diff --git a/content/3.defense-systems/sefir.md b/content/3.defense-systems/sefir.md
index fb73b3e68949a190225801dc2a259221cfcfc26e..dfae1a2285aa0ecb1fcfb18c8607df785c9d0c44 100644
--- a/content/3.defense-systems/sefir.md
+++ b/content/3.defense-systems/sefir.md
@@ -10,16 +10,26 @@ tableColumns:
     Activator: Unknown
     Effector: Unknown
     PFAM: PF08357, PF13676
+contributors: 
+  - Helena Shomar
+  - Marie Guillaume
+relevantAbstracts:
+  - doi: 10.1016/j.chom.2022.09.017
+  - doi: 10.1016/S0968-0004(03)00067-7
+
 ---
 
 # SEFIR
 ## Description
-The SEFIR defense system is composed of a single bacterial SEFIR (bSEFIR)-domain protein. bSEFIR-domain genes were identified in bacterial genomes, were shown to be enriched in defense islands and the activity of the defense system was first experimentally validated in *Bacillus sp.* NIO-1130 against phage phi29 [1]. 
+The SEFIR defense system is composed of a single bacterial SEFIR (bSEFIR)-domain protein. bSEFIR-domain genes were identified in bacterial genomes, were shown to be enriched in defense islands and the activity of the defense system was first experimentally validated in *Bacillus sp.* NIO-1130 against phage Phi29 :ref{doi=10.1016/j.chom.2022.09.017}. 
+
+Bacterial SEFIR domains were named after their eukaryotic homologs which were already known to be part of several eukayrotic immune proteins (e.g. SEFs and Interleukin-17 Receptors):ref{doi=10.1016/S0968-0004(03)00067-7}.
+
+Homologs of SEFIR domain proteins were also found in archaeal species : _Methanosarcina barkeri_ and _Methanosarcina mazei_ :ref{doi=10.1016/j.chom.2022.09.017}.  
 
-Bacterial SEFIR domains were named after their eukaryotic homologs which were already known to be part of several eukayrotic immune proteins (e.g. SEFs and Interleukin-17 Receptors) [2].
 
 ## Molecular mechanism
-SEFIR was shown to protect against phage infection through an abortive infection mechanism *via* NAD+ depletion. This is similar to what can be observed in other defense systems containing a TIR domain which shares homology with the SEFIR domain (in eukaryotes, both domains are part of the STIR super family) [1].
+SEFIR was shown to protect against phage infection through an abortive infection mechanism *via* NAD+ depletion. This is similar to what can be observed in other defense systems containing a TIR domain which shares homology with the SEFIR domain (in eukaryotes, both domains are part of the STIR super family) :ref{doi=10.1016/j.chom.2022.09.017}.
 
 ## Example of genomic structure
 
@@ -76,18 +86,5 @@ 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: 10.1016/j.chom.2022.09.017
-
----
-::
-
 
-## References
-[1] Millman, A. et al. An expanded arsenal of immune systems that protect bacteria from phages. Cell Host Microbe 30, 1556-1569.e5 (2022).
-[2] Novatchkova, M., Leibbrandt, A., Werzowa, J., Neubüser, A., & Eisenhaber, F. (2003). The STIR-domain superfamily in signal transduction, development and immunity. _Trends in biochemical sciences_, _28_(5), 226-229.