Area of research
Molecular Biology · Cardiology and Cardiovascular Medicine
Research interest
Research interests include RNA and protein synthesis mechanisms, RNA Research and Splicing, RNA modifications and cancer, and DNA and Nucleic Acid Chemistry.
Faecal microbiota transplant to ERadicate gastrointestinal carriage of Antibiotic-Resistant Organisms (FERARO): A feasibility randomised controlled trial
AMPK is a mechano-metabolic sensor linking cell adhesion and mitochondrial dynamics to Myosin-dependent cell migration
The metabolic effects of intermittent versus continuous feeding in critically ill patients
Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1
LARP6C orchestrates posttranscriptional reprogramming of gene expression during hydration to promote pollen tube guidance
Mining the PDB for Tractable Cases Where X-ray Crystallography Combined with Fragment Screens Can Be Used to Systematically Design Protein–Protein Inhibitors: Two Test Cases Illustrated by IL1β-IL1R and p38α–TAB1 Complexes
<i>PDXK</i> mutations cause polyneuropathy responsive to pyridoxal 5′‐phosphate supplementation
LARP4A recognizes polyA RNA via a novel binding mechanism mediated by disordered regions and involving the PAM2w motif, revealing interplay between PABP, LARP4A and mRNA
The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins
The <scp>La</scp> and related <scp>RNA</scp>‐binding proteins (LARPs): structures, functions, and evolving perspectives
Disulfide-activated protein kinase G Iα regulates cardiac diastolic relaxation and fine-tunes the Frank–Starling response
The RNA‐binding protein LARP4 regulates cancer cell migration and invasion
Synergic interplay of the La motif, RRM1 and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module
Mechanism and consequence of the autoactivation of p38α mitogen-activated protein kinase promoted by TAB1
The association of a La module with the PABP-interacting motif PAM2 is a recurrent evolutionary process that led to the neofunctionalization of La-related proteins