diff --git a/content/3.defense-systems/dgtpase.md b/content/3.defense-systems/dgtpase.md
index 9c346e976eb33457504d3a41bf1ee3081f793562..5579266d177af44a936c97e7e99a31064402041b 100644
--- a/content/3.defense-systems/dgtpase.md
+++ b/content/3.defense-systems/dgtpase.md
@@ -3,16 +3,25 @@ title: dGTPase
 layout: article
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     article:
-      doi: 10.1016/j.cell.2021.09.031
-      abstract: |
-        The cyclic pyrimidines 3',5'-cyclic cytidine monophosphate (cCMP) and 3',5'-cyclic uridine monophosphate (cUMP) have been reported in multiple organisms and cell types. As opposed to the cyclic nucleotides 3',5'-cyclic adenosine monophosphate (cAMP) and 3',5'-cyclic guanosine monophosphate (cGMP), which are second messenger molecules with well-established regulatory roles across all domains of life, the biological role of cyclic pyrimidines has remained unclear. Here we report that cCMP and cUMP are second messengers functioning in bacterial immunity against viruses. We discovered a family of bacterial pyrimidine cyclase enzymes that specifically synthesize cCMP and cUMP following phage infection and demonstrate that these molecules activate immune effectors that execute an antiviral response. A crystal structure of a uridylate cyclase enzyme from this family explains the molecular mechanism of selectivity for pyrimidines as cyclization substrates. Defense systems encoding pyrimidine cyclases, denoted here Pycsar (pyrimidine cyclase system for antiphage resistance), are widespread in prokaryotes. Our results assign clear biological function to cCMP and cUMP as immunity signaling molecules in bacteria.
+      doi:  10.1038/s41564-022-01158-0 
     Sensor: Monitoring of the host cell machinery integrity
     Activator: Direc
     Effector: Nucleotide modifying
     PFAM: PF01966, PF13286
+contributors: 
+  - Aude Bernheim
+relevantAbstracts:
+  - doi:  10.1038/s41564-022-01158-0 
 ---
 
 # dGTPase
+
+## Description
+dGTPase are a family of proteins discovered in :ref{doi=10.1038/s41564-022-01158-0}. It degrades dGTP into phosphate-free deoxyguanosine. It was suggested that these *"bacterial defensive proteins deplete  deoxynucleotides from the nucleotide pool during phage infection, thus starving the phage of an essential DNA building block and halting its replication"*. The mechanism is remindful of the mechanism of SAMHD1 in humans.
+
+## Molecular mechanism 
+dGTPase degrades dGTP into phosphate-free deoxyguanosine. Phage mutants which overcome this defense carry mutations in phage-RNAP-modifying proteins suggesting, that *"phage-mediated inhibition of host transcription may be involved in triggering the activation of bacterial dNTP-depletion"*. 
+
 ## Example of genomic structure
 
 The dGTPase system is composed of one protein: Sp_dGTPase.
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-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
-    - doi: 10.1038/s41564-022-01162-4
-
----
-::
-