diff --git a/content/2.general-concepts/Defense systems effectors b/content/2.general-concepts/defense-systems-effectors.md
similarity index 100%
rename from content/2.general-concepts/Defense systems effectors
rename to content/2.general-concepts/defense-systems-effectors.md
diff --git a/content/3.defense-systems/detocs.md b/content/3.defense-systems/detocs.md
index 72039702035ece976c7e9959daf598031222eb81..5a9a42d35cc06d89f0969f9ebd64bedd3fa94f1a 100644
--- a/content/3.defense-systems/detocs.md
+++ b/content/3.defense-systems/detocs.md
@@ -8,7 +8,7 @@ tableColumns:
         During viral infection, cells can deploy immune strategies that deprive viruses of molecules essential for their replication. Here, we report a family of immune effectors in bacteria that, upon phage infection, degrade cellular adenosine triphosphate (ATP) and deoxyadenosine triphosphate (dATP) by cleaving the N-glycosidic bond between the adenine and sugar moieties. These ATP nucleosidase effectors are widely distributed within multiple bacterial defense systems, including cyclic oligonucleotide-based antiviral signaling systems (CBASS), prokaryotic argonautes, and nucleotide-binding leucine-rich repeat (NLR)-like proteins, and we show that ATP and dATP degradation during infection halts phage propagation. By analyzing homologs of the immune ATP nucleosidase domain, we discover and characterize Detocs, a family of bacterial defense systems with a two-component phosphotransfer-signaling architecture. The immune ATP nucleosidase domain is also encoded within diverse eukaryotic proteins with immune-like architectures, and we show biochemically that eukaryotic homologs preserve the ATP nucleosidase activity. Our findings suggest that ATP and dATP degradation is a cell-autonomous innate immune strategy conserved across the tree of life.
     Sensor: Unknown
     Activator: Unknown
-    Effector:Nucleotide modifying
+    Effector: Nucleotide modifying
     PFAM: PF01048, PF18742
 contributors: 
     - François Rousset