<?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>0026-1742</journal-id>
<journal-title><![CDATA[Revista de la Facultad de Medicina (México)]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. Fac. Med. (Méx.)]]></abbrev-journal-title>
<issn>0026-1742</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Medicina]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0026-17422023000400008</article-id>
<article-id pub-id-type="doi">10.22201/fm.24484865e.2023.66.4.02</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[La función de las proteínas de choque térmico en las infecciones virales]]></article-title>
<article-title xml:lang="en"><![CDATA[The Role of Heat Shock Proteins in Viral Infections]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Olvera-Sánchez]]></surname>
<given-names><![CDATA[Sofía]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Martínez]]></surname>
<given-names><![CDATA[Federico]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México  ]]></institution>
<addr-line><![CDATA[Ciudad de México ]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>08</month>
<year>2023</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>08</month>
<year>2023</year>
</pub-date>
<volume>66</volume>
<numero>4</numero>
<fpage>8</fpage>
<lpage>19</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S0026-17422023000400008&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S0026-17422023000400008&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S0026-17422023000400008&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Las proteínas de choque térmico se describieron como una respuesta intracelular al estrés calórico; sin embargo, al paso del tiempo, se observó que estas proteínas tienen múltiples funciones y que participan de manera relevante tanto en los procesos fisiológicos como patológicos. Las actividades que realizan las proteínas de choque térmico se relacionan con su localización, que puede ser intra o extracelular, al momento fisiológico y a las diferentes asociaciones estructurales, que pueden ser desde péptidos derivados de estas, hasta dímeros o multímeros. Con base en estas características funcionales, se les ha denominado proteínas multiempleo o &#8220;moonlighting proteins&#8221;. En este artículo se describen algunas de las actividades de estas proteínas con relación al sistema inmunológico y las infecciones virales, en particular con los procesos inflamatorios.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Heat shock proteins (HSP) were first described as a cell response to heat stress. However, over time, it has become clear they have multiple functions inside and outside cells, and that they actively participate in different physiological and pathological processes. They perform functions related to their cellular location or physiological moment, which is why they have been called multi-use proteins or &#8220;moonlighting proteins&#8221;. Furthermore, HSP activity is associated with different structural conformations, from peptides derived from them or as dimers or multimers, to mention a few. This article describes these functions and their relationship with the immune system, and their relationship with viral infection, particularly with inflammatory processes.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[HSP]]></kwd>
<kwd lng="es"><![CDATA[infección viral]]></kwd>
<kwd lng="es"><![CDATA[COVID-19, sistema inmunológico]]></kwd>
<kwd lng="es"><![CDATA[inflamación]]></kwd>
<kwd lng="en"><![CDATA[HSP]]></kwd>
<kwd lng="en"><![CDATA[viral infection]]></kwd>
<kwd lng="en"><![CDATA[COVID-19]]></kwd>
<kwd lng="en"><![CDATA[immune system]]></kwd>
<kwd lng="en"><![CDATA[inflammation processes]]></kwd>
</kwd-group>
</article-meta>
</front><back>
<ref-list>
<ref id="B1">
<label>1</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Richter]]></surname>
<given-names><![CDATA[K]]></given-names>
</name>
<name>
<surname><![CDATA[Haslbeck]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Buchner]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The heat shock response: life on the verge of death]]></article-title>
<source><![CDATA[Molecular Cell]]></source>
<year>2010</year>
<volume>40</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>253-66</page-range></nlm-citation>
</ref>
<ref id="B2">
<label>2</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kampinga]]></surname>
<given-names><![CDATA[HH]]></given-names>
</name>
<name>
<surname><![CDATA[Hageman]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Vos]]></surname>
<given-names><![CDATA[MJ]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Guidelines for the nomenclature of the human heat shock proteins]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2009</year>
<volume>14</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>105-11</page-range></nlm-citation>
</ref>
<ref id="B3">
<label>3</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Chatterjee]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Burns]]></surname>
<given-names><![CDATA[TF.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Targeting heat shock proteins in cancer: A promising therapeutic approach]]></article-title>
<source><![CDATA[Int J Mol Sci]]></source>
<year>2017</year>
<volume>18</volume>
<numero>9</numero>
<issue>9</issue>
<page-range>1978</page-range></nlm-citation>
</ref>
<ref id="B4">
<label>4</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Mogk]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Ruger-Herreros]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
<name>
<surname><![CDATA[Bukau]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Cellular functions and mechanisms of action of small heat shock proteins]]></article-title>
<source><![CDATA[Annu Rev Microbiol]]></source>
<year>2019</year>
<volume>73</volume>
<page-range>89-110</page-range></nlm-citation>
</ref>
<ref id="B5">
<label>5</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zolkiewski]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
<name>
<surname><![CDATA[Nagy]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Aggregate reactivation mediated by the Hsp100 chaperones]]></article-title>
<source><![CDATA[Arch Biochem Biophys]]></source>
<year>2012</year>
<volume>520</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>1-6</page-range></nlm-citation>
</ref>
<ref id="B6">
<label>6</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Jackson]]></surname>
<given-names><![CDATA[SE.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hsp90: structure and function]]></article-title>
<source><![CDATA[Top Curr Chem]]></source>
<year>2013</year>
<volume>328</volume>
<page-range>155-240</page-range></nlm-citation>
</ref>
<ref id="B7">
<label>7</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Takakuwa]]></surname>
<given-names><![CDATA[JE]]></given-names>
</name>
<name>
<surname><![CDATA[Nitika Knighton]]></surname>
<given-names><![CDATA[LE]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Oligomerization of Hsp70: Current perspectives on regulation and function]]></article-title>
<source><![CDATA[Front Mol Biosci]]></source>
<year>2019</year>
<volume>6</volume>
<page-range>1-7</page-range></nlm-citation>
</ref>
<ref id="B8">
<label>8</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Enriquez]]></surname>
<given-names><![CDATA[AS]]></given-names>
</name>
<name>
<surname><![CDATA[Rojo]]></surname>
<given-names><![CDATA[HM]]></given-names>
</name>
<name>
<surname><![CDATA[Bhatt]]></surname>
<given-names><![CDATA[JM]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The human mitocondrial Hsp60 in the APO conformation forms a stable tetradecameric complex]]></article-title>
<source><![CDATA[Cell Cycle]]></source>
<year>2017</year>
<volume>16</volume>
<numero>13</numero>
<issue>13</issue>
<page-range>1309-19</page-range></nlm-citation>
</ref>
<ref id="B9">
<label>9</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Caruso Bavisotto]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
<name>
<surname><![CDATA[Alberti]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
<name>
<surname><![CDATA[Vitale]]></surname>
<given-names><![CDATA[AM]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hsp60 Post-translational modifications: Functional and pathological consequences]]></article-title>
<source><![CDATA[Front Mol Biosci]]></source>
<year>2020</year>
<volume>7</volume>
<page-range>1-11</page-range></nlm-citation>
</ref>
<ref id="B10">
<label>10</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Boelens]]></surname>
<given-names><![CDATA[WC.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structural aspects of the human small heat shock proteins related to their functional activities]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2020</year>
<volume>25</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>581-91</page-range></nlm-citation>
</ref>
<ref id="B11">
<label>11</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Collier]]></surname>
<given-names><![CDATA[MP]]></given-names>
</name>
<name>
<surname><![CDATA[Moreira]]></surname>
<given-names><![CDATA[KB]]></given-names>
</name>
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[KH]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns]]></article-title>
<source><![CDATA[Sci Rep]]></source>
<year>2021</year>
<volume>11</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>1-15</page-range></nlm-citation>
</ref>
<ref id="B12">
<label>12</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Jeffery]]></surname>
<given-names><![CDATA[CJ.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Protein moonlighting: what is it, and why is it important?]]></article-title>
<source><![CDATA[Philos Trans R Soc Lond B Biol Sci]]></source>
<year>2018</year>
<volume>373</volume>
<numero>1738</numero>
<issue>1738</issue>
<page-range>1-8</page-range></nlm-citation>
</ref>
<ref id="B13">
<label>13</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Molvarec]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Tamási]]></surname>
<given-names><![CDATA[L]]></given-names>
</name>
<name>
<surname><![CDATA[Losonczy]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Circulating heat shock protein 70 (HSPA1A) in normal and pathological pregnancies]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2010</year>
<volume>15</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>237-47</page-range></nlm-citation>
</ref>
<ref id="B14">
<label>14</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Dvorakova]]></surname>
<given-names><![CDATA[L]]></given-names>
</name>
<name>
<surname><![CDATA[Ivankova]]></surname>
<given-names><![CDATA[K]]></given-names>
</name>
<name>
<surname><![CDATA[Krofta]]></surname>
<given-names><![CDATA[L]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Expression profile of heat shock proteins in placental tissues of patients with preterm prelabor rupture of membranes and spontaneous preterm labor with intact membranes]]></article-title>
<source><![CDATA[Am J Reprod Immunol]]></source>
<year>2017</year>
<volume>78</volume>
<numero>4</numero>
<issue>4</issue>
</nlm-citation>
</ref>
<ref id="B15">
<label>15</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Monreal-Flores]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Espinosa-García]]></surname>
<given-names><![CDATA[MT]]></given-names>
</name>
<name>
<surname><![CDATA[García-Regalado]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The heat shock protein 60 promotes progesterone synthesis in mitochondria of JEG-3 cells]]></article-title>
<source><![CDATA[Reprod Biol]]></source>
<year>2017</year>
<volume>17</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>154-61</page-range></nlm-citation>
</ref>
<ref id="B16">
<label>16</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Olvera-Sanchez]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Espinosa-Garcia]]></surname>
<given-names><![CDATA[MT]]></given-names>
</name>
<name>
<surname><![CDATA[Monreal]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Mitochondrial heat shock protein participates in placental steroidogenesis]]></article-title>
<source><![CDATA[Placenta]]></source>
<year>2011</year>
<volume>32</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>222-9</page-range></nlm-citation>
</ref>
<ref id="B17">
<label>17</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Hromadnikova]]></surname>
<given-names><![CDATA[I]]></given-names>
</name>
<name>
<surname><![CDATA[Dvorakova]]></surname>
<given-names><![CDATA[L]]></given-names>
</name>
<name>
<surname><![CDATA[Kotlabova]]></surname>
<given-names><![CDATA[K]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Circulating heat shock protein mRNA profile in gestational hypertension, pre-eclampsia &amp; foetal growth restriction]]></article-title>
<source><![CDATA[Indian J Med Res]]></source>
<year>2016</year>
<volume>144</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>229-37</page-range></nlm-citation>
</ref>
<ref id="B18">
<label>18</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Álvarez-Cabrera]]></surname>
<given-names><![CDATA[MC]]></given-names>
</name>
<name>
<surname><![CDATA[Barrientos-Galeana]]></surname>
<given-names><![CDATA[E]]></given-names>
</name>
<name>
<surname><![CDATA[Barrera-García]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Secretion of heat shock -60, -70 kD protein, IL-1&#946; and TNF&#945; levels in serum of a term normal pregnancy and patients with pre-eclampsia development]]></article-title>
<source><![CDATA[J Cell Mol Med]]></source>
<year>2018</year>
<volume>22</volume>
<numero>11</numero>
<issue>11</issue>
<page-range>5748-52</page-range></nlm-citation>
</ref>
<ref id="B19">
<label>19</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Yun]]></surname>
<given-names><![CDATA[CW]]></given-names>
</name>
<name>
<surname><![CDATA[Kim]]></surname>
<given-names><![CDATA[HJ]]></given-names>
</name>
<name>
<surname><![CDATA[Lim]]></surname>
<given-names><![CDATA[JH]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock proteins: Agents of cancer development and therapeutic targets in anti-cancer therapy]]></article-title>
<source><![CDATA[Cells]]></source>
<year>2019</year>
<volume>9</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>1-30</page-range></nlm-citation>
</ref>
<ref id="B20">
<label>20</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Bellini]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Barutta]]></surname>
<given-names><![CDATA[F]]></given-names>
</name>
<name>
<surname><![CDATA[Mastrocola]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock proteins in vascular diabetic complications: Review and future perspective]]></article-title>
<source><![CDATA[Int J Mol Sci]]></source>
<year>2017</year>
<volume>18</volume>
<numero>12</numero>
<issue>12</issue>
<page-range>2-26</page-range></nlm-citation>
</ref>
<ref id="B21">
<label>21</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Skórzy&#324;ska-Dziduszko]]></surname>
<given-names><![CDATA[KE]]></given-names>
</name>
<name>
<surname><![CDATA[Kimber-Trojnar]]></surname>
<given-names><![CDATA[&#379;]]></given-names>
</name>
<name>
<surname><![CDATA[Patro-Ma&#322;ysza]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock proteins as a potential therapeutic target in the treatment of gestational diabetes mellitus: what we know so far]]></article-title>
<source><![CDATA[Int J Mol Sci]]></source>
<year>2018</year>
<volume>19</volume>
<numero>10</numero>
<issue>10</issue>
<page-range>1-14</page-range></nlm-citation>
</ref>
<ref id="B22">
<label>22</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[McCarty]]></surname>
<given-names><![CDATA[MF.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Induction of heat shock proteins may combat insulin resistance]]></article-title>
<source><![CDATA[Med Hypotheses]]></source>
<year>2006</year>
<volume>66</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>527-34</page-range></nlm-citation>
</ref>
<ref id="B23">
<label>23</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Rodríguez-Iturbe]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
<name>
<surname><![CDATA[Johnson]]></surname>
<given-names><![CDATA[RJ.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock proteins and cardiovascular disease]]></article-title>
<source><![CDATA[Physiol Int]]></source>
<year>2018</year>
<volume>105</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>19-37</page-range></nlm-citation>
</ref>
<ref id="B24">
<label>24</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Ranek]]></surname>
<given-names><![CDATA[MJ]]></given-names>
</name>
<name>
<surname><![CDATA[Stachowski]]></surname>
<given-names><![CDATA[MJ]]></given-names>
</name>
<name>
<surname><![CDATA[Kirk]]></surname>
<given-names><![CDATA[JA]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The role of heat shock proteins and co-chaperones in heart failure]]></article-title>
<source><![CDATA[Philos Trans R Soc Lond B Biol Sci]]></source>
<year>2018</year>
<volume>373</volume>
<numero>1738</numero>
<issue>1738</issue>
<page-range>20160530</page-range></nlm-citation>
</ref>
<ref id="B25">
<label>25</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Deniset]]></surname>
<given-names><![CDATA[JF]]></given-names>
</name>
<name>
<surname><![CDATA[Pierce]]></surname>
<given-names><![CDATA[GN.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock proteins: Mediators of atherosclerotic development]]></article-title>
<source><![CDATA[Curr Drug Targets]]></source>
<year>2015</year>
<volume>16</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>816-26</page-range></nlm-citation>
</ref>
<ref id="B26">
<label>26</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Binder]]></surname>
<given-names><![CDATA[RJ.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock protein vaccines: from bench to bedside]]></article-title>
<source><![CDATA[Int Rev Immunol]]></source>
<year>2006</year>
<volume>25</volume>
<numero>5-6</numero>
<issue>5-6</issue>
<page-range>353-75</page-range></nlm-citation>
</ref>
<ref id="B27">
<label>27</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Pockley]]></surname>
<given-names><![CDATA[AG]]></given-names>
</name>
<name>
<surname><![CDATA[Henderson]]></surname>
<given-names><![CDATA[B.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Extracellular cell stress (heat shock) proteins-immune responses and disease: an over- view]]></article-title>
<source><![CDATA[Philos Trans R Soc Lond B Biol Sci]]></source>
<year>2018</year>
<volume>373</volume>
<numero>1738</numero>
<issue>1738</issue>
<page-range>20160522</page-range></nlm-citation>
</ref>
<ref id="B28">
<label>28</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Sedger]]></surname>
<given-names><![CDATA[L]]></given-names>
</name>
<name>
<surname><![CDATA[Ruby]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock response to vaccinia virus infection]]></article-title>
<source><![CDATA[J Virol]]></source>
<year>1994</year>
<volume>68</volume>
<numero>7</numero>
<issue>7</issue>
<page-range>4685-9</page-range></nlm-citation>
</ref>
<ref id="B29">
<label>29</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[De Maio]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Vazquez]]></surname>
<given-names><![CDATA[D.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Extracellular heat shock proteins: a new location, a new function]]></article-title>
<source><![CDATA[Shock]]></source>
<year>2013</year>
<volume>40</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>239-46</page-range></nlm-citation>
</ref>
<ref id="B30">
<label>30</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Reddy]]></surname>
<given-names><![CDATA[VS]]></given-names>
</name>
<name>
<surname><![CDATA[Madala]]></surname>
<given-names><![CDATA[SK]]></given-names>
</name>
<name>
<surname><![CDATA[Trinath]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Extracellular small heat shock proteins: exosomal biogenesis and function]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2018</year>
<volume>23</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>441-54</page-range></nlm-citation>
</ref>
<ref id="B31">
<label>31</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[De Maio]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: a form of communication during injury, infection, and cell damage. It is never known how far a controversial finding will go! Dedicated to Ferruccio Ritossa]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2011</year>
<volume>16</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>235-49</page-range></nlm-citation>
</ref>
<ref id="B32">
<label>32</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wells]]></surname>
<given-names><![CDATA[AD]]></given-names>
</name>
<name>
<surname><![CDATA[Malkovsky]]></surname>
<given-names><![CDATA[M.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock proteins, tumor immunogenicity and antigen presentation: an integrated view]]></article-title>
<source><![CDATA[Immunol Today]]></source>
<year>2000</year>
<volume>21</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>129-32</page-range></nlm-citation>
</ref>
<ref id="B33">
<label>33</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wallin]]></surname>
<given-names><![CDATA[RP]]></given-names>
</name>
<name>
<surname><![CDATA[Lundqvist]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Moré]]></surname>
<given-names><![CDATA[SH]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat-shock proteins as activators of the innate immune system]]></article-title>
<source><![CDATA[Trends Immunol]]></source>
<year>2002</year>
<volume>23</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>130-5</page-range></nlm-citation>
</ref>
<ref id="B34">
<label>34</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Basu]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Binder]]></surname>
<given-names><![CDATA[RJ]]></given-names>
</name>
<name>
<surname><![CDATA[Suto]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and actívate the NF-kappa B pathway]]></article-title>
<source><![CDATA[Int Immunol]]></source>
<year>2000</year>
<volume>12</volume>
<numero>11</numero>
<issue>11</issue>
<page-range>1539-46</page-range></nlm-citation>
</ref>
<ref id="B35">
<label>35</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Quintana]]></surname>
<given-names><![CDATA[FJ]]></given-names>
</name>
<name>
<surname><![CDATA[Solomon]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Cohen]]></surname>
<given-names><![CDATA[IR]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Induction of IgG3 to LPS via Toll-like receptor 4 co-stimulation]]></article-title>
<source><![CDATA[PLoS One]]></source>
<year>2008</year>
<volume>3</volume>
<numero>10</numero>
<issue>10</issue>
</nlm-citation>
</ref>
<ref id="B36">
<label>36</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Feng]]></surname>
<given-names><![CDATA[Z]]></given-names>
</name>
<name>
<surname><![CDATA[Huang]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Investigation on the effect of peptides mixture from tumor cells inducing antitumor specific immune response]]></article-title>
<source><![CDATA[Sci China C Life Sci]]></source>
<year>2002</year>
<volume>45</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>361-9</page-range></nlm-citation>
</ref>
<ref id="B37">
<label>37</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Pockley]]></surname>
<given-names><![CDATA[AG]]></given-names>
</name>
<name>
<surname><![CDATA[Multhoff]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Cell stress proteins in extracelular fluids: friend or foe?]]></article-title>
<source><![CDATA[Novartis Found Symp]]></source>
<year>2008</year>
<volume>291</volume>
<page-range>86-95</page-range></nlm-citation>
</ref>
<ref id="B38">
<label>38</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Asea]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Kraeft]]></surname>
<given-names><![CDATA[SK]]></given-names>
</name>
<name>
<surname><![CDATA[Kurt-Jones]]></surname>
<given-names><![CDATA[EA]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[HSP70 stimulates cytokine production through a CD14-dependant pathway, demonstrating its dual role as a chaperone and cytokine]]></article-title>
<source><![CDATA[Nat Med]]></source>
<year>2000</year>
<volume>6</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>435-42</page-range></nlm-citation>
</ref>
<ref id="B39">
<label>39</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Basta]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Stoessel]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Basler]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Cross-presentation of the long-lived lymphocytic choriomeningitis virus nucleoprotein does not require neosynthesis and is enhanced via heat shock proteins]]></article-title>
<source><![CDATA[J Immunol]]></source>
<year>2005</year>
<volume>175</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>796-805</page-range></nlm-citation>
</ref>
<ref id="B40">
<label>40</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Guo]]></surname>
<given-names><![CDATA[QY]]></given-names>
</name>
<name>
<surname><![CDATA[Yuan]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Peng]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Antitumor activity of mixed heat shock protein/peptide vaccine and cyclophosphamide plus interleukin-12 in mice sarcoma]]></article-title>
<source><![CDATA[J Exp Clin Cancer Res]]></source>
<year>2011</year>
<volume>30</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>24</page-range></nlm-citation>
</ref>
<ref id="B41">
<label>41</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[McCarthy]]></surname>
<given-names><![CDATA[MK]]></given-names>
</name>
<name>
<surname><![CDATA[Weinberg]]></surname>
<given-names><![CDATA[JB.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The immunoproteasome and viral infection: a complex regulator of inflammation]]></article-title>
<source><![CDATA[Front Microbiol]]></source>
<year>2015</year>
<volume>29</volume>
<page-range>6-21</page-range></nlm-citation>
</ref>
<ref id="B42">
<label>42</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Yamano]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
<name>
<surname><![CDATA[Mizukami]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Murata]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hsp90-mediated assembly of the 26 S proteasome is involved in major histocompatibility complex class I antigen processing]]></article-title>
<source><![CDATA[J Biol Chem]]></source>
<year>2008</year>
<volume>283</volume>
<numero>42</numero>
<issue>42</issue>
<page-range>28060-5</page-range></nlm-citation>
</ref>
<ref id="B43">
<label>43</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
<name>
<surname><![CDATA[Androlewicz]]></surname>
<given-names><![CDATA[MJ.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Heat shock protein 70 moderately enhances peptide binding and transport by the transporter associated with antigen processing]]></article-title>
<source><![CDATA[Immunol Lett]]></source>
<year>2001</year>
<volume>75</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>143-8</page-range></nlm-citation>
</ref>
<ref id="B44">
<label>44</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[van Eden]]></surname>
<given-names><![CDATA[W.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Immune tolerance therapies for autoimmune diseases based on heat shock protein T-cell epitopes]]></article-title>
<source><![CDATA[Philos Trans R Soc Lond B Biol Sci]]></source>
<year>2018</year>
<volume>373</volume>
<numero>1738</numero>
<issue>1738</issue>
<page-range>20160531</page-range></nlm-citation>
</ref>
<ref id="B45">
<label>45</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Prakken]]></surname>
<given-names><![CDATA[BJ]]></given-names>
</name>
<name>
<surname><![CDATA[Samodal]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Le]]></surname>
<given-names><![CDATA[TD]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Epitope-specific immunotherapy induces immune deviation of proinflammatory T cells in rheumatoid arthritis]]></article-title>
<source><![CDATA[Proc Natl Acad Sci U S A]]></source>
<year>2004</year>
<volume>101</volume>
<numero>12</numero>
<issue>12</issue>
<page-range>4228-33</page-range></nlm-citation>
</ref>
<ref id="B46">
<label>46</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Koffeman]]></surname>
<given-names><![CDATA[EC]]></given-names>
</name>
<name>
<surname><![CDATA[Genovese]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Amox]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Epitopespecific immunotherapy of rheumatoid arthritis: clinical responsiveness occurs with immune deviation and relies on the expression of a cluster of molecules associated with T cell tolerance in a double-blind, placebo-controlled, pilot phase II trial]]></article-title>
<source><![CDATA[Arthritis Rheum]]></source>
<year>2009</year>
<volume>60</volume>
<numero>11</numero>
<issue>11</issue>
<page-range>3207-16</page-range></nlm-citation>
</ref>
<ref id="B47">
<label>47</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wy&#380;ewski]]></surname>
<given-names><![CDATA[Z]]></given-names>
</name>
<name>
<surname><![CDATA[Gregorczyk]]></surname>
<given-names><![CDATA[KP]]></given-names>
</name>
<name>
<surname><![CDATA[Szczepanowska]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Functional role of Hsp60 as a positive regulator of human viral infection progression]]></article-title>
<source><![CDATA[Acta Virol]]></source>
<year>2018</year>
<volume>62</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>33-40</page-range></nlm-citation>
</ref>
<ref id="B48">
<label>48</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Lubkowska]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Pluta]]></surname>
<given-names><![CDATA[W]]></given-names>
</name>
<name>
<surname><![CDATA[Stro&#324;ska]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Role of heat shock proteins (HSP70 and HSP90) in viral infection]]></article-title>
<source><![CDATA[Int J Mol Sci]]></source>
<year>2021</year>
<volume>22</volume>
<numero>17</numero>
<issue>17</issue>
<page-range>9366</page-range></nlm-citation>
</ref>
<ref id="B49">
<label>49</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Vega]]></surname>
<given-names><![CDATA[VL]]></given-names>
</name>
<name>
<surname><![CDATA[Rodríguez-Silva]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Frey]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membraneassociated form that activates macrophages]]></article-title>
<source><![CDATA[J Immunol]]></source>
<year>2008</year>
<volume>180</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>4299-307</page-range></nlm-citation>
</ref>
<ref id="B50">
<label>50</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Vabulas]]></surname>
<given-names><![CDATA[RM]]></given-names>
</name>
<name>
<surname><![CDATA[Ahmad-Nejad]]></surname>
<given-names><![CDATA[P]]></given-names>
</name>
<name>
<surname><![CDATA[da Costa]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells]]></article-title>
<source><![CDATA[J Biol Chem]]></source>
<year>2001</year>
<volume>276</volume>
<numero>33</numero>
<issue>33</issue>
<page-range>31332-9</page-range></nlm-citation>
</ref>
<ref id="B51">
<label>51</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Swaroop]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Mahadevan]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Shankar]]></surname>
<given-names><![CDATA[SK]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[HSP60 critically regulates endogenous IL-1&#946; production in activated microglia by stimulating NLRP3 inflammasome pathway]]></article-title>
<source><![CDATA[J Neuroinflammation]]></source>
<year>2018</year>
<volume>15</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>317</page-range></nlm-citation>
</ref>
<ref id="B52">
<label>52</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Ghosh]]></surname>
<given-names><![CDATA[JC]]></given-names>
</name>
<name>
<surname><![CDATA[Dohi]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
<name>
<surname><![CDATA[Kang]]></surname>
<given-names><![CDATA[BH]]></given-names>
</name>
<name>
<surname><![CDATA[Altieri]]></surname>
<given-names><![CDATA[DC.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hsp60 regulation of tumor cell apoptosis]]></article-title>
<source><![CDATA[J Biol Chem]]></source>
<year>2008</year>
<volume>283</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>5188-94</page-range></nlm-citation>
</ref>
<ref id="B53">
<label>53</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Tanaka]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
<name>
<surname><![CDATA[Kanai]]></surname>
<given-names><![CDATA[F]]></given-names>
</name>
<name>
<surname><![CDATA[Kawakami]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Interaction of the hepatitis B virus X protein (HBx) with heat shock protein 60 enhances HBx-mediated apoptosis]]></article-title>
<source><![CDATA[Biochem Biophys Res Commun]]></source>
<year>2004</year>
<volume>318</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>461-9</page-range></nlm-citation>
</ref>
<ref id="B54">
<label>54</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Okamoto]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
<name>
<surname><![CDATA[Nishimura]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
<name>
<surname><![CDATA[Ichimura]]></surname>
<given-names><![CDATA[T.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90]]></article-title>
<source><![CDATA[EMBO J]]></source>
<year>2006</year>
<volume>25</volume>
<numero>20</numero>
<issue>20</issue>
<page-range>5015-25</page-range></nlm-citation>
</ref>
<ref id="B55">
<label>55</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Batra]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Tripathi]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Kumar]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Human Heat shock protein 40 (Hsp40/DnaJB1) promotes influenza A virus replication by assisting nuclear import of viral ribonucleoproteins]]></article-title>
<source><![CDATA[Sci Rep]]></source>
<year>2016</year>
<volume>6</volume>
<page-range>19063</page-range></nlm-citation>
</ref>
<ref id="B56">
<label>56</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zaim]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Chong]]></surname>
<given-names><![CDATA[JH]]></given-names>
</name>
<name>
<surname><![CDATA[Sankaranarayanan]]></surname>
<given-names><![CDATA[V]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[COVID-19 and multiorgan response]]></article-title>
<source><![CDATA[Curr Probl Cardiol]]></source>
<year>2020</year>
<volume>45</volume>
<numero>8</numero>
<issue>8</issue>
<page-range>100618</page-range></nlm-citation>
</ref>
<ref id="B57">
<label>57</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Arya]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Kumari]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Pandey]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
<name>
<surname><![CDATA[Mistry]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Structural insights into SARS-CoV-2 proteins]]></article-title>
<source><![CDATA[J Mol Biol]]></source>
<year>2021</year>
<volume>433</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>166725</page-range></nlm-citation>
</ref>
<ref id="B58">
<label>58</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Marino Gammazza]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Légaré]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Lo Bosco]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2020</year>
<volume>25</volume>
<numero>5</numero>
<issue>5</issue>
<page-range>737-41</page-range></nlm-citation>
</ref>
<ref id="B59">
<label>59</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Lucchese]]></surname>
<given-names><![CDATA[G]]></given-names>
</name>
<name>
<surname><![CDATA[Flöel]]></surname>
<given-names><![CDATA[A.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[SARS-CoV-2 and Guillain-Barré syndrome: molecular mimicry with human heat shock proteins as potential pathogenic mechanism]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2020</year>
<volume>25</volume>
<numero>5</numero>
<issue>5</issue>
<page-range>731-5</page-range></nlm-citation>
</ref>
<ref id="B60">
<label>60</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Del Carmen Domínguez]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Cabrales]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Lorenzo]]></surname>
<given-names><![CDATA[N]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Biodistribution and pharmacokinetic profiles of an altered peptide ligand derived from heat-shock proteins 60 in Lewis rats]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2020</year>
<volume>25</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>133-40</page-range></nlm-citation>
</ref>
<ref id="B61">
<label>61</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Hernandez-Cedeño]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Venegas-Rodriguez]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Peña-Ruiz]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[CIGB-258, a peptide derived from human heatshock protein 60, decreases hyperinflammation in COVID-19 patients]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2021</year>
<volume>26</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>515-25</page-range></nlm-citation>
</ref>
<ref id="B62">
<label>62</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Qu]]></surname>
<given-names><![CDATA[B]]></given-names>
</name>
<name>
<surname><![CDATA[Jia]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
<name>
<surname><![CDATA[Liu]]></surname>
<given-names><![CDATA[Y]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The detection and role of heat shock protein 70 in various nondisease conditions and disease conditions: a literature review]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2015</year>
<volume>20</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>885-92</page-range></nlm-citation>
</ref>
<ref id="B63">
<label>63</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wan]]></surname>
<given-names><![CDATA[Q]]></given-names>
</name>
<name>
<surname><![CDATA[Song]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development]]></article-title>
<source><![CDATA[Signal Transduct Target Ther]]></source>
<year>2020</year>
<volume>5</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>125</page-range></nlm-citation>
</ref>
<ref id="B64">
<label>64</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Jakovac]]></surname>
<given-names><![CDATA[H.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[COVID-19 and hypertension: is the HSP60 culprit for the severe course and worse outcome?]]></article-title>
<source><![CDATA[Am J Physiol Heart Circ Physiol]]></source>
<year>2020</year>
<volume>319</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>H793-6</page-range></nlm-citation>
</ref>
<ref id="B65">
<label>65</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Tian]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Guo]]></surname>
<given-names><![CDATA[X]]></given-names>
</name>
<name>
<surname><![CDATA[Liu]]></surname>
<given-names><![CDATA[XM]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Extracellular HSP60 induces inflammation through activating and up-regulating TLRs in cardiomyocytes]]></article-title>
<source><![CDATA[Cardiovasc Res]]></source>
<year>2013</year>
<volume>98</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>391-401</page-range></nlm-citation>
</ref>
<ref id="B66">
<label>66</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Romagnoli]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Peris]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[De Gaudio]]></surname>
<given-names><![CDATA[AR]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[SARS-CoV-2 and COVID-19: from the bench to the bedside]]></article-title>
<source><![CDATA[Physiol Rev]]></source>
<year>2020</year>
<volume>100</volume>
<numero>4</numero>
<issue>4</issue>
<page-range>1455-66</page-range></nlm-citation>
</ref>
<ref id="B67">
<label>67</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Krause]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[Keane]]></surname>
<given-names><![CDATA[K]]></given-names>
</name>
<name>
<surname><![CDATA[Rodrigues-Krause]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Elevated levels of extracellular heat-shock protein 72 (eHSP72) are positively correlated with insulin resistance in vivo and cause pancreatic &#946;-cell dysfunction and death in vitro]]></article-title>
<source><![CDATA[Clin Sci (Lond)]]></source>
<year>2014</year>
<volume>126</volume>
<numero>10</numero>
<issue>10</issue>
<page-range>739-52</page-range></nlm-citation>
</ref>
<ref id="B68">
<label>68</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Chung]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Nguyen]]></surname>
<given-names><![CDATA[AK]]></given-names>
</name>
<name>
<surname><![CDATA[Henstridge]]></surname>
<given-names><![CDATA[DC]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[HSP72 protects against obesity-induced insulin resistance]]></article-title>
<source><![CDATA[Proc Natl Acad Sci]]></source>
<year>2008</year>
<volume>105</volume>
<numero>5</numero>
<issue>5</issue>
<page-range>1739-44</page-range></nlm-citation>
</ref>
<ref id="B69">
<label>69</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Rodrigues-Krause]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
<name>
<surname><![CDATA[Krause]]></surname>
<given-names><![CDATA[M]]></given-names>
</name>
<name>
<surname><![CDATA[O&#8217;Hagan]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Divergence of intracellular and extracellular HSP72 in type 2 diabetes: does fat matter?]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2012</year>
<volume>17</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>293-302</page-range></nlm-citation>
</ref>
<ref id="B70">
<label>70</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Pobre]]></surname>
<given-names><![CDATA[KFR]]></given-names>
</name>
<name>
<surname><![CDATA[Poet]]></surname>
<given-names><![CDATA[GJ]]></given-names>
</name>
<name>
<surname><![CDATA[Hendershot]]></surname>
<given-names><![CDATA[LM.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: getting by with a little help from. ERdj friends]]></article-title>
<source><![CDATA[J Biol Chem]]></source>
<year>2019</year>
<volume>294</volume>
<page-range>2098-108</page-range></nlm-citation>
</ref>
<ref id="B71">
<label>71</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Chu]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
<name>
<surname><![CDATA[Chan]]></surname>
<given-names><![CDATA[CM]]></given-names>
</name>
<name>
<surname><![CDATA[Zhang]]></surname>
<given-names><![CDATA[X]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells]]></article-title>
<source><![CDATA[J Biol Chem]]></source>
<year>2018</year>
<volume>293</volume>
<page-range>11709-26</page-range></nlm-citation>
</ref>
<ref id="B72">
<label>72</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Ibrahim]]></surname>
<given-names><![CDATA[IM]]></given-names>
</name>
<name>
<surname><![CDATA[Abdelmalek]]></surname>
<given-names><![CDATA[DH]]></given-names>
</name>
<name>
<surname><![CDATA[Elfiky]]></surname>
<given-names><![CDATA[AA.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[GRP78: A cell&#8217;s response to stress]]></article-title>
<source><![CDATA[Life Sci]]></source>
<year>2019</year>
<page-range>156-63</page-range></nlm-citation>
</ref>
<ref id="B73">
<label>73</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Sabirli]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Koseler]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Goren]]></surname>
<given-names><![CDATA[T]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[High GRP78 levels in Covid-19 infection: A case-control study]]></article-title>
<source><![CDATA[Life Sci]]></source>
<year>2021</year>
<volume>265</volume>
<page-range>118781</page-range></nlm-citation>
</ref>
<ref id="B74">
<label>74</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Ibrahim]]></surname>
<given-names><![CDATA[IM]]></given-names>
</name>
<name>
<surname><![CDATA[Abdelmalek]]></surname>
<given-names><![CDATA[DH]]></given-names>
</name>
<name>
<surname><![CDATA[Elshahat]]></surname>
<given-names><![CDATA[ME]]></given-names>
</name>
<name>
<surname><![CDATA[Elfiky]]></surname>
<given-names><![CDATA[AA.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[COVID-19 spike-host cell receptor GRP78 binding site prediction]]></article-title>
<source><![CDATA[J Infect]]></source>
<year>2020</year>
<volume>80</volume>
<numero>5</numero>
<issue>5</issue>
<page-range>554-62</page-range></nlm-citation>
</ref>
<ref id="B75">
<label>75</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Ha]]></surname>
<given-names><![CDATA[DP]]></given-names>
</name>
<name>
<surname><![CDATA[Van Krieken]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Carlos]]></surname>
<given-names><![CDATA[AJ]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[The stress-inducible molecular chaperone GRP78 as potential therapeutic target for coronavirus infection]]></article-title>
<source><![CDATA[J Infect]]></source>
<year>2020</year>
<volume>81</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>452-82</page-range></nlm-citation>
</ref>
<ref id="B76">
<label>76</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Palmeira]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
<name>
<surname><![CDATA[Sousa]]></surname>
<given-names><![CDATA[E]]></given-names>
</name>
<name>
<surname><![CDATA[Köseler]]></surname>
<given-names><![CDATA[A]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Preliminary virtual screening studies to identify GRP78 inhibitors which may interfere with SARS-CoV-2 infection]]></article-title>
<source><![CDATA[Pharmaceuticals (Basel)]]></source>
<year>2020</year>
<volume>13</volume>
<numero>6</numero>
<issue>6</issue>
<page-range>132</page-range></nlm-citation>
</ref>
<ref id="B77">
<label>77</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Rayner]]></surname>
<given-names><![CDATA[JO]]></given-names>
</name>
<name>
<surname><![CDATA[Roberts]]></surname>
<given-names><![CDATA[RA]]></given-names>
</name>
<name>
<surname><![CDATA[Kim]]></surname>
<given-names><![CDATA[J]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[AR12 (OSU-03012) suppresses GRP78 expression and inhibits SARS-CoV-2 replication]]></article-title>
<source><![CDATA[Biochem Pharmacol]]></source>
<year>2020</year>
<volume>182</volume>
<page-range>114227</page-range></nlm-citation>
</ref>
<ref id="B78">
<label>78</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Chen]]></surname>
<given-names><![CDATA[HW]]></given-names>
</name>
<name>
<surname><![CDATA[Kuo]]></surname>
<given-names><![CDATA[HT]]></given-names>
</name>
<name>
<surname><![CDATA[Wang]]></surname>
<given-names><![CDATA[SJ]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[In vivo heat shock protein assembles with septic liver NF-kappaB/I-kappaB complex regulating NF-kappaB activity]]></article-title>
<source><![CDATA[Shock]]></source>
<year>2005</year>
<volume>24</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>232-8</page-range></nlm-citation>
</ref>
<ref id="B79">
<label>79</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Zheng]]></surname>
<given-names><![CDATA[F]]></given-names>
</name>
<name>
<surname><![CDATA[Liao]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
<name>
<surname><![CDATA[Fan]]></surname>
<given-names><![CDATA[QH]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Clinical characteristics of children with coronavirus disease 2019 in Hubei, China]]></article-title>
<source><![CDATA[Curr Med Sci]]></source>
<year>2020</year>
<volume>40</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>275-80</page-range></nlm-citation>
</ref>
<ref id="B80">
<label>80</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Heck]]></surname>
<given-names><![CDATA[TG]]></given-names>
</name>
<name>
<surname><![CDATA[Scomazzon]]></surname>
<given-names><![CDATA[SP]]></given-names>
</name>
<name>
<surname><![CDATA[Nunes]]></surname>
<given-names><![CDATA[PR]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Acute exercise boosts cell proliferation and the heat shock response in lymphocytes: correlation with cytokine production and extracellular-to-intracellular HSP70 ratio]]></article-title>
<source><![CDATA[Cell Stress Chaperones]]></source>
<year>2017</year>
<volume>22</volume>
<numero>2</numero>
<issue>2</issue>
<page-range>271-91</page-range></nlm-citation>
</ref>
<ref id="B81">
<label>81</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[C]]></given-names>
</name>
<name>
<surname><![CDATA[Chu]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
<name>
<surname><![CDATA[Liu]]></surname>
<given-names><![CDATA[X]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target]]></article-title>
<source><![CDATA[Emerg Microbes Infect]]></source>
<year>2020</year>
<volume>9</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>2663-72</page-range></nlm-citation>
</ref>
<ref id="B82">
<label>82</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Kim]]></surname>
<given-names><![CDATA[JM]]></given-names>
</name>
<name>
<surname><![CDATA[Lee]]></surname>
<given-names><![CDATA[DH]]></given-names>
</name>
<name>
<surname><![CDATA[Kim]]></surname>
<given-names><![CDATA[JS]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[5,7-dihydroxy-3,4,6- trimethoxyflavone inhibits the inflammatory effects induced by Bacteroides fragilis enterotoxin via dissociating the complex of heat shock protein 90 and I kappaB Alpha and I kappaB kinase-gamma in intestinal epithelial cell culture]]></article-title>
<source><![CDATA[Clin Exp Immunol]]></source>
<year>2009</year>
<volume>155</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>541-51</page-range></nlm-citation>
</ref>
<ref id="B83">
<label>83</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Geller]]></surname>
<given-names><![CDATA[R]]></given-names>
</name>
<name>
<surname><![CDATA[Taguwa]]></surname>
<given-names><![CDATA[S]]></given-names>
</name>
<name>
<surname><![CDATA[Frydman]]></surname>
<given-names><![CDATA[J.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Broad action of Hsp90 as a host chaperone required for viral replication]]></article-title>
<source><![CDATA[Biochim Biophys Acta]]></source>
<year>2012</year>
<volume>1823</volume>
<numero>3</numero>
<issue>3</issue>
<page-range>698-706</page-range></nlm-citation>
</ref>
<ref id="B84">
<label>84</label><nlm-citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname><![CDATA[Wan]]></surname>
<given-names><![CDATA[Q]]></given-names>
</name>
<name>
<surname><![CDATA[Song]]></surname>
<given-names><![CDATA[D]]></given-names>
</name>
<name>
<surname><![CDATA[Li]]></surname>
<given-names><![CDATA[H]]></given-names>
</name>
<name>
<surname><![CDATA[He]]></surname>
<given-names><![CDATA[ML.]]></given-names>
</name>
</person-group>
<article-title xml:lang=""><![CDATA[Stress proteins: the biological functions in virus infection, present and challenges for target-based antiviral drug development]]></article-title>
<source><![CDATA[Signal Transduct Target Ther]]></source>
<year>2020</year>
<volume>5</volume>
<numero>1</numero>
<issue>1</issue>
<page-range>125</page-range></nlm-citation>
</ref>
</ref-list>
</back>
</article>
