Cathepsin L was identified as uniquely essential for processing neuropeptide precursors in secretory vesicles, revealing how the body manufactures its own bioactive peptides from larger precursor proteins.
Key findingCathepsin L was identified as uniquely essential for processing neuropeptide precursors in secretory vesicles, revealing how the body manufactures its
What the researchers found
Cathepsin L was identified as uniquely essential for processing neuropeptide precursors in secretory vesicles, revealing how the body manufactures its own bioactive peptides from larger precursor proteins.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2010.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides.
Neuropeptides, 44(6), 457-66
Citation
Funkelstein, Lydiane; Beinfeld, Margery; Minokadeh, Ardalan; Zadina, James; Hook, Vivian. (2010). Unique biological function of cathepsin L in secretory vesicles for biosynthesis of neuropeptides.. Neuropeptides, 44(6), 457-66. https://doi.org/10.1016/j.npep.2010.08.003