Mike Lumb

Affiliations: 
NPP University College London, London, United Kingdom 
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"Mike Lumb"
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Publications

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Terunuma M, Revilla-Sanchez R, Quadros IM, et al. (2014) Postsynaptic GABAB receptor activity regulates excitatory neuronal architecture and spatial memory. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 34: 804-16
Gielen MC, Lumb MJ, Smart TG. (2012) Benzodiazepines modulate GABAA receptors by regulating the preactivation step after GABA binding. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 5707-15
Smith KR, Oliver PL, Lumb MJ, et al. (2010) Identification and characterisation of a Maf1/Macoco protein complex that interacts with GABAA receptors in neurons. Molecular and Cellular Neurosciences. 44: 330-41
Twelvetrees AE, Yuen EY, Arancibia-Carcamo IL, et al. (2010) Delivery of GABAARs to synapses is mediated by HAP1-KIF5 and disrupted by mutant huntingtin. Neuron. 65: 53-65
Arancibia-Cárcamo IL, Yuen EY, Muir J, et al. (2009) Ubiquitin-dependent lysosomal targeting of GABA(A) receptors regulates neuronal inhibition. Proceedings of the National Academy of Sciences of the United States of America. 106: 17552-7
Huber PA, Birdsey GM, Lumb MJ, et al. (2005) Peroxisomal import of human alanine:glyoxylate aminotransferase requires ancillary targeting information remote from its C terminus. The Journal of Biological Chemistry. 280: 27111-20
Cheng L, Lumb M, Polgár L, et al. (2005) How can the mood stabilizer VPA limit both mania and depression? Molecular and Cellular Neurosciences. 29: 155-61
Lumb MJ, Birdsey GM, Danpure CJ. (2003) Correction of an enzyme trafficking defect in hereditary kidney stone disease in vitro. The Biochemical Journal. 374: 79-87
Danpure CJ, Lumb MJ, Birdsey GM, et al. (2003) Alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting in human hereditary kidney stone disease. Biochimica Et Biophysica Acta. 1647: 70-5
Lumb MJ, Danpure CJ. (2000) Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. The Journal of Biological Chemistry. 275: 36415-22
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