Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor (Q28216333)

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scientific article (publication date: 4 October 2002)

Language	Label	Description	Also known as
English	Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor	scientific article (publication date: 4 October 2002)

Statements

scholarly article

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Identification of mRNA/protein (mRNP) complexes containing Puralpha, mStaufen, fragile X protein, and myosin Va and their association with rough endoplasmic reticulum equipped with a kinesin motor (English)

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endoplasmic reticulum

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author name string

Sachiyo Ohashi

1

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Katsuya Koike

2

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Akira Omori

3

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Sachiyo Ichinose

4

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Susumu Ohara

5

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Shunsuke Kobayashi

6

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Taka-Aki Sato

7

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Kaijiro Anzai

8

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language of work or name

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publication date

4 October 2002

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Journal of Biological Chemistry

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277

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40

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37804-10

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Puralpha: a multifunctional single-stranded DNA- and RNA-binding protein

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Pur alpha protein implicated in dendritic RNA transport interacts with ribosomes in neuronal cytoplasm.

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Protein synthesis at synaptic sites on dendrites

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A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum

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Human and murine FMR-1: alternative splicing and translational initiation downstream of the CGG-repeat.

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The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein

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A role for a rat homolog of staufen in the transport of RNA to neuronal dendrites

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Microtubule-dependent recruitment of Staufen-green fluorescent protein into large RNA-containing granules and subsequent dendritic transport in living hippocampal neurons

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Fragile X mental retardation protein is translated near synapses in response to neurotransmitter activation

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Microarray identification of FMRP-associated brain mRNAs and altered mRNA translational profiles in fragile X syndrome

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A conserved double-stranded RNA-binding domain

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Mammalian staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum

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Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function

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The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif

1 reference

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Monoclonal antibodies to kinesin heavy and light chains stain vesicle-like structures, but not microtubules, in cultured cells

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The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation

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She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p

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Direct interaction of microtubule- and actin-based transport motors

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Suppression of kinesin expression in cultured hippocampal neurons using antisense oligonucleotides.

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KIF5C, a novel neuronal kinesin enriched in motor neurons

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Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them

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FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association

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Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex

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Single-stranded nucleic acid-binding protein, Pur alpha, interacts with RNA homologous to 18S ribosomal RNA and inhibits translation in vitro

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Evidence that fragile X mental retardation protein is a negative regulator of translation

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The fragile X mental retardation protein inhibits translation via interacting with mRNA

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Ribosomal proteins of Escherichia coli. I. Purification of the 30 S ribosomal proteins

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Identifiers

10.1074/JBC.M203608200

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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