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Items: 1 to 20 of 215

1.

Human Pat1b connects deadenylation with mRNA decapping and controls the assembly of processing bodies.

Ozgur S, Chekulaeva M, Stoecklin G.

Mol Cell Biol. 2010 Sep;30(17):4308-23. doi: 10.1128/MCB.00429-10. Epub 2010 Jun 28.

2.

Role of Rck-Pat1b binding in assembly of processing-bodies.

Ozgur S, Stoecklin G.

RNA Biol. 2013 Apr;10(4):528-39. doi: 10.4161/rna.24086. Epub 2013 Mar 27.

3.

HPat provides a link between deadenylation and decapping in metazoa.

Haas G, Braun JE, Igreja C, Tritschler F, Nishihara T, Izaurralde E.

J Cell Biol. 2010 Apr 19;189(2):289-302. doi: 10.1083/jcb.200910141.

4.

Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping.

Fenger-Grøn M, Fillman C, Norrild B, Lykke-Andersen J.

Mol Cell. 2005 Dec 22;20(6):905-15.

5.

The human Pat1b protein: a novel mRNA deadenylation factor identified by a new immunoprecipitation technique.

Totaro A, Renzi F, La Fata G, Mattioli C, Raabe M, Urlaub H, Achsel T.

Nucleic Acids Res. 2011 Jan;39(2):635-47. doi: 10.1093/nar/gkq797. Epub 2010 Sep 17.

6.

Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates.

Scheller N, Mina LB, Galão RP, Chari A, Giménez-Barcons M, Noueiry A, Fischer U, Meyerhans A, Díez J.

Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13517-22. doi: 10.1073/pnas.0906413106. Epub 2009 Jul 23.

7.

RNA decapping inside and outside of processing bodies.

Fillman C, Lykke-Andersen J.

Curr Opin Cell Biol. 2005 Jun;17(3):326-31. Review.

PMID:
15901504
8.

Functional link between the mammalian exosome and mRNA decapping.

Wang Z, Kiledjian M.

Cell. 2001 Dec 14;107(6):751-62.

9.

The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1.

Chang CT, Bercovich N, Loh B, Jonas S, Izaurralde E.

Nucleic Acids Res. 2014 Apr;42(8):5217-33. doi: 10.1093/nar/gku129. Epub 2014 Feb 8.

10.

Lsm1-7-Pat1 complex: a link between 3' and 5'-ends in mRNA decay?

Tharun S.

RNA Biol. 2009 Jul-Aug;6(3):228-32. Epub 2009 Jul 24.

PMID:
19279404
11.

Yeast Sm-like proteins function in mRNA decapping and decay.

Tharun S, He W, Mayes AE, Lennertz P, Beggs JD, Parker R.

Nature. 2000 Mar 30;404(6777):515-8.

PMID:
10761922
12.
13.

Cytoplasmic foci are sites of mRNA decay in human cells.

Cougot N, Babajko S, Séraphin B.

J Cell Biol. 2004 Apr;165(1):31-40. Epub 2004 Apr 5.

15.

An essential component of the decapping enzyme required for normal rates of mRNA turnover.

Beelman CA, Stevens A, Caponigro G, LaGrandeur TE, Hatfield L, Fortner DM, Parker R.

Nature. 1996 Aug 15;382(6592):642-6.

PMID:
8757137
16.

Arabidopsis DCP2, DCP1, and VARICOSE form a decapping complex required for postembryonic development.

Xu J, Yang JY, Niu QW, Chua NH.

Plant Cell. 2006 Dec;18(12):3386-98. Epub 2006 Dec 8.

17.

miRISC recruits decapping factors to miRNA targets to enhance their degradation.

Nishihara T, Zekri L, Braun JE, Izaurralde E.

Nucleic Acids Res. 2013 Oct;41(18):8692-705. doi: 10.1093/nar/gkt619. Epub 2013 Jul 17.

18.
19.

Initiation-mediated mRNA decay in yeast affects heat-shock mRNAs, and works through decapping and 5'-to-3' hydrolysis.

Heikkinen HL, Llewellyn SA, Barnes CA.

Nucleic Acids Res. 2003 Jul 15;31(14):4006-16.

20.

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