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Results: 1 to 20 of 94

1.

Smaug destroys a huge treasure.

Götze M, Wahle E.

Genome Biol. 2014 Jan 27;15(1):101. doi: 10.1186/gb4156.

PMID:
24468051
[PubMed - in process]
2.

Global regulation of mRNA translation and stability in the early Drosophila embryo by the Smaug RNA-binding protein.

Chen L, Dumelie JG, Li X, Cheng MH, Yang Z, Laver JD, Siddiqui NU, Westwood JT, Morris Q, Lipshitz HD, Smibert CA.

Genome Biol. 2014 Jan 7;15(1):R4. doi: 10.1186/gb-2014-15-1-r4.

PMID:
24393533
[PubMed - in process]
Free PMC Article
3.

Smaug recruits the CCR4/POP2/NOT deadenylase complex to trigger maternal transcript localization in the early Drosophila embryo.

Semotok JL, Cooperstock RL, Pinder BD, Vari HK, Lipshitz HD, Smibert CA.

Curr Biol. 2005 Feb 22;15(4):284-94.

PMID:
15723788
[PubMed - indexed for MEDLINE]
Free Article
4.

Maternal mRNA deadenylation and decay by the piRNA pathway in the early Drosophila embryo.

Rouget C, Papin C, Boureux A, Meunier AC, Franco B, Robine N, Lai EC, Pelisson A, Simonelig M.

Nature. 2010 Oct 28;467(7319):1128-32. doi: 10.1038/nature09465. Epub 2010 Oct 17.

PMID:
20953170
[PubMed - indexed for MEDLINE]
5.

microRNA-independent recruitment of Argonaute 1 to nanos mRNA through the Smaug RNA-binding protein.

Pinder BD, Smibert CA.

EMBO Rep. 2013 Jan;14(1):80-6. doi: 10.1038/embor.2012.192. Epub 2012 Nov 27.

PMID:
23184089
[PubMed - indexed for MEDLINE]
Free PMC Article
6.

Smaug: an unexpected journey into the mechanisms of post-transcriptional regulation.

Pinder BD, Smibert CA.

Fly (Austin). 2013 Jul-Sep;7(3):142-5. doi: 10.4161/fly.24336. Epub 2013 Mar 21.

PMID:
23519205
[PubMed - indexed for MEDLINE]
Free PMC Article
7.

Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro.

Smibert CA, Lie YS, Shillinglaw W, Henzel WJ, Macdonald PM.

RNA. 1999 Dec;5(12):1535-47.

PMID:
10606265
[PubMed - indexed for MEDLINE]
Free PMC Article
8.

Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression.

Nelson MR, Leidal AM, Smibert CA.

EMBO J. 2004 Jan 14;23(1):150-9. Epub 2003 Dec 11.

PMID:
14685270
[PubMed - indexed for MEDLINE]
Free PMC Article
9.

smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo.

Smibert CA, Wilson JE, Kerr K, Macdonald PM.

Genes Dev. 1996 Oct 15;10(20):2600-9.

PMID:
8895661
[PubMed - indexed for MEDLINE]
Free Article
10.

Rapid ATP-dependent deadenylation of nanos mRNA in a cell-free system from Drosophila embryos.

Jeske M, Meyer S, Temme C, Freudenreich D, Wahle E.

J Biol Chem. 2006 Sep 1;281(35):25124-33. Epub 2006 Jun 22.

PMID:
16793774
[PubMed - indexed for MEDLINE]
Free Article
11.

An essential role for the RNA-binding protein Smaug during the Drosophila maternal-to-zygotic transition.

Benoit B, He CH, Zhang F, Votruba SM, Tadros W, Westwood JT, Smibert CA, Lipshitz HD, Theurkauf WE.

Development. 2009 Mar;136(6):923-32. doi: 10.1242/dev.031815.

PMID:
19234062
[PubMed - indexed for MEDLINE]
Free PMC Article
12.

Oskar allows nanos mRNA translation in Drosophila embryos by preventing its deadenylation by Smaug/CCR4.

Zaessinger S, Busseau I, Simonelig M.

Development. 2006 Nov;133(22):4573-83. Epub 2006 Oct 18.

PMID:
17050620
[PubMed - indexed for MEDLINE]
Free Article
13.

Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels.

Jeske M, Moritz B, Anders A, Wahle E.

EMBO J. 2011 Jan 5;30(1):90-103. doi: 10.1038/emboj.2010.283. Epub 2010 Nov 16.

PMID:
21081899
[PubMed - indexed for MEDLINE]
Free PMC Article
14.

Drosophila maternal Hsp83 mRNA destabilization is directed by multiple SMAUG recognition elements in the open reading frame.

Semotok JL, Luo H, Cooperstock RL, Karaiskakis A, Vari HK, Smibert CA, Lipshitz HD.

Mol Cell Biol. 2008 Nov;28(22):6757-72. doi: 10.1128/MCB.00037-08. Epub 2008 Sep 15. Erratum in: Mol Cell Biol. 2008 Dec;28(24):7533.

PMID:
18794360
[PubMed - indexed for MEDLINE]
Free PMC Article
15.

Temporal reciprocity of miRNAs and their targets during the maternal-to-zygotic transition in Drosophila.

Bushati N, Stark A, Brennecke J, Cohen SM.

Curr Biol. 2008 Apr 8;18(7):501-6. doi: 10.1016/j.cub.2008.02.081.

PMID:
18394895
[PubMed - indexed for MEDLINE]
Free Article
16.

Mammalian Smaug is a translational repressor that forms cytoplasmic foci similar to stress granules.

Baez MV, Boccaccio GL.

J Biol Chem. 2005 Dec 30;280(52):43131-40. Epub 2005 Oct 12.

PMID:
16221671
[PubMed - indexed for MEDLINE]
Free Article
17.

SMAUG is a major regulator of maternal mRNA destabilization in Drosophila and its translation is activated by the PAN GU kinase.

Tadros W, Goldman AL, Babak T, Menzies F, Vardy L, Orr-Weaver T, Hughes TR, Westwood JT, Smibert CA, Lipshitz HD.

Dev Cell. 2007 Jan;12(1):143-55.

PMID:
17199047
[PubMed - indexed for MEDLINE]
Free Article
18.

The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators.

Aviv T, Lin Z, Lau S, Rendl LM, Sicheri F, Smibert CA.

Nat Struct Biol. 2003 Aug;10(8):614-21.

PMID:
12858164
[PubMed - indexed for MEDLINE]
19.

Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila.

Dahanukar A, Walker JA, Wharton RP.

Mol Cell. 1999 Aug;4(2):209-18.

PMID:
10488336
[PubMed - indexed for MEDLINE]
Free Article
20.

Wispy, the Drosophila homolog of GLD-2, is required during oogenesis and egg activation.

Cui J, Sackton KL, Horner VL, Kumar KE, Wolfner MF.

Genetics. 2008 Apr;178(4):2017-29. doi: 10.1534/genetics.107.084558.

PMID:
18430932
[PubMed - indexed for MEDLINE]
Free PMC Article

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