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

Functional and Biochemical Characterization of Dib1's Role in Pre-Messenger RNA Splicing.

Journal of molecular biology - 25 May 2018

Schreib Christian C, Bowman Emily K, Hernandez Cody A, Lucas Amber L, Potts Camille H S, Maeder Corina

Abstract excerpt

The spliceosome is a dynamic macromolecular machine that undergoes a series of conformational rearrangements as it transitions between the several states required for accurate splicing. The transition from the B to Bact is a key part of spliceosome assembly and is defined by the departure of several proteins, including essential U5 component Dib1. Recent structural studies suggest that Dib1 has a role in...

Read the complete abstract on PubMed

Topics

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

Share to DNA Helicases
Share to Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Folding

Share to RNA Precursors

Share to RNA, Small Nuclear

Share to RNA Splicing

Share to Saccharomyces cerevisiae Proteins

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 29715471
DOI: 10.1016/j.jmb.2018.04.027
PMCID: PMC6155989

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

Functional and Biochemical Characterization of Dib1's Role in Pre-Messenger RNA Splicing.PMID 29715471Read ↗

A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity.Semantic proximity Read ↗

Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1.Semantic proximity Read ↗

Structural and mechanistic basis for preferential deadenylation of U6 snRNA by Usb1.Semantic proximity Read ↗

"Nought may endure but mutability": spliceosome dynamics and the regulation of splicing.Semantic proximity Read ↗

Structure of the yeast spliceosomal postcatalytic P complex.Semantic proximity Read ↗

An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p.Semantic proximity Read ↗

Spliceosome-mediated decay (SMD) regulates expression of nonintronic genes in budding yeast.Semantic proximity Read ↗

The debranching enzyme Dbr1 regulates lariat turnover and intron splicingSemantic proximity Read ↗

Biochemical characterization and crystal structure of a Dim1 family associated protein: Dim2.Semantic proximity Read ↗

Dynamics of the DEAD-box ATPase Prp5 RecA-like domains provide a conformational switch during spliceosome assembly.Semantic proximity Read ↗

Characterization of a Brg1 hypomorphic allele demonstrates that genetic and biochemical activity are tightly correlated.Semantic proximity Read ↗

Structures of aberrant spliceosome intermediates on their way to disassemblySemantic proximity Read ↗

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