Cordelia Schiene‐Fischer
Papers
1
Total Citations
39
H-Index
1
About
Cordelia Schiene‐Fischer is a leading biochemist whose research centers on peptidylprolyl cis-trans isomerases (PPIases), particularly cyclophilins, and their roles in protein folding, cellular signaling, and disease. Her most cited work, "Secreted Cyclophilin A Mediates Matrix Assembly of Hensin" (2008, 39 citations), reveals a groundbreaking mechanism: extracellular cyclophilin A acts as a chaperone to assemble the multidomain protein hensin (DMBT1 ortholog) into the extracellular matrix, driving terminal epithelial differentiation. This discovery bridges protein isomerase activity with tissue morphogenesis and innate immunity, highlighting cyclophilin A’s dual intracellular and extracellular functions. Schiene‐Fischer’s contributions have illuminated how PPIases regulate protein conformation beyond the ribosome, impacting fields from cancer biology to fibrosis. Her work is distinguished by its focus on secreted cyclophilins as mediators of matrix assembly and differentiation, earning recognition for its translational potential. With a citation record that underscores her influence, she continues to unravel the molecular logic of isomerases in health and disease, offering students a compelling model of how fundamental protein chemistry drives complex physiological outcomes.
Research Focus
Key Achievements
Top Papers
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