The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding-Reference-Cited by-同舟云学术

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The structure of the ARE-binding domains of Hu antigen R (HuR) undergoes conformational changes during RNA binding

Published:2013-02-16 Issue:3 Volume:69 Page:373-380
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Wang Hong,Zeng Fuxing,Liu Qiao,Liu Huihui,Liu Zexian,Niu Liwen,Teng Maikun,Li Xu

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2013/03/00/be5209/be5209.pdf

Reference28 articles.

1. AU-rich elements and associated factors: are there unifying principles?

2. The X-ray Crystal Structure of the First RNA Recognition Motif and Site-Directed Mutagenesis Suggest a Possible HuR Redox Sensing Mechanism

3. Post-transcriptional regulation of gene expression by degradation of messenger RNAs

4. HuR and mRNA stability

5. The RNA-binding protein HuD: a regulator of neuronal differentiation, maintenance and plasticity

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4. SUMOylation controls Hu antigen R posttranscriptional activity in liver cancer;Cell Reports;2024-03

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