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 …

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… - Cellular …, 2013 - pubmed.ncbi.nlm.nih.gov
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 …

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… - Cellular …, 2013 - europepmc.org
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 …

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… - Cellular …, 2013 - research.monash.edu
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 …

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… - Cellular …, 2013 - infona.pl
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 …