Magnesium‐dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction-Reference-Cited by-同舟云学术

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Magnesium‐dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction

Published:2014-07-14 Issue:16 Volume:281 Page:3685-3700
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Lozano Gloria¹,Fernandez Noemi¹,Martinez‐Salas Encarnacion¹

Affiliation:

1. Centro de Biología Molecular Severo Ochoa Consejo Superior de Investigaciones Científicas – Universidad Autónoma de Madrid Cantoblanco Spain

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12890

Reference63 articles.

1. A complex gene regulatory mechanism that operates at the nexus of multiple RNA processing decisions

2. RNA structure analysis of human spliceosomes reveals a compact 3D arrangement of snRNAs at the catalytic core

3. Structural basis for the biological relevance of the invariant apical stem in IRES-mediated translation

4. Structure of the full-length HCV IRES in solution

5. Factorless Ribosome Assembly on the Internal Ribosome Entry Site of Cricket Paralysis Virus

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1. Validating the EMCV IRES Secondary Structure with Structure–Function Analysis;Biochemistry;2023-12-11

2. Picornavirus translation strategies;FEBS Open Bio;2022-03-30

3. The DDX23 Negatively Regulates Translation and Replication of Foot-and-Mouth Disease Virus and Is Degraded by 3C Proteinase;Viruses;2020-11-25

4. RNA-protein coevolution study of Gemin5 uncovers the role of the PXSS motif of RBS1 domain for RNA binding;RNA Biology;2020-05-31

5. Rab1b and ARF5 are novel RNA-binding proteins involved in FMDV IRES–driven RNA localization;Life Science Alliance;2019-01-17

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