Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM.
3' Untranslated Regions
AU Rich Elements
/ genetics
Crystallography, X-Ray
Dimerization
ELAV Proteins
/ chemistry
ELAV-Like Protein 1
/ chemistry
Humans
Magnetic Resonance Spectroscopy
RNA Recognition Motif
/ genetics
RNA-Binding Proteins
/ chemistry
Ribonucleoside Diphosphate Reductase
/ chemistry
Tumor Suppressor Proteins
/ chemistry
NMR spectroscopy
RNA-binding protein
crystal structure
dimerization
multiple register
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
19 02 2019
19 02 2019
Historique:
pubmed:
6
2
2019
medline:
3
5
2019
entrez:
6
2
2019
Statut:
ppublish
Résumé
Human antigen R (HuR) is a key regulator of cellular mRNAs containing adenylate/uridylate-rich elements (AU-rich elements; AREs). These are a major class of
Identifiants
pubmed: 30718402
pii: 1808696116
doi: 10.1073/pnas.1808696116
pmc: PMC6386705
doi:
Substances chimiques
3' Untranslated Regions
0
ELAV Proteins
0
ELAV-Like Protein 1
0
RNA-Binding Proteins
0
Tumor Suppressor Proteins
0
ribonucleotide reductase M2
EC 1.17.4.-
RRM1 protein, human
EC 1.17.4.1
Ribonucleoside Diphosphate Reductase
EC 1.17.4.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2935-2944Informations de copyright
Copyright © 2019 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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