<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>1405-888X</journal-id>
<journal-title><![CDATA[TIP. Revista especializada en ciencias químico-biológicas]]></journal-title>
<abbrev-journal-title><![CDATA[TIP]]></abbrev-journal-title>
<issn>1405-888X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Estudios Superiores Zaragoza]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S1405-888X2020000100206</article-id>
<article-id pub-id-type="doi">10.22201/fesz.23958723e.2020.0.234</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Características comunes de las chaperonas pequeñas y diméricas]]></article-title>
<article-title xml:lang="en"><![CDATA[Common characteristics of small dimeric chaperones]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Nava Ramírez]]></surname>
<given-names><![CDATA[Teresa]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Hansberg]]></surname>
<given-names><![CDATA[Wilhelm]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Instituto de Fisiología Celular Departamento de Biología Celular y del Desarrollo]]></institution>
<addr-line><![CDATA[Ciudad de México ]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2020</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2020</year>
</pub-date>
<volume>23</volume>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S1405-888X2020000100206&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S1405-888X2020000100206&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S1405-888X2020000100206&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Las chaperonas moleculares constituyen un mecanismo importante para evitar la muerte celular provocada por la agregación de proteínas. Las chaperonas independientes del ATP son un grupo de proteínas de bajo peso molecular que pueden proteger y ayudar a alcanzar la estructura nativa de las proteínas desplegadas o mal plegadas sin necesidad de un gasto energético. Hemos encontrado que el dominio C-terminal de las catalasas de subunidad grande tiene actividad de chaperona. Por ello, en esta revisión analizamos las características más comunes de las chaperonas pequeñas y más estudiadas como: &#945;B-cristalina, Hsp20, Spy, Hsp33 y Hsp31. En particular, se examina la participación de los aminoácidos hidrofóbicos y de los aminoácidos con carga en el reconocimiento de las proteínas sustrato, así como el papel que tiene la forma dimérica y su oligomerización en la actividad de chaperona. En cada una de esas chaperonas revisaremos la estructura de la proteína, su función, localización celular e importancia para la célula.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Molecular chaperones constitute an important mechanism to prevent cell death caused by protein aggregation. ATP-independent chaperones are a group of low molecular weight proteins that can protect or restore the native structure of unfolded or mis-folded proteins without expenditure of energy. Because we recently found that the C-terminal domain of large-size subunit catalases has a chaperone activity, we are reviewing common characteristics of the most studied low molecular size chaperones, such as &#945;B-crystalline, Hsp20, Spy, Hsp33 and Hsp31. We particularly examine the participation of hydrophobic and charged amino acid residues in protein substrate recognition and the role of dimer formation and its oligomerization in the molecular chaperone activity. We review for each of these molecular chaperones its protein structure, its cellular function and localization, and its importance for the cell.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[chaperonas moleculares]]></kwd>
<kwd lng="es"><![CDATA[independientes de ATP]]></kwd>
<kwd lng="es"><![CDATA[mecanismo de acción]]></kwd>
<kwd lng="es"><![CDATA[dímero]]></kwd>
<kwd lng="es"><![CDATA[oligomerización]]></kwd>
<kwd lng="en"><![CDATA[molecular chaperones]]></kwd>
<kwd lng="en"><![CDATA[ATP-independent]]></kwd>
<kwd lng="en"><![CDATA[mechanisms of action]]></kwd>
<kwd lng="en"><![CDATA[dimers]]></kwd>
<kwd lng="en"><![CDATA[oligomerization]]></kwd>
</kwd-group>
</article-meta>
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