Despite both aggregation and Hsp40 affinity increasing across a majority of the observed proteome after cellular propachlor exposure, there is no meaningful correlation between these two factors. This is consistent with a previous study that found that stress-dependent protein aggregation does not correlate with stability across diverse stresses . Generally, different measures of protein stabilization are poorly correlated with each other, as protein misfolding involves multiple processes that will be probed differently by different assays . The vesicular trafficking proteins SMAP2, GAK, CLTA, CLTB, CLTC, CLTC1, AP1B1, AP1M1, EPS15, and CLINT1 all substantially lose solubility in response to propachlor treatment, but this network only modestly increases its DNAJB8 affinity. These proteins rely on Hsp70 for clathrin disaggregation, but GAK serves as a dedicated Hsp40 co-chaperone outside of neuronal cells . These proteins may not be well-surveyed by a promiscuous Hsp40 such as DNAJB8, even under conditions that lead to their destabilization. Alternatively, they may have lower thresholds for aggregation as compared to proteins that show greater differential DNAJB8 affinity following propachlor treatment . GAPDH is highly abundant in the human proteome with many functions beyond its canonical role in glycolysis . These functions are readily perturbed by a diverse range of post-translational modifications which can lead to toxic aggregation , making its destabilization following propachlor exposure particularly hazardous for cellular proteostasis. Hence, we looked for the presence of GAPDH-propachlor adducts.