This study investigates white striping (WS) in chicken breast meat using shotgun proteomics. WS is a myopathy causing significant economic losses in the poultry industry, characterized by white lines on raw meat. Researchers analyzed WS and normal chicken breast meat samples collected 6 hours postmortem, identifying 148 differentially abundant proteins (|fold change| >1.4; p-value <0.05) in WS compared to normal meat. These proteins were associated with pathways such as BAG2 signaling, glycogen degradation, and collagen metabolism. Potential upstream regulators included LIPE, UCP1, ATP5IF1, and DMD. The results suggest that WS is linked to impaired carbohydrate metabolism, protein synthesis, and calcium buffering in muscle cells. The study also identified changes in muscle fiber types, with increased abundance of myosin binding protein C1 (representing slow twitch muscle) and decreased abundance of myosin binding protein H (representing fast twitch muscle), indicating a shift in muscle fiber composition. Additionally, lower collagen type 1 isoforms and higher vimentin abundance were observed in WS meat, suggesting altered connective tissue and muscle structure. The findings provide insights into the cellular mechanisms underlying WS and its impact on meat quality. The study highlights the importance of proteomic analysis in understanding the molecular basis of chicken breast myopathies and their effects on meat quality.This study investigates white striping (WS) in chicken breast meat using shotgun proteomics. WS is a myopathy causing significant economic losses in the poultry industry, characterized by white lines on raw meat. Researchers analyzed WS and normal chicken breast meat samples collected 6 hours postmortem, identifying 148 differentially abundant proteins (|fold change| >1.4; p-value <0.05) in WS compared to normal meat. These proteins were associated with pathways such as BAG2 signaling, glycogen degradation, and collagen metabolism. Potential upstream regulators included LIPE, UCP1, ATP5IF1, and DMD. The results suggest that WS is linked to impaired carbohydrate metabolism, protein synthesis, and calcium buffering in muscle cells. The study also identified changes in muscle fiber types, with increased abundance of myosin binding protein C1 (representing slow twitch muscle) and decreased abundance of myosin binding protein H (representing fast twitch muscle), indicating a shift in muscle fiber composition. Additionally, lower collagen type 1 isoforms and higher vimentin abundance were observed in WS meat, suggesting altered connective tissue and muscle structure. The findings provide insights into the cellular mechanisms underlying WS and its impact on meat quality. The study highlights the importance of proteomic analysis in understanding the molecular basis of chicken breast myopathies and their effects on meat quality.