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

A multifunctional RNA recognition motif in poly(A)-specific ribonuclease with cap and poly(A) binding properties.

The Journal of biological chemistry - 9 Nov 2007

Nilsson Per, Henriksson Niklas, Niedzwiecka Anna, Balatsos Nikolaos A A, Kokkoris Kyriakos, Eriksson Jens, Virtanen Anders

Abstract excerpt

Poly(A)-specific ribonuclease (PARN) is an oligomeric, processive and cap-interacting 3' exoribonuclease that efficiently degrades mRNA poly(A) tails. Here we show that the RNA recognition motif (RRM) of PARN harbors both poly(A) and cap binding properties, suggesting that the RRM plays an important role for the two critical and unique properties that are tightly associated with PARN activity, i.e. recognition...

Read the complete abstract on PubMed

Topics

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

Share to Adenine
Share to Amino Acid Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Conserved Sequence

Share to Exoribonucleases

Share to Kinetics

Share to Poly A

Share to Protein Folding

Source

Identifiers

PMID: 17785461
DOI: 10.1074/jbc.M702375200

Genes

PARN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A multifunctional RNA recognition motif in poly(A)-specific ribonuclease with cap and poly(A) binding properties.PMID 17785461Read ↗

The RRM domain of poly(A)-specific ribonuclease has a noncanonical binding site for mRNA cap analog recognition.Semantic proximity Read ↗

Distinct roles of the R3H and RRM domains in poly(A)-specific ribonuclease structural integrity and catalysis.Semantic proximity Read ↗

Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease.Semantic proximity Read ↗

The R3H domain stabilizes poly(A)-specific ribonuclease by stabilizing the RRM domain.Semantic proximity Read ↗

Dissimilar roles of the four conserved acidic residues in the thermal stability of poly(A)-specific ribonuclease.Semantic proximity Read ↗

Functional characterization of 2',5'-linked oligoadenylate binding determinant of human RNase L.Semantic proximity Read ↗

Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damageSemantic proximity Read ↗

Coupled 5' nucleotide recognition and processivity in Xrn1-mediated mRNA decay.Semantic proximity Read ↗

Structure of mitochondrial poly(A) RNA polymerase reveals the structural basis for dimerization, ATP selectivity and the SPAX4 disease phenotype.Semantic proximity Read ↗

Poly(A)-specific ribonuclease (PARN) mediates 3'-end maturation of the telomerase RNA component.Semantic proximity Read ↗

Poly(ADP-ribose): Structure, Physicochemical Properties and Quantification In Vivo, with Special Reference to Poly(ADP-ribose) Binding Protein Modules.Semantic proximity Read ↗

Grabbing the message: structural basis of mRNA 3'UTR recognition by Hrp1.Semantic proximity Read ↗

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