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  • E-mailAurora.Martinez@uib.no
  • Phone+47 55 58 64 27
  • Visitor Address
    Jonas Lies vei 91
    5009 Bergen
  • Postal Address
    Postboks 7804
    5020 Bergen

Aurora Martinez is the leader of the research group Biorecognition that studies the relation between biomolecular structure and function to understand and develop new therapeutic options for genetic diseases, notably neurometabolic disorders such as phenylketonuria (PKU) and defects in dopamine synthesis.

Aurora is also a partner in the KG Jebsen Centre for neuropsychiatric disorders. In addition, she is also a partner in the project 'Molecular control of Arc protein: Decoding a master regulator of synaptic plasticity and cognition', coordinated by Clive Bramham, which received support from the Toppforsk Program (NFR).

  • Show author(s) (2022). Structural mechanism for tyrosine hydroxylase inhibition by dopamine and reactivation by Ser40 phosphorylation. Nature Communications.
  • Show author(s) (2022). Screening for modulators of vesicular monoamine transporter 2 activity in transfected Hek293 cells using a fluorescent substrate.
  • Show author(s) (2022). Does alpha-Synuclein modulate Tyrosine Hydoxylase activity?
  • Show author(s) (2021). The Pah-R261Q mouse reveals oxidative stress associated with amyloid-like hepatic aggregation of mutant phenylalanine hydroxylase. Nature Communications. 15 pages.
  • Show author(s) (2021). Relevance of Electrostatics for the Interaction of Tyrosine Hydroxylase with Porous Silicon Nanoparticles. Molecular Pharmaceutics.
  • Show author(s) (2021). Personalized medicine to improve treatment of dopa-responsive dystonia—a focus on tyrosine hydroxylase deficiency. Journal of Personalized Medicine. 28 pages.
  • Show author(s) (2021). Inhibition of the Human Hsc70 System by Small Ligands as a Potential Anticancer Approach. Cancers.
  • Show author(s) (2021). HTSDSF Explorer, A Novel Tool to Analyze High-throughput DSF Screenings. Journal of Molecular Biology (JMB).
  • Show author(s) (2021). Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism. iScience.
  • Show author(s) (2021). Acute intermittent porphyria: An overview of therapy developments and future perspectives focusing on stabilisation of HMBS and proteostasis regulators. International Journal of Molecular Sciences. 25 pages.

More information in national current research information system (CRIStin)

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