The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity

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The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity

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scientific article published on 18 October 2018

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wetenschappelijk artikel

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наукова стаття, опублікована в жовтні 2018

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The crystal structure of Stauf ...... light on substrate selectivity

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The crystal structure of Stauf ...... light on substrate selectivity

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The crystal structure of Stauf ...... light on substrate selectivity

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The crystal structure of Stauf ...... light on substrate selectivity

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The crystal structure of Stauf ...... light on substrate selectivity

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The crystal structure of Stauf ...... light on substrate selectivity

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P1476

The crystal structure of Stauf ...... light on substrate selectivity

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P2093

Christiane Emmerich

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Claire Basquin

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Kristina Schaaf

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Lina Bandholz-Cajamarca

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

Mammalian Staufen1 recruits Upf1 to specific mRNA 3'UTRs so as to elicit mRNA decay

The double-stranded RNA-binding protein Staufen is incorporated in human immunodeficiency virus type 1: evidence for a role in genomic RNA encapsidation

Molecular mapping of the determinants involved in human Staufen-ribosome association

Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro

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

A conserved double-stranded RNA-binding domain

Identification of Staufen in the human immunodeficiency virus type 1 Gag ribonucleoprotein complex and a role in generating infectious viral particles

A genome-wide approach identifies distinct but overlapping subsets of cellular mRNAs associated with Staufen1- and Staufen2-containing ribonucleoprotein complexes

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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e201800187

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scholarly article

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10.26508/LSA.201800187

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English

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Uwe Irion

Daniela Lazzaretti

Fulvia Bono

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2018-10-18T00:00:00Z

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30456389

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6238398

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