Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2. (Q40988437)

25 September 2017

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title

Cytoplasmic regulatory functions of the KH-domain proteins hnRNPs K and E1/E2. (English)

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25 September 2017

3

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25 September 2017

Ostareck-Lederer A

1

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PubMed ID

9852755

25 September 2017

Ostareck DH

series ordinal

2

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PubMed ID

9852755

25 September 2017

language of work or name

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1 November 1998

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25 September 2017

3

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Trends in Biochemical Sciences

inferred from page(s)

published in

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25 September 2017

23

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25 September 2017

409-411

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25 September 2017

11

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hnRNP proteins and the biogenesis of mRNA

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1 reference

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Nucleocytoplasmic transport: the soluble phase

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mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3' end.

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The pre-mRNA binding K protein contains a novel evolutionarily conserved motif

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The KH domain occurs in a diverse set of RNA-binding proteins that include the antiterminator NusA and is probably involved in binding to nucleic acid.

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Characterisation of the nucleic-acid-binding activity of KH domains. Different properties of different domains.

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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome

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Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding protein and is specifically expressed in the developing motor system

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Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome

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The K protein domain that recruits the interleukin 1-responsive K protein kinase lies adjacent to a cluster of c-Src and Vav SH3-binding sites. Implications that K protein acts as a docking platform

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Heterogeneous nuclear ribonucleoprotein K is a transcription factor

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A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway

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The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein

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Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains

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Erythroid cell-specific determinants of alpha-globin mRNA stability

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Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the alpha-globin mRNA stability complex

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Four highly stable eukaryotic mRNAs assemble 3' untranslated region RNA-protein complexes sharing cis and trans components.

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Poly(rC) binding protein 2 binds to stem-loop IV of the poliovirus RNA 5' noncoding region: identification by automated liquid chromatography-tandem mass spectrometry

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Identifiers

DOI

1 reference

25 September 2017

1 reference

PubMed ID

9852755