display abstract

components/content/ReferencesList.vue

 <template>
   <ClientOnly fallback-tag="span" fallback="Loading references...">
-    <v-list v-if="computedItems.length > 0" :items="computedItems" item-props lines="three">
-      <template #subtitle="{ item }">
-        <div>{{ item.subtitle }}</div>
-        <div>{{ item.containerTitle }} ({{ item.year }})</div>
-      </template>
-      <template #prepend="{ item }">
-        <v-avatar>
-          <v-icon>{{ item.prependIcon }}</v-icon>
-        </v-avatar>
-      </template>
+    <v-list v-if="computedItems.length > 0">
+      <v-list-item v-for="item in computedItems" :key="item.title" :title="item.title" lines="three" :href="item.href"
+        :target="item.target">
+        <template #title="{ title }">
+          <span class="font-weight-bold">{{ title }}</span>
+        </template>
+        <template #prepend>
+          <v-avatar>
+            <v-icon>{{ item.prependIcon }}</v-icon>
+          </v-avatar>
+        </template>
+        <template #subtitle>
+          <div>{{ item.subtitle }}</div>
+          <div>{{ item.containerTitle }} ({{ item.year }})</div>
+        </template>
+        <v-card flat color="transparent" class="text-justify my-2">
+          {{ item.abstract }}
+        </v-card>
+      </v-list-item>
+
+
     </v-list>
   </ClientOnly>
 </template>
@@ -61,12 +72,18 @@ const computedItems = computed(() => {
         published,
         ...rest
       } = doi.message;
+      console.log(abstract)
+      let sanitizedAbstract = abstract
+      if (sanitizedAbstract) {
+        sanitizedAbstract = /\<jats\:p\>(.*)\<\/jats\:p\>/.exec(sanitizedAbstract)?.[1] ?? ''
+      }
+      console.log(sanitizedAbstract)
       return {
         DOI,
         title: title[0],
         subtitle: toAuthorsString(doi?.message?.author ?? []),
         containerTitle: cts?.length > 0 ? cts[0] : ct?.length > 0 ? ct[0] : "",
-        abstract,
+        abstract: sanitizedAbstract,
         year: published["date-parts"][0][0],
         href: getReferenceUrl(DOI),
         target: "_blank",

content/2.defense-systems/abia.md

@@ -32,6 +32,18 @@ A system from *lactococcal plasmid* in *lactococci* has an anti-phage effect aga
 
 ## Relevant abstracts
 
+
+::references-list
+---
+items:
+    - 10.1016/j.mib.2005.06.006
+    - 10.1023/A:1002027321171
+    - 10.1093/nar/gkac467
+---
+::
+
+<!-- 10.1016/j.mib.2005.06.006  -->
+
 **Chopin, M.-C., Chopin, A. & Bidnenko, E. Phage abortive infection in lactococci: variations on a theme. Curr Opin Microbiol 8, 473-479 (2005).**
 Abortive infection (Abi) systems, also called phage exclusion, block phage multiplication and cause premature bacterial cell death upon phage infection. This decreases the number of progeny particles and limits their spread to other cells allowing the bacterial population to survive. Twenty Abi systems have been isolated in Lactococcus lactis, a bacterium used in cheese-making fermentation processes, where phage attacks are of economical importance. Recent insights in their expression and mode of action indicate that, behind diverse phenotypic and molecular effects, lactococcal Abis share common traits with the well-studied Escherichia coli systems Lit and Prr. Abis are widespread in bacteria, and recent analysis indicates that Abis might have additional roles other than conferring phage resistance.
 

content/2.defense-systems/avast.md

@@ -94,6 +94,15 @@ Subsystem CcAvs4 with a system from *Corallococcus coralloides* in *Escherichia
 
 ## Relevant abstracts
 
+
+::references-list
+---
+items:
+    - 10.1126/science.abm4096
+    - 10.1126/science.aba0372
+---
+::
+
 **Gao, L. A. et al. Prokaryotic innate immunity through pattern recognition of conserved viral proteins. Science 377, eabm4096 (2022).**
 Many organisms have evolved specialized immune pattern-recognition receptors, including nucleotide-binding oligomerization domain-like receptors (NLRs) of the STAND superfamily that are ubiquitous in plants, animals, and fungi. Although the roles of NLRs in eukaryotic immunity are well established, it is unknown whether prokaryotes use similar defense mechanisms. Here, we show that antiviral STAND (Avs) homologs in bacteria and archaea detect hallmark viral proteins, triggering Avs tetramerization and the activation of diverse N-terminal effector domains, including DNA endonucleases, to abrogate infection. Cryo-electron microscopy reveals that Avs sensor domains recognize conserved folds, active-site residues, and enzyme ligands, allowing a single Avs receptor to detect a wide variety of viruses. These findings extend the paradigm of pattern recognition of pathogen-specific proteins across all three domains of life.