Cardiolipin Modulates the Activity of the Intramembrane Protease GlpG Inducing Membrane Restructuring
Barbara Maier, Oskar Engberg, Viola Döbel, Jenny Leopold, Holger A. Scheidt, Rosalie A. M. van Beekveld, Markus Weingarth, Albert A. Smith, Daniel Huster · 2026
Read Cardiolipin Modulates the Activity of the Intramembrane Protease GlpG Inducing Membrane Restructuring by Barbara Maier, Oskar Engberg, Viola Döbel, Jenny Leopold, Holger A. Scheidt, Rosalie A. M. van Beekveld, Markus Weingarth, Albert A. Smith, Daniel Huster (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13564412.txt.
Description
Barbara Maier and co-authors show how one fat reshapes a membrane protease in a 2026 paper. Cardiolipin is a four tailed fat found in bacteria and mitochondria. The protease GlpG cuts proteins inside the membrane of Escherichia coli.
With cardiolipin in the mix, GlpG cut its targets about forty percent faster. Neighbor fats shed their thinning once cardiolipin took the ring seat. The guest fat itself thinned to match the protease girth. A wide NMR sweep charted the fat's shape and motion. Chain disorder and film thinning came with the protease near. One fat can thus retune a membrane enzyme's pace.
Catalog record
| CREATOR | Barbara Maier, Oskar Engberg, Viola Döbel, Jenny Leopold, Holger A. Scheidt, Rosalie A. M. van Beekveld, Markus Weingarth, Albert A. Smith, Daniel Huster |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 59 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |