diff --git a/content/3.defense-systems/lit.md b/content/3.defense-systems/lit.md
index e64c9beb952d6afb1098b56d99752a743477661b..32da3b98187307570feea1e63ea0c59ef0406fcf 100644
--- a/content/3.defense-systems/lit.md
+++ b/content/3.defense-systems/lit.md
@@ -10,9 +10,26 @@ tableColumns:
     Activator: Direct
     Effector: Other (Cleaves an elongation factor, inhibiting cellular translation
     PFAM: PF10463
+contributors: 
+  - Lucas Paoli
+relevantAbstracts:
+  - doi: 10.1128/jb.169.3.1232-1238.1987
+  - doi: 10.1128/jb.170.5.2056-2062.1988
+  - doi: 10.1073/pnas.91.2.802
+  - doi: 10.1074/jbc.M002546200
+  - doi: 10.1186/1743-422X-7-360
 ---
 
 # Lit
+
+## Description
+
+Lit was first identified in 1989 :ref{doi=10.1128/jb.169.3.1232-1238.1987}, stands for late inhibitors of T4, and was found to inhibit phage T4 in Escherichia coli (K12). The Lit gene is found in the e14 cryptic prophage :ref{doi=10.1128/jb.170.5.2056-2062.1988}. Lit is also partially active against other T-even phages :ref{doi=10.1073/pnas.91.2.802}.
+
+## Molecular mechanisms
+
+The Lit system detects cleaves EF-Tu translation factor :ref{doi=10.1073/pnas.91.2.802} at a late stage of phage maturation, when the major capsid protein binds to EF-Tu and triggers its cleavage by Lit :ref{doi=10.1074/jbc.M002546200}. As a result, the translation is inhbited, which ultimately leads to cell death. Lit is part of the abortive infection category of defense systems.
+
 ## Example of genomic structure
 
 The Lit system is composed of one protein: Lit.
@@ -68,15 +85,3 @@ end
     style Title3 fill:none,stroke:none,stroke-width:none
     style Title4 fill:none,stroke:none,stroke-width:none
 </mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
-    - doi: 10.1073/pnas.91.2.802
-    - doi: 10.1074/jbc.M002546200
-    - doi: 10.1186/1743-422X-7-360
-
----
-::
-