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Andrew studied Biochemistry obtaining a BSc (hons) and PhD from the Universities of Bristol and Birmingham, respectively. He was awarded an IRTA fellowship and joined Dr. Stephen Shears at NIEHS (a division of NIH) in Research Triangle Park, NC, USA where he utilised his prior experience in protein purification combined with newly acquired expertise in molecular biology to isolate, clone and characterise novel inositol polyphosphate phosphatases/kinases. He subsequently became a Research Assistant Professor in the Laboratory of Professor Edward Clark at the University of Washington, Seattle, USA, where he initiated his interest in molecular mechanisms of programmed cell death, with a focus on the regulation of B cell fate by pro-survival TNF superfamily members (CD40L, BAFF, APRIL) and BCL2 family proteins including Bim and Bfl-1/A1. He subsequently returned to the UK where he joined Professor Gerry Cohen’s lab at the MRC Toxicology Unit, studying both intrinsic (NOXA) and extrinsic apoptotic pathways (TRAIL signalling). Following Professor Cohen’s retirement, he joined Dr. Michal Malewicz’s group where he identified and further characterised a novel accessory NHEJ DNA repair factor, PAXX. He subsequently joined Marion Macfarlane’s group, where he continues to investigate molecular mechanisms of cell death with a primary focus on regulation of FADD-containing multiprotein complexes including the Death-inducing Signalling Complex (DISC) and TNF Receptor Complex II involved in apoptotic and necroptotic cell death pathways, which are triggered in response to toxic insult/injury.



Key publications: 

Craxton, A., Munnur, D., Jukes-Jones, R., Skalka, G., Langlais, C., Cain, K and Malewicz, M. PAXX is essential for directing the activity of DNA Polymerase in DNA repair. (2018) Nature Communications 9:3877.

Craxton, A., Somers, J., Munnur, D., Jukes-Jones, Cain, K and Malewicz, M. XLS (c9orf142/PAXX) is a new component of mammalian DNA double strand break repair. (2015) Cell. Death & Differentiation 22: 890.

Craxton, A., Butterworth, M., Harper, N., Ciechanover, A. and Cohen, G.M. NOXA, a sensor of proteasome integrity, is degraded by 26S proteasomes by an ubiquitin-independent pathway that is blocked by MCL-1. (2012) Cell. Death & Differentiation 19: 1424.

Senior Investigator Scientist

Contact Details

MRC Toxicology Unit
Gleeson Building
Tennis Court Road


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