The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets.
RNA Biol
; 11(10): 1250-61, 2014.
Article
em En
| MEDLINE
| ID: mdl-25584704
Palavras-chave
AREs, Adenylate and uridylate Rich Elements; AU, Analytical Ultracentrifugation; CARM1, Coactivator associated Arginine Methyltransferase 1; CD, Circular Dichroism; Cdk1, Cyclin-dependent kinase 1; Chk2, Checkpoint kinase 2; ELAV1, Embryonic Lethal Abnormal Vision system human homolog 1; EMSA, Electrophoretic Mobility Shift Assay; FIR, FBP-Interacting Repressor; FL, Full-Length, HNS, HuR Nucleocytoplasmic Shuttling Sequence; HSQC, Heteronuclear Single-Quantum Correlation; HuR, Human antigen R; Human antigen R (HuR); MD, Molecular Dynamics; NMR, Nuclear Magnetic Resonance; NOE, Nuclear Overhauser Effect; Nuclear Magnetic Resonance (NMR); PCA, Principal Component Analysis; PKCα, Protein Kinase C α; PKCδ, Protein Kinase C δ; PMSF, PhenylMethylSulfonyl Fluoride; PTB, Polypyrimidine Tract Binding protein; RBPs, RNA Binding Proteins; RNA binding; RNA binding protein (RBP); RNA recognition motif (RRM); RRMs, RNA Recognition Motifs; SPR, Surface Plasmon Resonance; Serine Phosphorylation; WT, Wild-Type; dimerization; hnRNP1, heterogeneous nuclear RiboNucleoprotein C protein
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
RNA
/
Proteínas de Ligação a RNA
/
Motivos de Aminoácidos
/
Proteínas ELAV
Limite:
Humans
Idioma:
En
Revista:
RNA Biol
Ano de publicação:
2014
Tipo de documento:
Article