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

Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals.

Journal of molecular biology - 4 Jan 2008

Deka Pritilekha, Bucheli Miriam E, Moore Claire, Buratowski Stephen, Varani Gabriele

Abstract excerpt

Yeast Npl3 is homologous to SR proteins in higher eukaryotes, a family of RNA-binding proteins that have multiple essential roles in RNA metabolism. This protein competes with 3'-end processing factors for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. The NMR structure of...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cross-Linking Reagents
Share to Models, Chemical

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to RNA-Binding Proteins

Share to Serine

Share to Static Electricity

Share to Ultraviolet Rays

Source

Open in PubMed Open full text

Identifiers

PMID: 18022637
DOI: 10.1016/j.jmb.2007.09.029
PMCID: PMC2214835

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals.PMID 18022637Read ↗

Yeast Nop3p has structural and functional similarities to mammalian pre-mRNA binding proteins.Semantic proximity Read ↗

NOP3 is an essential yeast protein which is required for pre-rRNA processing.Semantic proximity Read ↗

The shuttling protein Npl3 promotes translation termination accuracy in Saccharomyces cerevisiae.Semantic proximity Read ↗

Structural and functional analyses of SARS-CoV-2 Nsp3 and its specific interactions with the 5’ UTR of the viral genomeSemantic proximity Read ↗

A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting.Semantic proximity Read ↗

Potential RNA binding proteins in Saccharomyces cerevisiae identified as suppressors of temperature-sensitive mutations in NPL3.Semantic proximity Read ↗

Structures of nonsense-mediated mRNA decay factors UPF3B and UPF3A in complex with UPF2 reveal molecular basis for competitive binding and for neurodevelopmental disorder-causing mutation.Semantic proximity Read ↗

Effects of the yeast RNA-binding protein Whi3 on the half-life and abundance of CLN3 mRNA and other targets.Semantic proximity Read ↗

The mitochondrial protein targeting suppressor (mts1) mutation maps to the mRNA-binding domain of Npl3p and affects translation on cytoplasmic polysomes.Semantic proximity Read ↗

Npl3 is an antagonist of mRNA 3' end formation by RNA polymerase II.Semantic proximity Read ↗

An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors.Semantic proximity Read ↗

Whi3, a developmental regulator of budding yeast, binds a large set of mRNAs functionally related to the endoplasmic reticulum.Semantic proximity Read ↗

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