Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3.

By O. Sørensen, P. Follin, A. Johnsen, J. Calafat, G. Tjabringa, P. Hiemstra, N. Borregaard. Blood, 2001

943 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Microbiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/9c750563d9ca90ece363a9caafce47cefb51777e

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. Robert E. W. Hancock

In Microbiology

1. Robert E. W. Hancock
2. M. Malmsten
3. A. Schmidtchen
4. Mukesh Pasupuleti
5. D. Davidson

In Molecular Biology

1. M. Malmsten
2. A. Schmidtchen
3. Mukesh Pasupuleti
4. Robert E. W. Hancock
5. N. Borregaard

Citations in the corpus

• The Human Antimicrobial Peptide LL-37 Is a Multifunctional Modulator of Innate Immune Responses1 (2002, background): “hCAP-18 was found to be cleaved extracellularly by proteinase 3 to generate the peptide LL-37 ( 25 ).”
• Antimicrobial peptides: key components of the innate immune system (2012, background): “In humans, the hCAP18 propeptide is processed by a serine proteinase 3 or aspartic protease gastricin in neutrophils to release the active fragment LL-37 or ALL-38 respectively (Sörensen et al., 2001; Sorensen et al., 2003; de Haar et al., 2006).”
• Neutrophils, from marrow to microbes. (2010, background): “Neutrophils that have migrated into tissues are more active as phagocytic cells than blood neutrophils (Sørensen et al., 2001) and activate a transcriptional program that results in generation of several chemokines, including IL-8 and Groa (Theilgaard- Mö nch et al., 2004; Scapini et al., 2000,…”