diff --git a/content/3.defense-systems/psyrta.md b/content/3.defense-systems/psyrta.md
index 8c6cd412c758ab6e171948e15d101dedd91a95b9..b8fc01fa3574dd889d887394a782c166f42f3315 100644
--- a/content/3.defense-systems/psyrta.md
+++ b/content/3.defense-systems/psyrta.md
@@ -26,18 +26,23 @@ Originally found in a high throughput shotgun cloning of bacterial fragments in
 
 ## Molecular mechanisms
 
-from :ref{doi=10.1016/j.molcel.2013.02.002} "The psyrT shares homology with domains of the RecQ helicase,
-a family of proteins implicated in DNA repair (Bernstein et al.,
-2010); and the antitoxin of the same system, psyrA, has a nucle-
-otide binding domain (COG0758) that was previously described
-in proteins involved in DNA uptake"
-
-from :ref{10.1016/j.chom.2022.09.017} "Both systems encode an antitoxin
-with homology to DprA, a single-stranded DNA (ssDNA)-binding
-protein known to be involved in DNA transformation (Mortier-
-Barrie` re et al., 2007). The toxin contains a phosphoribosyl trans-
-ferase (PRTase) domain, which was previously found in effectors
-of retron abortive infection systems "
+from :ref{doi=10.1016/j.molcel.2013.02.002} :
+
+> The psyrT shares homology with domains of the RecQ helicase,
+> a family of proteins implicated in DNA repair (Bernstein et al.,
+> 2010); and the antitoxin of the same system, psyrA, has a nucle-
+> otide binding domain (COG0758) that was previously described
+> in proteins involved in DNA uptake
+
+
+from :ref{10.1016/j.chom.2022.09.017} :
+
+> Both systems encode an antitoxin
+> with homology to DprA, a single-stranded DNA (ssDNA)-binding
+> protein known to be involved in DNA transformation (Mortier-
+> Barrière et al., 2007). The toxin contains a phosphoribosyl trans-
+> ferase (PRTase) domain, which was previously found in effectors
+> of retron abortive infection systems "
 
 
 ## Example of genomic structure