The x-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible HuR redox sensing mechanism

RM Benoit, NC Meisner, J Kallen, P Graff… - Journal of molecular …, 2010 - Elsevier
Hu-antigen R (HuR) is a ubiquitous RNA-binding protein that comprises three RNA
recognition motifs (RRMs). The first two tandem RRMs are known to bind to AU-rich …

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

H Wang, F Zeng, Q Liu, H Liu, Z Liu, L Niu… - … Section D: Biological …, 2013 - scripts.iucr.org
Human RNA-binding protein (HuR), a ubiquitously expressed member of the Hu protein
family, plays an important role in mRNA degradation and has been implicated as a key post …

Highly selective actions of HuR in antagonizing AU-rich element-mediated mRNA destabilization

CYA Chen, N Xu, AB Shyu - Molecular and cellular biology, 2002 - Taylor & Francis
Human RNA-binding protein HuR, a nucleocytoplasmic shuttling protein, is a ubiquitously
expressed member of the family of Hu proteins, which consist of two N-terminal RNA …

Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM

N Ripin, J Boudet, MM Duszczyk… - Proceedings of the …, 2019 - National Acad Sciences
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 cis elements within 3 …

[HTML][HTML] Specific protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences

EJ Fialcowitz-White, BY Brewer, JD Ballin… - Journal of Biological …, 2007 - ASBMB
The RNA-binding factor HuR is a ubiquitously expressed member of the Hu protein family
that binds and stabilizes mRNAs containing AU-rich elements (AREs). Hu proteins share a …

HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs

M Pabis, GM Popowicz, R Stehle… - Nucleic acids …, 2019 - academic.oup.com
HuR/ELAVL1 is an RNA-binding protein involved in differentiation and stress response that
acts primarily by stabilizing messenger RNA (mRNA) targets. HuR comprises three RNA …

Preliminary crystallographic analysis of the RNA-binding domain of HuR and its poly (U)-binding properties

H Wang, H Li, H Shi, Y Liu, H Liu, H Zhao… - … Section F: Structural …, 2011 - scripts.iucr.org
Human antigen R (HuR), a ubiquitously expressed member of the Hu protein family, is an
important post-transcriptional regulator which has three RNA-recognition motif (RRM) …

Domain-specific phosphomimetic mutation allows dissection of different protein kinase C (PKC) isotype-triggered activities of the RNA binding protein HuR

S Schulz, A Doller, NR Pendini, JA Wilce, J Pfeilschifter… - Cellular signalling, 2013 - Elsevier
The ubiquitous mRNA binding protein human antigen R (HuR) participates in the post-
transcriptional regulation of many AU-rich element (ARE)-bearing mRNAs. Previously, by …

Regulation of HuR structure and function by dihydrotanshinone-I

P Lal, L Cerofolini, VG D'Agostino, C Zucal… - Nucleic acids …, 2017 - academic.oup.com
The Human antigen R protein (HuR) is an RNA-binding protein that recognizes U/AU-rich
elements in diverse RNAs through two RNA-recognition motifs, RRM1 and RRM2, and post …

Structural basis for recognition of AU-rich element RNA by the HuD protein

X Wang, TM Tanaka Hall - Nature structural biology, 2001 - nature.com
Hu proteins bind to adenosine-uridine (AU)-rich elements (AREs) in the 3′ untranslated
regions of many short-lived mRNAs, thereby stabilizing them. Here we report the crystal …