LeeAnn Higgins
Papers
1
Total Citations
34
H-Index
1
About
LeeAnn Higgins is a leading figure in proteomics and protein biochemistry, with a research focus that bridges molecular chaperone biology and vision science. Her most cited work, "Disruption of the Chaperonin Containing TCP-1 Function Affects Protein Networks Essential for Rod Outer Segment Morphogenesis and Survival" (2010, 34 citations), represents a landmark contribution to understanding how the Type II Chaperonin Containing TCP-1 (CCT/TRiC) governs protein homeostasis in the retina. This study demonstrated that CCT dysfunction disrupts the folding of critical cytoskeletal and signaling proteins, leading to impaired rod outer segment morphogenesis and photoreceptor cell death—a finding with direct implications for retinal degenerative diseases. Higgins’ work has been instrumental in revealing that CCT folds approximately 10% of newly translated cytosolic proteins, including key players in actin and tubulin networks. Her research has provided foundational insights into how chaperone networks maintain cellular architecture and survival, particularly in highly specialized sensory neurons. With over 30 citations on this pivotal paper alone, Higgins’ contributions continue to shape our understanding of protein folding quality control in health and disease, making her work essential reading for students and researchers in cell biology, neurobiology, and proteostasis.
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Top Papers
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