<italic>

Italic

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

Remarks

Emphasis as a Toggle Switch: The @toggle attribute controls the behavior of this element. When the value of @toggle is set to “no”, the emphasized text remains in the requested style, no matter what the surrounding text does. When the value of @toggle is is “yes”,, if the surrounding text is set to the same emphasis style, the text within this element will change to another emphasis style, so that the text will always be typographically distinct from its surroundings.
Using the element <italic> as an example, setting the @toggle attribute to “no” would mean that a material marked as italics will always be italics, even in an italic context. In contrast, if the @toggle attribute was set to “yes” on the <italic> element, 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, but not italic. The <italic> element would still produce italics everywhere else.

Attributes

id Document Internal Identifier
specific-use Specific Use
toggle Toggle Switch
xml:base Base

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 | private-char | chem-struct | inline-formula | tex-math | mml:math | abbrev | milestone-end | milestone-start | named-content | styled-content | fn | target | xref | sub | sup)*

Description

This element may be contained in:

Example 1

For a foreign phrase:

...
<ref id="c35">
<label>35.</label>
<note>
<p>The geometric optimization and electronic transport properties are 
all calculated by a developed <italic>ab-initio</italic> software package 
Atomistix ToolKit, which is based on the spin-polarized density-functional 
theory combined with the non-equilibrium Greens functions. ...</p>
</note>
</ref>
...

Example 2

For variable names:

...
<table-wrap id="t2" orientation="portrait" position="float">
<label>Table II.</label>
<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>
...

Example 3

<article dtd-version="1.1d2">
<front>
...
<article-meta>
<article-id pub-id-type="publisher-id">040549897</article-id>
...
<permissions>
<copyright-statement>Copyright &#x00A9; 2000, The
National Academy of Sciences</copyright-statement>
<copyright-year>2000</copyright-year>
</permissions>
<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>