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<italic> Italic

Used to mark text that should appear in an italic or slanted font.

Usage/Remarks

Italics are typically used when marking biological nomenclature such as genus or species, book titles, foreign phrases, and some mathematical expressions.
Using the Toggle Switch with Italics
The @toggle attribute can control the behavior of the <italic> element. For example, setting the @toggle attribute to “no” would mean that material marked as italics will always be italics, even in an italic context. In contrast, if the @toggle attribute is set to “yes” on an <italic> element, then if the formatting context imposes italics (whether due to another <italic> element, a stylesheet, some CSS, or other means), then the italics would be turned off within that context, making the emphasized text emphasized by contrast (typographically distinct from its surroundings) but not italic.
Attributes
specific-use
toggle (default = yes)

Base Attributes

id
xml:base
Models and Context
May be contained in
<addr-line>, <aff>, <alt-title>, <article-title>, <attrib>, <bold>, <chapter-title>, <chem-struct>, <code>, <collab>, <comment>, <compound-kwd-part>, <compound-subject-part>, <conf-theme>, <copyright-statement>, <data-title>, <def-head>, <disp-formula>, <element-citation>, <ext-link>, <fixed-case>, <funding-statement>, <gov>, <inline-formula>, <inline-media>, <inline-supplementary-material>, <italic>, <kwd>, <license-p>, <meta-value>, <mixed-citation>, <monospace>, <named-content>, <on-behalf-of>, <overline>, <p>, <part-title>, <preformat>, <price>, <product>, <rb>, <related-article>, <related-object>, <resource-name>, <roman>, <sans-serif>, <sc>, <see>, <see-also>, <series>, <source>, <std>, <strike>, <styled-content>, <sub>, <subject>, <subtitle>, <sup>, <supplement>, <support-source>, <target>, <td>, <term>, <term-head>, <textual-form>, <th>, <title>, <trans-source>, <trans-title>, <underline>, <verse-line>, <xref>
Description
Any combination of:
Content Model
<!ELEMENT  italic       (#PCDATA %emphasized-text;)*                 >
Expanded Content Model

(#PCDATA | email | ext-link | uri | inline-supplementary-material | related-article | related-object | bold | fixed-case | italic | monospace | overline | roman | sans-serif | sc | strike | underline | ruby | alternatives | inline-graphic | inline-media | chem-struct | inline-formula | abbrev | index-term | index-term-range-end | named-content | styled-content | fn | target | xref | sub | sup)*

Tagged Samples
Variable names 
...
<table-wrap id="t2" orientation="portrait" position="float">
 <caption>
  <p>Models to approximate the bound frequencies as waves 
   in X→M (<inline-graphic id="g1" xlink:href="d1"/>: Rotational, 
   <inline-graphic id="g2" xlink:href="d2"/>: Vibrate in <italic>y</italic> 
   direction, <inline-graphic id="g3" xlink:href="d3"/>: Vibrate in
   <italic>x</italic> direction, <inline-graphic id="g4" xlink:href="d4"/>: 
   Vibrate mainly in <italic>y</italic> direction including a small 
   portion of vibration in <italic>x</italic> direction, 
   <inline-graphic id="g5" xlink:href="d5"/>: Vibrate mainly in 
   <italic>x</italic> direction including a small portion of vibration 
   in <italic>y</italic> direction).</p>
 </caption>
 <table border="1">...</table>
</table-wrap>
...
Scientific terminology 
<article dtd-version="1.3">
 <front>
  <article-meta>
   ...
   <abstract>
    <p>Current evidence suggests that the length of poly(A) tails of 
     bacterial mRNAs result from a competition between poly(A) polymerase
     and exoribonucleases that attack the 3&#x2032; ends of RNAs. Here, 
     we show that host factor Hfq is also involved in poly(A) tail metabolism.
     Inactivation of the <italic>hfq</italic> gene reduces the length of poly(A) 
     tails synthesized at the 3&#x2032; end of the <italic>rpsO</italic>
     mRNA by poly(A) polymerase I <italic>in vivo</italic>. <italic>In vitro</italic>,
     Hfq stimulates synthesis of long tails by poly(A) polymerase I. The strong
     binding of Hfq to oligoadenylated RNA probably explains why it stimulates
     elongation of primers that already harbor tails of 20&#x2013;35 A.
     Polyadenylation becomes processive in the presence of Hfq. The similar
     properties of Hfq and the PABPII poly(A) binding protein, which stimulates
     poly(A) tail elongation in mammals, indicates that similar mechanisms 
     control poly(A) tail synthesis in prokaryotes and eukaryotes.</p>
   </abstract>
  </article-meta>
 </front>
 ...
</article>