Kevin Drew

The paper develops a proteomics-based machine learning workflow to identify cell-type-specific protein complexes in mouse embryonic stem cells, revealing 3,986 complexes and 1,388 unique interactions specific to mESC.

The paper reconstructs the protein interactome of the Last Eukaryotic Common Ancestor and identifies new human gene-disease associations for bone density and congenital birth defects.

DirectContacts2 identifies direct protein interactions using mass spectrometry data and machine learning, improving accuracy over existing resources and providing structural models for disease-related complexes.

This study identifies RSG1/CPLANE2 as a causative gene for human ciliopathy and shows its role in ciliary transition zone assembly.

Machine learning integration of over 25,000 mass spectrometry experiments yields 15,326 human protein complexes covering 13,769 proteins, plus 511 AlphaFold-derived mutually exclusive subunit pairs.

This study defines the RBC proteome and interactome using mass spectrometry and machine learning, revealing key biological processes and structural models.

hu.MAP 2.0 integrates over 15,000 proteomic experiments to identify nearly 7,000 human protein complexes, improving accuracy and uncovering new biological insights.

This study identifies 316 proteins involved in phosphorylation-sensitive interactions using a combination of phosphatase treatment, chromatography, and mass spectrometry.

The paper introduces DIF-FRAC, a label-free method to identify RNA-associated proteins in vertebrate tissues, revealing novel RAPs and RNA-enriched organelles.

The paper maps protein complexes across 13 plant species, revealing conserved and novel assemblies with agricultural relevance.

The paper systematically identifies endogenous human ribonucleoprotein complexes using a proteomics method and provides a resource for studying RNA-associated protein complexes.

The paper identifies phase-separated organelles called Dynein Assembly Particles in ciliated cells and links their dysfunction to a human genetic disease.

The paper synthesizes over 9,000 mass spectrometry experiments to create hu.MAP, a comprehensive human protein complex map with improved accuracy and coverage of disease-associated proteins.