Mammalian Smaug is a translational repressor that forms cytoplasmic foci similar to stress granules (Q24338191)

positive regulation of translation

GOA release 2020-03-11

1 reference

Sterile alpha motif domain containing 4

GOA release 2020-03-11

1 reference

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

María V Baez

series ordinal

1

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Graciela L Boccaccio

series ordinal

2

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language of work or name

English

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publication date

30 December 2005

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published in

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volume

280

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page(s)

43131-40

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issue

52

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

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

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Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes

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Molecular mechanisms of translational control

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

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Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes

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Cytoplasmic foci are sites of mRNA decay in human cells

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The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies

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The RasGAP-associated endoribonuclease G3BP assembles stress granules

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Stress granules and processing bodies are dynamically linked sites of mRNP remodeling

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inferred from DOI database lookup

7 January 2021

based on heuristic

Ligand-dependent recruitment of the ErbB4 signaling complex into neuronal lipid rafts

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.M508374200

1 reference

Consolidated OpenCitations Corpus – April 2017

4732742

4732742

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference