Happy to share my first preprint which closes another chapter of my PhD thesis. This work demonstrates that FFPE tissues retain biologically meaningful phosphorylation signalling, creating a robust fr...

Photo-crosslinking mass spectrometry enables the identification of protein-RNA interactions in living cells, pinpointing interaction interfaces at single-amino acid resolution. However, current isolat...

Expressions of Interest for Casual Teacher in Science at Western Sydney University, The College.

This one had so many steps to get behind the paywall of that I thought I was trying to find a certain global leader's name thousands of ti...

Zero-distance photo-crosslinking reveals direct protein-DNA interactions in living cells, enabling quantitative analysis of the DNA-interacting proteome on a timescale of minutes with single-amino-aci...

Paper alert! We report the first inhibitors for nucleoside kinases NME1-4 and for the nucleotide-binding protein HINT1. On top, we provide probes for MBLAC2, an off-target of every second (!) hydroxamic acid-based HDAC inhibitor! https://t.co/uuRCO78xFz 👇🧵

Exciting leadership opportunity to join an Aust-based tech company on a global mission to revolutionise the field of chromatography & proteomics.

Interview with Dr Samantha Emery-Corbin, a research fellow at the Monash Proteomics and Metabolomics Platform in Melbourne.

Formalin-fixed paraffin-embedded (FFPE) tissues present an important resource for cancer proteomics. They are more readily available than fresh frozen (FF) tissues and can be stored at ambient tempera...

Come and celebrate our 150th year. Explore our events, our history, and the foundation we’ve built for the future.

Mass spectrometry-based single-cell proteomics (SCP) is gaining momentum but remains limited to a few laboratories due to the high costs and specialized expertise required. The ability to send samples to specialized core facilities would benefit nonspecialist laboratories and popularize SCP for biological applications. However, no methods have been tested in SCP to “freeze” the proteome state while maintaining cell integrity for transfer between laboratories or prolonged sorting using fluorescence-activated cell sorting (FACS). This study evaluates whether short-term formaldehyde (FA) fixation can maintain the cell states. We demonstrate that short-term FA fixation does not substantially affect protein recovery, even without heating and strong detergents, and maintains analytical depth compared with classical workflows. Fixation also preserves drug-induced specific perturbations of the protein abundance during cell sorting and sample preparation for SCP analysis. Our findings suggest that FA fixation can facilitate SCP by enabling sample shipping and prolonged sorting, potentially democratizing access to SCP technology and expanding its application in biological research, thereby accelerating discoveries in cell biology and personalized medicine.

imageimageFormalin fixed paraffin embedded (FFPE) patient tumor specimens are readily accessible and established gold standard for cancer diagnostics in pathology laboratories. To start building a pan...

Diagnosis of non-small cell lung cancer (NSCLC) currently relies on imaging; however, these methods are not effective for detecting early stage disease. Investigating blood-based protein biomarkers aims to simplify the diagnostic process and identify disease-associated changes before they can be seen by using imaging techniques. In this study, plasma and frozen whole blood cell pellets from NSCLC patients and healthy controls were processed using both classical and novel techniques to produce a unique set of four sample types from a single blood draw. These samples were analyzed using 12 immunoassays and liquid chromatography–mass spectrometry to collectively screen 3974 proteins. Analysis of all fractions produced a set of 522 differentially expressed proteins, with conventional blood analysis (proteomic analysis of plasma) accounting for only 7 of the total. Boosted regression tree analysis of the differentially expressed proteins produced a panel of 13 proteins that were able to discriminate between controls and NSCLC patients, with an area under the ROC curve (AUC) of 0.864 for the set. Our rapid and reproducible (<10% CV for technical replicates) blood preparation and analysis methods enabled the production of high-quality data from only 30 μL of complex samples that typically require significant fractionation prior to proteomic analysis. With our methods, almost 4000 proteins were identified from a single fraction over a 62.5 min gradient by LC-MS/MS.