Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization.

The EMBO journal - 14 Jul 2015

Neuenkirchen Nils, Englbrecht Clemens, Ohmer Jürgen, Ziegenhals Thomas, Chari Ashwin, Fischer Utz

Abstract excerpt

The assembly of spliceosomal U snRNPs depends on the coordinated action of PRMT5 and SMN complexes in vivo. These trans-acting factors enable the faithful delivery of seven Sm proteins onto snRNA and the formation of the common core of snRNPs. To gain mechanistic insight into their mode of action, we reconstituted the assembly machinery from recombinant sources. We uncover a stepwise and ordered formation of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Minor Histocompatibility Antigens
Share to Muscular Atrophy, Spinal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein-Arginine N-Methyltransferases

Share to Recombinant Proteins

Share to Ribonucleoproteins, Small Nuclear

Share to RNA, Small Nuclear

Share to SMN Complex Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 26069323
DOI: 10.15252/embj.201490350
PMCID: PMC4547896

Genes

PRMT5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization.PMID 26069323Read ↗

Spinal Muscular Atrophy: From Defective Chaperoning of snRNP Assembly to Neuromuscular DysfunctionSemantic proximity Read ↗

Negative cooperativity between Gemin2 and RNA provides insights into RNA selection and the SMN complex's release in snRNP assemblySemantic proximity Read ↗

A Comprehensive Interaction Map of the Human Survival of Motor Neuron (SMN) ComplexSemantic proximity Read ↗

Structural requirements for protein-catalyzed annealing of U4 and U6 RNAs during di-snRNP assembly.Semantic proximity Read ↗

Essential Role for the Tudor Domain of SMN in Spliceosomal U snRNP Assembly: Implications for Spinal Muscular AtrophySemantic proximity Read ↗

Evolutionary diversification of the Sm family of RNA-associated proteins.Semantic proximity Read ↗

Identification and structural analysis of the Schizosaccharomyces pombe SMN complex.Semantic proximity Read ↗

Emerging Roles of Gemin5: From snRNPs Assembly to Translation ControlSemantic proximity Read ↗

U1 snRNP-Specific U1C Acts as the Gatekeeper of the Survival of Motor Neurons (SMN) Complex in snRNP BiogenesisSemantic proximity Read ↗

Spliceosomal small nuclear ribonucleoprotein biogenesis defects and motor neuron selectivity in spinal muscular atrophy.Semantic proximity Read ↗

SMN controls neuromuscular junction integrity through U7 snRNPSemantic proximity Read ↗

Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.