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The protein encoded by PARN is a 3'-exoribonuclease, with similarity to the RNase D family of 3'-exonucleases. Zusätzlich bieten wir Ihnen PARN Antikörper (66) und PARN Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
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we found a polyadenylation-dependent 3' end maturation pathway for the human telomerase RNA that relies on the nuclear poly(A)-binding protein PABPN1 (zeige PABPN1 Proteine) and the poly(A)-specific RNase PARN.
PARN increased telomerase RNA component levels by deadenylating telomerase RNA component, thereby limiting its degradation by EXOSC10 (zeige EXOSC10 Proteine).
Large monoallelic mutations of PARN can cause developmental/mental illness. Biallelic PARN mutations cause severe bone marrow failure and central hypomyelination.
results highlight the clinical significance of PARN and NOC (zeige CCRN4L Proteine) on the survival in SCC (zeige CYP11A1 Proteine) diagnosed patients.
Mutations in the PARN gene cause dyskeratosis congenital.
The results indicate that the cellular level of miR (zeige MLXIP Proteine)-122 is determined by the balance between the opposing effects of GLD-2 (zeige PAPD4 Proteine) and PARN/CUGBP1 (zeige CELF1 Proteine) on the metabolism of its 3'-terminus.
3 families with dyskeratosis congenita had key domain mutations in PARN shortening telomeres, reducing deadenylation, and downregulating TERC, DKC1 (zeige DKC1 Proteine), RTEL1, and TERF1 (zeige TERF1 Proteine).
PARN and RTEL1 mutation carriers had shortened leukocyte telomere lengths.
poly(A)-specific ribonuclease (PARN) was upregulated in gastric tumor tissues and gastric cancer cell lines MKN28 and AGS (zeige JAG1 Proteine).
poly(A) polymerase (zeige PAPOLA Proteine) Gld2 (zeige PAPD4 Proteine), deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd (zeige NGDN Proteine)) are components of a dendritic CPEB (zeige CPEB1 Proteine)-associated polyadenylation apparatus
these data indicate that PARN modulates decay of a defined set of mRNAs in mammalian cells and implicate this deadenylase in coordinating control of genes required for cell movement.
Solution structures of the cap-binding domain of mouse PARN with and without the m(7)GpppG cap analog reveal a novel cap-binding mode.
A modeled PARN, which shows that the RRM domain from one subunit and the R3H domain from the other subunit enclose the active site.
The protein encoded by this gene is a 3'-exoribonuclease, with similarity to the RNase D family of 3'-exonucleases. It prefers poly(A) as the substrate, hence, efficiently degrades poly(A) tails of mRNAs. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. This protein is also involved in silencing of certain maternal mRNAs during oocyte maturation and early embryonic development, as well as in nonsense-mediated decay (NMD) of mRNAs that contain premature stop codons. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, deadenylation nuclease
, poly(A)-specific ribonuclease (deadenylation nuclease)
, poly(A)-specific ribonuclease PARN
, polyadenylate-specific ribonuclease