Dr Angelo Keramidas
Dr

Angelo Keramidas

Email: 
Phone: 
+61 7 334 66362

Background

I am interested in ion channels in health and disease. Improved technologies for genetic screening is revealing an expanding catalogue of genetic variants to ion channels that give rise neurological disorders, such as epilespy syndromes, autism spectrum disorder and other neurodevelopmental disorders. My main research focus is on neurotransmitter-activated receptor ion channels that are found at neuronal synapses. These include GABA-A, glycine and glutamate (NMDA) receptors. I also work on other ion channesl such as voltage-gated sodium channels and synaptic receptors expressed in invertebrate nervous systems.

I am an expert at recording single ion channel, synaptic and conventional whole-cell currents for functional and pharmacological analyisis.

I collaborate with biophysicists, molecular biologists, geneticists, electrophysiologists and clinicians that specialise in genetic neurological disorders. I have active projects in collaboration with research groups in Australia, USA and Europe.

Availability

Dr Angelo Keramidas is:
Available for supervision

Fields of research

Neurosciences Zoology

Qualifications

  • Bachelor of Science, unknown
  • Doctor of Philosophy, unknown

Research impacts

I am collaborating with basic and clinical research groups that bring together a great diversity of research techniques with the common aim of developing personalised medicine for affected individuals with neurological disorders.

Search Professor Angelo Keramidas’s works on UQ eSpace

49 works between 1999 and 2024
All (49) Journal Article (46) Conference Publication (3)

41 - 49 of 49 works

2004

Journal Article

Ligand-gated ion channels: Mechanisms underlying ion selectivity

Keramidas, Angelo, Moorhouse, Andrew J., Schofield, Peter R. and Barry, Peter H. (2004). Ligand-gated ion channels: Mechanisms underlying ion selectivity. Progress in Biophysics and Molecular Biology, 86 (2), 161-204. doi: 10.1016/j.pbiomolbio.2003.09.002

Ligand-gated ion channels: Mechanisms underlying ion selectivity

2003

Journal Article

The contribution of proline 250 (P-2’) to pore diameter and ion selectivity in the human glycine receptor channel

Lee, David J.-S., Keramidas, Angelo, Moorhouse, Andrew J., Schofield, Peter R. and Barry, Peter H. (2003). The contribution of proline 250 (P-2’) to pore diameter and ion selectivity in the human glycine receptor channel. Neuroscience Letters, 351 (3), 196-200. doi: 10.1016/S0304-3940(03)00977-7

The contribution of proline 250 (P-2’) to pore diameter and ion selectivity in the human glycine receptor channel

2003

Journal Article

The contribution of proline 250 (P-2 ') to pore diameter and ion selectivity in the human glycine receptor channel

Lee, DJS, Keramidas, A, Moorhouse, AJ, Schofield, PR and Barry, PH (2003). The contribution of proline 250 (P-2 ') to pore diameter and ion selectivity in the human glycine receptor channel. Neuroscience Letters, 351 (3), 196-200. doi: 10.1016/S0304-3940(03)00977-7

The contribution of proline 250 (P-2 ') to pore diameter and ion selectivity in the human glycine receptor channel

2003

Conference Publication

Mechanism of ion permeation in the glycine receptor and its cation-selective mutations

O'Mara, Megan, Keramidas, Angelo, Barry, Peter H. and Chung, Shin-Ho (2003). Mechanism of ion permeation in the glycine receptor and its cation-selective mutations. 47th Annual Meeting of the Biophysical Society, San Antonio, Texas, 1-5 March 2003. Bethesda, MD, U.S.A.: Cell Press for the Biophysical Society.

Mechanism of ion permeation in the glycine receptor and its cation-selective mutations

2003

Conference Publication

Mechanism of ion permeation in the glycine receptor and its cation-selective mutations

O'Mara, M., Keramidas, A., Barry, P. H. and Chung, S. H. (2003). Mechanism of ion permeation in the glycine receptor and its cation-selective mutations. 47th Annual Meeting of the Biophysical-Society, San Antonio Texas, 1-5 March 2003. Bethesda, MD United States: Biophysical Society.

Mechanism of ion permeation in the glycine receptor and its cation-selective mutations

2002

Journal Article

Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels

Moorhouse, Andrew J., Keramidas, Angelo, Zaykin, Andrey, Schofield, Peter R. and Barry, Peter H. (2002). Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels. Journal of General Physiology, 119 (5), 411-425. doi: 10.1085/jgp.20028553

Single channel analysis of conductance and rectification in cation-selective, mutant glycine receptor channels

2002

Journal Article

Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity

Keramidas, Angelo, Moorhouse, Andrew J., Pierce, Kerrie D. and Schofield, Peter R. (2002). Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity. Journal of General Physiology, 119 (5), 393-410. doi: 10.1085/jgp.20028552

Cation-selective mutations in the M2 domain of the inhibitory glycine receptor channel reveal determinants of ion-charge selectivity

2000

Journal Article

M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective

Keramidas, A, Moorhouse, AJ, French, CR, Schofield, PR and Barry, PH (2000). M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective. Biophysical Journal, 79 (1), 247-259. doi: 10.1016/S0006-3495(00)76287-4

M2 pore mutations convert the glycine receptor channel from being anion- to cation-selective

1999

Journal Article

Measurement of the limiting equivalent conductivities and mobilities of the most prevalent ionic species of EGTA (EGTA2- and EGTA3-) for use in electrophysiological experiments

Keramidas, Angelo , Barry, Peter H., Moorhouse, Andrew and Kuhlmann, Levin (1999). Measurement of the limiting equivalent conductivities and mobilities of the most prevalent ionic species of EGTA (EGTA2- and EGTA3-) for use in electrophysiological experiments. Journal of Neuroscience Methods, 89 (1), 41-47. doi: 10.1016/S0165-0270(99)00036-9

Measurement of the limiting equivalent conductivities and mobilities of the most prevalent ionic species of EGTA (EGTA2- and EGTA3-) for use in electrophysiological experiments

Current funding

  • 2023 - 2026
    Tuning the activating stimulus of voltage-gated sodium channels
    ARC Discovery Projects
    Open grant

Past funding

  • 2023 - 2024
    GluCI Project
    Vestaron Corporation
    Open grant
  • 2019 - 2022
    Regulation of glutamate receptor dynamics in mammalian central neurons
    ARC Discovery Projects
    Open grant
  • 2019 - 2022
    Investigating NMDA receptor-mediated pathological mechanisms underlying epilepsy and associated neurological disorders (NHMRC Project Grant led by University of the Sunshine Coast)
    University of the Sunshine Coast
    Open grant
  • 2015 - 2017
    Using artificial synapses to investigate the functional pathology underlying epilepsy
    NHMRC Project Grant
    Open grant
  • 2012 - 2014
    Understanding the mechanisms of GABA type-A receptor activation and drug modulation
    ARC Discovery Projects
    Open grant

Availability

Dr Angelo Keramidas is:
Available for supervision

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Available projects

  • GABA-A and glycine receptor variants in epilepsy and autism

    New gene variants identified by our clinical collaborators to receptors that mediate neuronal inhibition. These variants lead to receptor functional deficits that manifest as neurological syndromes in young affected individuals.

    We aim to characterise the functional deficists in these receptors and explore personalised treatment options that are tailored to each receptor variant.

  • Glutamate (NMDA) receptors in develpmental delay

    Genetic variants to glutamate receptors have been discovered by our clinical geneticists. We aim the understand how these variants lead to developmental delay and co-morbid disorders in affected individuals and explore pharmacotherapies that correct the functional deficits in these important receptors.

  • Tuning the activating stimulus of voltage-gated sodium channels

    This project will use natural and modified peptides that are derived from venoms of different species, such as spiders and ants to probe and manipulate the functional properties of voltage-gated ion channels, which are critically important to the function of the nervous system.

    You will learn patch-clamp electrophysiology (whole-cell and single channels) and how to isolate, synthesise and determine the structure of venom peptides and their mechanisms of action at ion channels.

Supervision history

Current supervision

Completed supervision

Enquiries

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