Rate My Professor Shane Colley

Dr. Shane Colley is a Lecturer in Molecular Pathology in the School of Medical, Molecular and Forensic Sciences at Murdoch University. He obtained his Doctorate of Philosophy from the Department of Biochemistry at The University of Western Australia. His previous research has centred on the molecular mechanics and control of cellular activities, with a particular focus on steroid action and steroid receptor repressors in relation to breast, prostate, and colorectal cancers. Earlier in his career, Dr. Colley held the position of Research Fellow at the Harry Perkins Institute of Medical Research. There, he worked on translational models of breast cancer explored in mice, including the PyMT model, and contributed to the multinational FANTOM5 collaboration, which produced significant findings on gene expression patterns across human cell types and tissues.

At Murdoch University, Dr. Colley plays a key role in education, serving as lecturer for several undergraduate units. These include Diagnostic Genomics (BMS327), which covers topics such as isolation and assessment of genomic DNA; Haematology (BMS218), emphasizing laboratory techniques, safety protocols, and aspects like haemoglobinisation; and Cell Biology (BIO152), addressing cellular structures, biochemistry, growth, and experimental practices. He has revised laboratory manuals for these courses and maintains office hours for student support. Dr. Colley supervises honours students, co-leading the MMFS Honours Project at PathWest in 2024 with Associate Professor Murray Adams. His publication record features a peer-reviewed journal article entitled 'A novel ADP-ribosylation like factor (ARL-6)'. Beyond the university, he participates in outreach, delivering informative sessions on ABO blood group typing to Year 12 students through the Perth Blood Institute's Medical Science Encounter program and contributing to MMFS Futures Days for Year 11 students. Dr. Colley has also chaired sessions at Endocrine Society Australia meetings and presented on SRA-binding proteins relevant to nuclear receptor functions.