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

Essential yeast protein with unexpected similarity to subunits of mammalian cleavage and polyadenylation specificity factor (CPSF).

Science (New York, N.Y.) - 29 Nov 1996

Chanfreau G, Noble S M, Guthrie C

Abstract excerpt

The 3' ends of most eukaryotic messenger RNAs are generated by internal cleavage and polyadenylation. In mammals, there is a strict dependence of both reactions on the sequence AAUAAA, which occurs upstream of polyadenylation [poly(A)] sites and which is recognized by CPSF. In contrast, cis-acting signals for yeast 3'-end generation are highly divergent from those of mammals, suggesting that trans-acting factors...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Cattle

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to RNA, Messenger

Share to Saccharomyces cerevisiae

Source

Identifiers

PMID: 8929408
DOI: 10.1126/science.274.5292.1511

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Essential yeast protein with unexpected similarity to subunits of mammalian cleavage and polyadenylation specificity factor (CPSF).PMID 8929408Read ↗

RBBP6 activates the pre-mRNA 3’-end processing machinery in humansSemantic proximity Read ↗

Pti1p and Ref2p found in association with the mRNA 3' end formation complex direct snoRNA maturation.Semantic proximity Read ↗

Functional analysis of yeast snoRNA and snRNA 3'-end formation mediated by uncoupling of cleavage and polyadenylation.Semantic proximity Read ↗

A multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor.Semantic proximity Read ↗

Molecular Insights into mRNA Polyadenylation and DeadenylationSemantic proximity Read ↗

Species-specific factors mediate extensive heterogeneity of mRNA 3' ends in yeasts.Semantic proximity Read ↗

Distinct roles of two Yth1p domains in 3'-end cleavage and polyadenylation of yeast pre-mRNAs.Semantic proximity Read ↗

The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3'-end formation.Semantic proximity Read ↗

RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor.Semantic proximity Read ↗

3'-end-forming signals of yeast mRNA.Semantic proximity Read ↗

Coupling between snoRNP assembly and 3' processing controls box C/D snoRNA biosynthesis in yeast.Semantic proximity Read ↗

Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor.Semantic proximity Read ↗

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