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2016

Journal Article

NaV1.7 as a pain target – from gene to pharmacology

Vetter, Irina, Deuis, Jennifer, Mueller, Alexander, Israel, Mathilde R., Hana Starobova, Zhang, Alan, Rash, Lachlan D. and Mobli, Mehdi (2016). NaV1.7 as a pain target – from gene to pharmacology. Pharmacology and Therapeutics, 172, 73-100. doi: 10.1016/j.pharmthera.2016.11.015

NaV1.7 as a pain target – from gene to pharmacology

2016

Journal Article

Selective inhibition of ASIC1a confers functional and morphological neuroprotection following traumatic spinal cord injury [version 1; referees: 1 approved, 1 approved with reservations]

Koehn, Liam M., Dong, Qing, Er, Sing-Yan, Rash, Lachlan D., King, Glenn F., Dziegielewska, Katarzyna M., Saunders, Norman R. and Habgood, Mark D. (2016). Selective inhibition of ASIC1a confers functional and morphological neuroprotection following traumatic spinal cord injury [version 1; referees: 1 approved, 1 approved with reservations]. F1000Research, 5 1822, 1822. doi: 10.12688/F1000RESEARCH.9094.1

Selective inhibition of ASIC1a confers functional and morphological neuroprotection following traumatic spinal cord injury [version 1; referees: 1 approved, 1 approved with reservations]

2016

Journal Article

Selective inhibition of ASIC1a confers functional and morphological neuroprotection following traumatic spinal cord injury

Koehn, Liam M, Noor, Natassya M, Dong, Qing, Er, Sing-Yan, Rash, Lachlan D, King, Glenn F, Dziegielewska, Katarzyna M, Saunders, Norman R and Habgood, Mark D (2016). Selective inhibition of ASIC1a confers functional and morphological neuroprotection following traumatic spinal cord injury. F1000Research, 5 1822, 1822. doi: 10.12688/f1000research.9094.2

Selective inhibition of ASIC1a confers functional and morphological neuroprotection following traumatic spinal cord injury

2015

Journal Article

PcTx1 affords neuroprotection in a conscious model of stroke in hypertensive rats via selective inhibition of ASIC1a

McCarthy, Claudia A., Rash, Lachlan D., Chassagnon, Irene R., King, Glenn F. and Widdop, Robert E. (2015). PcTx1 affords neuroprotection in a conscious model of stroke in hypertensive rats via selective inhibition of ASIC1a. Neuropharmacology, 99 5986, 650-657. doi: 10.1016/j.neuropharm.2015.08.040

PcTx1 affords neuroprotection in a conscious model of stroke in hypertensive rats via selective inhibition of ASIC1a

2015

Journal Article

Xenopus borealis as an alternative source of oocytes for biophysical and pharmacological studies of neuronal ion channels

Cristofori-Armstrong, Ben, Soh, Ming S., Talwar, Sahil, Brown, Darren L., Griffin, John D. O., Dekan, Zoltan, Stow, Jennifer L., King, Glenn F., Lynch, Joseph W. and Rash, Lachlan D. (2015). Xenopus borealis as an alternative source of oocytes for biophysical and pharmacological studies of neuronal ion channels. Scientific Reports, 5 (1) 14763, 14763.1-14763.12. doi: 10.1038/srep14763

Xenopus borealis as an alternative source of oocytes for biophysical and pharmacological studies of neuronal ion channels

2015

Journal Article

Molecular dynamics and functional studies define a hot spot of crystal contacts essential for PcTx1 inhibition of acid-sensing ion channel 1a

Saez, Natalie J., Deplazes, Evelyne, Cristofori-Armstrong, Ben, Chassagnon, Irene R., Lin, Xiaozhen, Mobli, Mehdi, Mark, Alan E., Rash, Lachlan D. and King, Glenn F. (2015). Molecular dynamics and functional studies define a hot spot of crystal contacts essential for PcTx1 inhibition of acid-sensing ion channel 1a. British Journal of Pharmacology, 172 (20), 4985-4995. doi: 10.1111/bph.13267

Molecular dynamics and functional studies define a hot spot of crystal contacts essential for PcTx1 inhibition of acid-sensing ion channel 1a

2015

Journal Article

Three peptide modulators of the human voltage-gated sodium channel 1.7, an important analgesic target, from venom of an Australian tarantula

Chow, Chun Yuen, Cristofori-Armstrong, Ben, Undheim, Eivind A. B., King, Glenn F. and Rash, Lachlan D. (2015). Three peptide modulators of the human voltage-gated sodium channel 1.7, an important analgesic target, from venom of an Australian tarantula. Toxins, 7 (7), 2494-2513. doi: 10.3390/toxins7072494

Three peptide modulators of the human voltage-gated sodium channel 1.7, an important analgesic target, from venom of an Australian tarantula

2015

Journal Article

Mutations in the voltage-gated potassium channel gene KCNH1 cause Temple-Baraitser syndrome and epilepsy (vol 47, pg 73, 2015)

Simons, Cas, Rash, Lachlan D., Crawford, Joanna, Ma, Linlin, Cristofori-Armstrong, Ben, Miller, David, Ru, Kelin, Baillie, Gregory J., Alanay, Yasemin, Jacquinet, Adeline, Debray, Franois-Guillaume, Verloes, Alain, Shen, Joseph, Yesil, Goezde, Guler, Serhat, Yuksel, Adnan, Cleary, John G., Grimmond, Sean M., McGaughran, Julie, King, Glenn F., Gabbett, Michael T. and Taft, Ryan J. (2015). Mutations in the voltage-gated potassium channel gene KCNH1 cause Temple-Baraitser syndrome and epilepsy (vol 47, pg 73, 2015). Nature Genetics, 47 (3), 304-304. doi: 10.1038/ng0315-304b

Mutations in the voltage-gated potassium channel gene KCNH1 cause Temple-Baraitser syndrome and epilepsy (vol 47, pg 73, 2015)

2015

Journal Article

Mutations in the voltage-gated potassium channel gene KCNH1 cause Temple-Baraitser syndrome and epilepsy

Simons Cas, Rash, Lachlan D., Crawford, Joanna, Ma, Linlin, Cristofori-Armstrong, Ben, Miller, David, Ru, Kelin, Baillie, Gregory J., Alanay, Yasemin, Jacquinet, Adeline, Debray, François-Guillaume, Verloes, Alain, Shen, Joseph, Yesil, Gözde, Guler, Serhat, Yuksel, Adnan, Cleary, John G., Grimmond, Sean M., McGaughran, Julie, King, Glenn F., Gabbett, Michael T. and Taft, Ryan J. (2015). Mutations in the voltage-gated potassium channel gene KCNH1 cause Temple-Baraitser syndrome and epilepsy. Nature Genetics, 47 (1), 73-77. doi: 10.1038/ng.3153

Mutations in the voltage-gated potassium channel gene KCNH1 cause Temple-Baraitser syndrome and epilepsy

2015

Book Chapter

Research methods

Fry, B. G., Undheim, E. A. B., Jackson, T. N. W., Georgieva, D., Vetter, I., Calvete, J. J., Schieb, H., Cribb, B. W., Yang, D. C., Daly, N. L., Manchadi, M. L. Roy, Gutierrez, J. M., Roelants, K., Lomonte, B., Nicholson, G. M., Dziemborowicz, S., Lavergne, V., Ragnarsson, L., Rash, L. D., Mobli, M., Hodgson, W. C., Casewell, N. R., Nouwens, A., Wagstaff, S. C., Ali, S. A., Whitehead, D. L., Herzig, V., Monagle, P., Kurniawan, N. D. ... Sunagar, K. (2015). Research methods. Venomous reptiles and their toxins: evolution, pathophysiology and biodiscovery. (pp. 153-214) New York, NY, United States: Oxford University Press.

Research methods

2015

Book Chapter

Therapeutic applications of spider-venom peptides

Smith, Jennifer J., Lau, Carus Ho Yee, Herzig, Volker, Ikonomopoulou, Maria P., Rash, Lachlan D. and King, Glenn F. (2015). Therapeutic applications of spider-venom peptides. Venoms to Drugs: Venom as a Source for the Development of Human Therapeutics. (pp. 221-244) edited by Glenn F. King. Cambridge, United Kingdom: Royal Society of Chemistry.. doi: 10.1039/9781849737876-00221

Therapeutic applications of spider-venom peptides

2014

Journal Article

Isolation, synthesis and characterization of omega-TRTX-Cc1a, a novel tarantula venom peptide that selectively targets L-type CaV channels

Klint, Julie K., Berecki, Géza, Durek, Thomas, Mobli, Mehdi, Knapp, Oliver, King, Glenn F., Adams, David J., Alewood, Paul F. and Rash, Lachlan D. (2014). Isolation, synthesis and characterization of omega-TRTX-Cc1a, a novel tarantula venom peptide that selectively targets L-type CaV channels. Biochemical Pharmacology, 89 (2), 276-286. doi: 10.1016/j.bcp.2014.02.008

Isolation, synthesis and characterization of omega-TRTX-Cc1a, a novel tarantula venom peptide that selectively targets L-type CaV channels

2014

Journal Article

Chemical synthesis, 3D structure and ASIC binding site of mambalgin-2

Schroeder, Christina I., Rash, Lachlan D., Vila-Farrés, Xavier, Rosengren, K. Johan, Mobli, Mehdi, King, Glenn F., Alewood, Paul F., Craik, David J. and Durek, Thomas (2014). Chemical synthesis, 3D structure and ASIC binding site of mambalgin-2. Angewandte Chemie International Edition, 53 (4), 1017-1020. doi: 10.1002/anie.201308898

Chemical synthesis, 3D structure and ASIC binding site of mambalgin-2

2014

Journal Article

Chemical synthesis, 3D structure, and ASIC binding site of the toxin mambalgin-2

Schroeder, Christina I., Rash, Lachlan D., Vila-Farrés, Xavier, Rosengren, K. Johan, Mobli, Mehdi, King, Glenn F., Alewood, Paul F., Craik, David J. and Durek, Thomas (2014). Chemical synthesis, 3D structure, and ASIC binding site of the toxin mambalgin-2. Angewandte Chemie, 126 (4), 1035-1038. doi: 10.1002/ange.201308898

Chemical synthesis, 3D structure, and ASIC binding site of the toxin mambalgin-2

2014

Journal Article

Understanding the Molecular Basis of Toxin Promiscuity: The Analgesic Sea Anemone Peptide APETx2 Interacts with Acid-Sensing Ion Channel 3 and hERG Channels via Overlapping Pharmacophores

Jensen, Jonas E., Cristofori-Armstrong, Ben, Anangi, Raveendra, Rosengren, K. Johan, Lau, Carus H. Y., Mobli, Mehdi, Brust, Andreas, Alewood, Paul F., King, Glenn F. and Rash, Lachlan D. (2014). Understanding the Molecular Basis of Toxin Promiscuity: The Analgesic Sea Anemone Peptide APETx2 Interacts with Acid-Sensing Ion Channel 3 and hERG Channels via Overlapping Pharmacophores. Journal of Medicinal Chemistry, 57 (21), 9195-9203. doi: 10.1021/jm501400p

Understanding the Molecular Basis of Toxin Promiscuity: The Analgesic Sea Anemone Peptide APETx2 Interacts with Acid-Sensing Ion Channel 3 and hERG Channels via Overlapping Pharmacophores

2013

Journal Article

ASIC3: first the heartache, now a migraine!

Rash, Lachlan D. (2013). ASIC3: first the heartache, now a migraine!. Headache, 53 (8), 1204-1206. doi: 10.1111/head.12170

ASIC3: first the heartache, now a migraine!

2013

Journal Article

Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli

Klint, Julie K., Senff, Sebastian, Saez, Natalie J., Seshadri, Radha, Lau, Ho Yee, Bende, Nira J., Undheim, Eivind A. B., Rash, Lachlan D., Mobli, Mehdi and King, Glenn F. (2013). Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli. PLoS One, 8 (5) e63865, e63865.1-e63865.12. doi: 10.1371/journal.pone.0063865

Production of recombinant disulfide-rich venom peptides for structural and functional analysis via expression in the periplasm of E. coli

2012

Journal Article

Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3

Anangi, Raveendra, Rash, Lachlan D., Mobli, Mehdi and King, Glenn F. (2012). Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3. Marine Drugs, 10 (7), 1605-1618. doi: 10.3390/md10071605

Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3

2012

Journal Article

Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3

Jensen, Jonas E., Mobli, Mehdi, Brust, Andreas, Alewood, Paul F., King, Glenn F. and Rash, Lachlan D. (2012). Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3. Marine Drugs, 10 (7), 1511-1527. doi: 10.3390/md10071511

Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3

2012

Journal Article

Inhibition of voltage-gated Na+ currents in sensory neurons by the sea anemone toxin APETx2

Blanchard, Maxime G., Rash, Lachlan D. and Kellenberger, Stephan (2012). Inhibition of voltage-gated Na+ currents in sensory neurons by the sea anemone toxin APETx2. British Journal of Pharmacology, 165 (7), 2167-2177. doi: 10.1111/j.1476-5381.2011.01674.x

Inhibition of voltage-gated Na+ currents in sensory neurons by the sea anemone toxin APETx2