Article Biochemistry & Molecular Biology

Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver

Y Lim et al.

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (2005)

Review Biochemistry & Molecular Biology

Arginine methylation: An emerging regulator of protein function

MT Bedford et al.

MOLECULAR CELL (2005)

Article Biochemistry & Molecular Biology

Reconstitution of two recombinant LSm protein complexes reveals aspects of their architecture, assembly, and function

B Zaric et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2005)

Article Biochemistry & Molecular Biology

The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner

W Jiang et al.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2005)

Article Biochemistry & Molecular Biology

PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine

JH Lee et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2005)

Article Biochemistry & Molecular Biology

Phosphorylation regulates the activity of the SMN complex during assembly of spliceosomal U snRNPs

M Grimmler et al.

EMBO REPORTS (2005)

Article Multidisciplinary Sciences

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

L Pellizzoni et al.

SCIENCE (2002)

Article Biochemistry & Molecular Biology

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

G Meister et al.

EMBO JOURNAL (2002)

Article Biochemistry & Molecular Biology

Negative regulation of transcription by the type II arginine methyltransferase PRMT5

E Fabbrizio et al.

EMBO REPORTS (2002)

Article Biochemistry & Molecular Biology

A novel WD repeat protein component of the methylosome binds Sm proteins

WJ Friesen et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2002)

Article Biochemistry & Molecular Biology

Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln

G Meister et al.

CURRENT BIOLOGY (2001)

Article Biochemistry & Molecular Biology

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

WJ Friesen et al.

MOLECULAR AND CELLULAR BIOLOGY (2001)

Article Biochemistry & Molecular Biology

PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins

TL Branscombe et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2001)

Article Biochemistry & Molecular Biology

The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1

L Pellizzoni et al.

CURRENT BIOLOGY (2001)

Review Cell Biology

Spliceosomal UsnRNP biogenesis, structure and function

CL Will et al.

CURRENT OPINION IN CELL BIOLOGY (2001)

Article Biochemistry & Molecular Biology

PRMT5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family

J Rho et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2001)

Article Biochemistry & Molecular Biology

Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

X Zhang et al.

EMBO JOURNAL (2000)

Article Biochemistry & Molecular Biology

ICln is essential for cellular and early embryonic viability

WT Pu et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2000)