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 <front>
  <journal-meta>
   <journal-id journal-id-type="publisher-id">Russian Journal of Biological Physics and Chemisrty</journal-id>
   <journal-title-group>
    <journal-title xml:lang="en">Russian Journal of Biological Physics and Chemisrty</journal-title>
    <trans-title-group xml:lang="ru">
     <trans-title>АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ</trans-title>
    </trans-title-group>
   </journal-title-group>
   <issn publication-format="print">2499-9962</issn>
  </journal-meta>
  <article-meta>
   <article-id pub-id-type="publisher-id">54333</article-id>
   <article-categories>
    <subj-group subj-group-type="toc-heading" xml:lang="ru">
     <subject>МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ</subject>
    </subj-group>
    <subj-group subj-group-type="toc-heading" xml:lang="en">
     <subject>MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY</subject>
    </subj-group>
    <subj-group>
     <subject>МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ</subject>
    </subj-group>
   </article-categories>
   <title-group>
    <article-title xml:lang="en">BIOLOGICAL EFFECTS OF POLYSACCHARIDES SIGNALING</article-title>
    <trans-title-group xml:lang="ru">
     <trans-title>БИОЛОГИЧЕСКИЕ ЭФФЕКТЫ СИГНАЛИНГА ПОЛИСАХАРИДОВ</trans-title>
    </trans-title-group>
   </title-group>
   <contrib-group content-type="authors">
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Генералов</surname>
       <given-names>Е А</given-names>
      </name>
      <name xml:lang="en">
       <surname>Generalov</surname>
       <given-names>E A</given-names>
      </name>
     </name-alternatives>
     <email>generals1179@gmail.com</email>
     <xref ref-type="aff" rid="aff-1"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Яковенко</surname>
       <given-names>Л В</given-names>
      </name>
      <name xml:lang="en">
       <surname>Yakovenko</surname>
       <given-names>L V</given-names>
      </name>
     </name-alternatives>
     <email>yakovenko.lv@physics.msu.ru</email>
     <xref ref-type="aff" rid="aff-2"/>
    </contrib>
   </contrib-group>
   <aff-alternatives id="aff-1">
    <aff>
     <institution xml:lang="ru">Институт молекулярной биологии им. В.А. Энгельгардта</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Engelhardt Institute of Molecular Biology, Russian Academy of Sciences</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-2">
    <aff>
     <institution xml:lang="ru">Московский государственный университет имени М.В. Ломоносова</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">M.V. Lomonosov Moscow State University</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <pub-date publication-format="print" date-type="pub" iso-8601-date="2018-09-25T20:22:29+03:00">
    <day>25</day>
    <month>09</month>
    <year>2018</year>
   </pub-date>
   <pub-date publication-format="electronic" date-type="pub" iso-8601-date="2018-09-25T20:22:29+03:00">
    <day>25</day>
    <month>09</month>
    <year>2018</year>
   </pub-date>
   <volume>3</volume>
   <issue>3</issue>
   <fpage>588</fpage>
   <lpage>597</lpage>
   <history>
    <date date-type="received" iso-8601-date="2018-09-20T20:22:29+03:00">
     <day>20</day>
     <month>09</month>
     <year>2018</year>
    </date>
    <date date-type="accepted" iso-8601-date="2018-09-20T20:22:29+03:00">
     <day>20</day>
     <month>09</month>
     <year>2018</year>
    </date>
   </history>
   <self-uri xlink:href="https://rusjbpc.ru/en/nauka/article/54333/view">https://rusjbpc.ru/en/nauka/article/54333/view</self-uri>
   <abstract xml:lang="ru">
    <p>В статье представлен обзор основных полисахаридных рецепторов - SR, CTLR, TLR, CR, NLR, LacCer. Описаны некоторые биологические активности полисахаридов, преимущественно - иммунологические, противоопухолевые, апоптотические, а также некоторые другие. Обсуждается роль рецепторов и моносахаридных последовательностей полисахаридов в регуляции иммунного ответа. Описаны возможные типы сигналинга и роль полисахаридов в нем. Рассмотрена возможность формирования метастабильных состояний клетки, возникающие за счет возникновения разнонаправленных внутриклеточных сигнальных каскадов при взаимодействии рецепторов и комплексных полисахаридных лигандов. Предполагается, что клетка, находящаяся в особом состоянии - бифуркационном, способна «совершать выбор» между различными типами ответов: апоптоз, пролиферация, арест клеточного цикла и другими. Приведены примеры активации различных сигнальных путей под действием полисахаридов, в том числе - возможности перехода трансформированных клеток в бифуркационное состояние.</p>
   </abstract>
   <trans-abstract xml:lang="en">
    <p>This article provides an overview of the main polysaccharide receptors - SR, CTLR, TLR, CR, NLR, LacCer. Some biological activities of polysaccharides, mainly immunological, antitumor, apoptotic, and some others also are described. The role of receptors and monosaccharide sequences of polysaccharides in the regulation of the immune response is discussed. Possible types of signaling and the role of polysaccharides in it are described. The possibility of formation of metastable states of the cell arising due to the appearance of multidirectional intracellular signaling cascades in the interaction of receptors and complex polysaccharide ligands is considered. It is assumed that a cell in a special state - a bifurcation one - is capable of &quot;making a choice&quot; between different types of responses: apoptosis, proliferation, cell cycle arrest, and others. Examples are given, including the possibility of transition of transformed cells into a bifurcation state in response to polysaccharide introduction into cell cultures.</p>
   </trans-abstract>
   <kwd-group xml:lang="ru">
    <kwd>полисахариды</kwd>
    <kwd>гликаны</kwd>
    <kwd>бифуркационное состояние</kwd>
    <kwd>сигналинг</kwd>
    <kwd>рецепторы</kwd>
   </kwd-group>
   <kwd-group xml:lang="en">
    <kwd>polysaccharides</kwd>
    <kwd>glycans</kwd>
    <kwd>bifurcation state</kwd>
    <kwd>signaling</kwd>
    <kwd>receptors</kwd>
   </kwd-group>
  </article-meta>
 </front>
 <body>
  <p></p>
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 <back>
  <ref-list>
   <ref id="B1">
    <label>1.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Lowe J.B. Glycan-dependent leukocyte adhesion and recruitment in inflammation. Curr Opin Cell Biol., 2003, vol. 15, no. 5, pp. 531-538.</mixed-citation>
     <mixed-citation xml:lang="en">Lowe J.B. Glycan-dependent leukocyte adhesion and recruitment in inflammation. Curr Opin Cell Biol., 2003, vol. 15, no. 5, pp. 531-538.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B2">
    <label>2.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Lowe J.B., Marth J.D. A genetic approach to mammalian glycan function. Annu. Rev. Biochem., 2003. vol. 72, pp. 673-691.</mixed-citation>
     <mixed-citation xml:lang="en">Lowe J.B., Marth J.D. A genetic approach to mammalian glycan function. Annu. Rev. Biochem., 2003. vol. 72, pp. 673-691.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B3">
    <label>3.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Ohtsubo K., Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell, 2006, vol. 126, no. 5, pp. 855-867.</mixed-citation>
     <mixed-citation xml:lang="en">Ohtsubo K., Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell, 2006, vol. 126, no. 5, pp. 855-867.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B4">
    <label>4.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Geier H., Celli J. Phagocytic receptors dictate phagosomal escape and intracellular proliferation of Francisella tularensis. Infect. Immun., 2011, vol. 79, no. 6, pp. 2204-2214.</mixed-citation>
     <mixed-citation xml:lang="en">Geier H., Celli J. Phagocytic receptors dictate phagosomal escape and intracellular proliferation of Francisella tularensis. Infect. Immun., 2011, vol. 79, no. 6, pp. 2204-2214.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B5">
    <label>5.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Li J., Lee D.S., Madrenas J. Evolving bacterial envelopes and plasticity of TLR2-dependent responses: basic research and translational opportunities. Frontiers in Immunology, 2013, vol. 4, pp. 347.</mixed-citation>
     <mixed-citation xml:lang="en">Li J., Lee D.S., Madrenas J. Evolving bacterial envelopes and plasticity of TLR2-dependent responses: basic research and translational opportunities. Frontiers in Immunology, 2013, vol. 4, pp. 347.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B6">
    <label>6.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Marakalala M.J., Williams D.L., Hoving J.C. [et al.] Dectin-1 plays a redundant role in the immunomodulatory activities of β-glucan-rich ligands in vivo. Microbes Infect., 2013, vol. 15, pp. 511-515.</mixed-citation>
     <mixed-citation xml:lang="en">Marakalala M.J., Williams D.L., Hoving J.C. [et al.] Dectin-1 plays a redundant role in the immunomodulatory activities of β-glucan-rich ligands in vivo. Microbes Infect., 2013, vol. 15, pp. 511-515.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B7">
    <label>7.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Taghavi M., Mortaz E., Khosravi A. [et al.] Zymosan attenuates melanoma growth progression, increases splenocyte proliferation and induces TLR-2/4 and TNF-α expression in mice. J. Inflamm., 2018, vol. 15, no. 5, pp. 1-10, e-pub.</mixed-citation>
     <mixed-citation xml:lang="en">Taghavi M., Mortaz E., Khosravi A. [et al.] Zymosan attenuates melanoma growth progression, increases splenocyte proliferation and induces TLR-2/4 and TNF-α expression in mice. J. Inflamm., 2018, vol. 15, no. 5, pp. 1-10, e-pub.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B8">
    <label>8.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Dillon S., Agrawal S., Banerjee K. Yeast zymosan, a stimulus for TLR2 and dectin-1, induces regulatory antigen-presenting cells and immunological tolerance. J. Clin. Invest., 2006, vol. 116, no. 4, pp. 916-928.</mixed-citation>
     <mixed-citation xml:lang="en">Dillon S., Agrawal S., Banerjee K. Yeast zymosan, a stimulus for TLR2 and dectin-1, induces regulatory antigen-presenting cells and immunological tolerance. J. Clin. Invest., 2006, vol. 116, no. 4, pp. 916-928.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B9">
    <label>9.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Sakashita Y., Hiyama E., Imamura Y. [et al.] Generation of pro-inflammatory and anti-inflammatory cytokines in the gut zymosan-induced peritonitis. Hiroshima J. Med. Sci., 2000, vol. 49, no. 1, pp. 43-48.</mixed-citation>
     <mixed-citation xml:lang="en">Sakashita Y., Hiyama E., Imamura Y. [et al.] Generation of pro-inflammatory and anti-inflammatory cytokines in the gut zymosan-induced peritonitis. Hiroshima J. Med. Sci., 2000, vol. 49, no. 1, pp. 43-48.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B10">
    <label>10.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Chan G.C.-F., Chan W.K., Sze D.M.-Y. The effects of β-glucans on human immune and cancer cells. J. of hem. and onc., 2009, vol. 2, p. 25.</mixed-citation>
     <mixed-citation xml:lang="en">Chan G.C.-F., Chan W.K., Sze D.M.-Y. The effects of β-glucans on human immune and cancer cells. J. of hem. and onc., 2009, vol. 2, p. 25.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B11">
    <label>11.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Toussi D.N., Massari P. Immune adjuvant effect of molecularly-defined Toll-Like receptor ligands. Vaccines, 2014, vol. 2, no. 2, pp. 323-353.</mixed-citation>
     <mixed-citation xml:lang="en">Toussi D.N., Massari P. Immune adjuvant effect of molecularly-defined Toll-Like receptor ligands. Vaccines, 2014, vol. 2, no. 2, pp. 323-353.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B12">
    <label>12.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Kawai T., Akira S. Role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol., 2010, vol. 11, no. 5, pp. 373-384.</mixed-citation>
     <mixed-citation xml:lang="en">Kawai T., Akira S. Role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol., 2010, vol. 11, no. 5, pp. 373-384.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B13">
    <label>13.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Lester S.N., Li K. Toll-like receptors in antiviral innate immunity. J. Mol. Biol., 2014, vol. 426, no. 6, pp. 1246-1264.</mixed-citation>
     <mixed-citation xml:lang="en">Lester S.N., Li K. Toll-like receptors in antiviral innate immunity. J. Mol. Biol., 2014, vol. 426, no. 6, pp. 1246-1264.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B14">
    <label>14.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Li X., Jiang S., Tapping R.I. Toll-like receptor signaling in cell proliferation and survival. Cytokine, 2010, vol. 49, no. 1, pp. 1-9, epub.</mixed-citation>
     <mixed-citation xml:lang="en">Li X., Jiang S., Tapping R.I. Toll-like receptor signaling in cell proliferation and survival. Cytokine, 2010, vol. 49, no. 1, pp. 1-9, epub.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B15">
    <label>15.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Oliveira-Nascimento L., Massari P., Wetzler L.M. The Role of TLR2 in Infection and Immunity. Front. Immunol., 2012, vol. 3, no. 79, pp. 1-17. Epub.</mixed-citation>
     <mixed-citation xml:lang="en">Oliveira-Nascimento L., Massari P., Wetzler L.M. The Role of TLR2 in Infection and Immunity. Front. Immunol., 2012, vol. 3, no. 79, pp. 1-17. Epub.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B16">
    <label>16.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Buwitt-Beckmann U., Heine H., Wiesmuller K.H. [et al.] Toll-like receptor 6-independent signaling by diacylated lipopeptides. Eur. J. Immunol., 2005, vol. 35, pp. 282-289.</mixed-citation>
     <mixed-citation xml:lang="en">Buwitt-Beckmann U., Heine H., Wiesmuller K.H. [et al.] Toll-like receptor 6-independent signaling by diacylated lipopeptides. Eur. J. Immunol., 2005, vol. 35, pp. 282-289.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B17">
    <label>17.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Frodermann V., Chau T.A., Sayedyahossein S. [et al.] A modulatory interleukin-10 response to staphylococcal peptidoglycan prevents Th1/Th17 adaptive immunity to Staphylococcus aureus. J. Infect. Dis., 2011, vol. 204, pp. 253-262.</mixed-citation>
     <mixed-citation xml:lang="en">Frodermann V., Chau T.A., Sayedyahossein S. [et al.] A modulatory interleukin-10 response to staphylococcal peptidoglycan prevents Th1/Th17 adaptive immunity to Staphylococcus aureus. J. Infect. Dis., 2011, vol. 204, pp. 253-262.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B18">
    <label>18.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Bulut Y., Faure E., Thomas L. [et al.] Cooperation of Toll-like receptor 2 and 6 for cellular activation by soluble tuberculosis factor and Borrelia burgdorferi outer surface protein A lipoprotein: role of Toll-interacting protein and IL-1 receptor signaling molecules in Toll-like receptor 2 signaling. J. Immunol., 2001, vol. 167, no. 2, pp. 987-994.</mixed-citation>
     <mixed-citation xml:lang="en">Bulut Y., Faure E., Thomas L. [et al.] Cooperation of Toll-like receptor 2 and 6 for cellular activation by soluble tuberculosis factor and Borrelia burgdorferi outer surface protein A lipoprotein: role of Toll-interacting protein and IL-1 receptor signaling molecules in Toll-like receptor 2 signaling. J. Immunol., 2001, vol. 167, no. 2, pp. 987-994.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B19">
    <label>19.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Brown J., Wang H., Hajishengallis G.N., Martin M. TLR-signaling networks an integration of adaptor molecules, kinases, and cross-talk. J. Dent. Res., 2011, vol. 90, no. 4. pp. 417-427.</mixed-citation>
     <mixed-citation xml:lang="en">Brown J., Wang H., Hajishengallis G.N., Martin M. TLR-signaling networks an integration of adaptor molecules, kinases, and cross-talk. J. Dent. Res., 2011, vol. 90, no. 4. pp. 417-427.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B20">
    <label>20.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Chau T.A., McCully M.L., Brintnell W. [et al.] Toll-like receptor 2 ligands on the staphylococcal cell wall downregulate superantigen induced T cell activation and prevent toxic shock syndrome. Nat. Med., 2009, vol. 15, pp. 641-648.</mixed-citation>
     <mixed-citation xml:lang="en">Chau T.A., McCully M.L., Brintnell W. [et al.] Toll-like receptor 2 ligands on the staphylococcal cell wall downregulate superantigen induced T cell activation and prevent toxic shock syndrome. Nat. Med., 2009, vol. 15, pp. 641-648.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B21">
    <label>21.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Depaolo R.W., Tang F., Kim I. [et al.] Toll-like receptor 6 drives differentiation of tolerogenic dendritic cells and contributes to LcrV mediated plague pathogenesis. Cell host microbe, 2008, vol. 4, pp. 350-361.</mixed-citation>
     <mixed-citation xml:lang="en">Depaolo R.W., Tang F., Kim I. [et al.] Toll-like receptor 6 drives differentiation of tolerogenic dendritic cells and contributes to LcrV mediated plague pathogenesis. Cell host microbe, 2008, vol. 4, pp. 350-361.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B22">
    <label>22.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Uematsu S., Akira S. Toll-like receptors (TLRs) and their Ligands. Handb. Exp. Pharmacol., 2008, vol. 183, pp. 1-20.</mixed-citation>
     <mixed-citation xml:lang="en">Uematsu S., Akira S. Toll-like receptors (TLRs) and their Ligands. Handb. Exp. Pharmacol., 2008, vol. 183, pp. 1-20.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B23">
    <label>23.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Tatematsu M., Yoshida R., Morioka Y. [et al.] Raftlin controls lipopolysaccharide-induced TLR4 internalization and TICAM-1 signaling in a cell type-specific manner. J. Immunol., 2016, vol. 196, no. 9, pp. 3865-3876.</mixed-citation>
     <mixed-citation xml:lang="en">Tatematsu M., Yoshida R., Morioka Y. [et al.] Raftlin controls lipopolysaccharide-induced TLR4 internalization and TICAM-1 signaling in a cell type-specific manner. J. Immunol., 2016, vol. 196, no. 9, pp. 3865-3876.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B24">
    <label>24.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Zhou X.-L., Yang M., Xue B.-G. [et al.] Anti-inflammatory action of Ginkgo Biloba leaf polysaccharide via TLR4/NF-κb signaling suppression. Biomedical research, 2014, vol. 25, no. 4, pp. 449-454.</mixed-citation>
     <mixed-citation xml:lang="en">Zhou X.-L., Yang M., Xue B.-G. [et al.] Anti-inflammatory action of Ginkgo Biloba leaf polysaccharide via TLR4/NF-κb signaling suppression. Biomedical research, 2014, vol. 25, no. 4, pp. 449-454.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B25">
    <label>25.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Rajaiah R., Perkins D.J., Ireland D.D.C., Vogela S.N. Immunology and inflammation CD14 dependence of TLR4 endocytosis and TRIF signaling displays ligand specificity and is dissociable in endotoxin tolerance. Proc. Natl. Acad. Sci. USA, 2015, vol. 112, no. 27, pp. 8391-8396.</mixed-citation>
     <mixed-citation xml:lang="en">Rajaiah R., Perkins D.J., Ireland D.D.C., Vogela S.N. Immunology and inflammation CD14 dependence of TLR4 endocytosis and TRIF signaling displays ligand specificity and is dissociable in endotoxin tolerance. Proc. Natl. Acad. Sci. USA, 2015, vol. 112, no. 27, pp. 8391-8396.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B26">
    <label>26.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Zhang S., Nie S., Huang D., Huang J. [et al.] Polysaccharide from Ganoderma atrum evokes antitumor activity via Toll-like receptor 4-mediated NF-κB and mitogen-activated protein kinase signaling pathways. J. Agric. Food chem., 2013, vol. 61, no. 15, pp. 3676-3682.</mixed-citation>
     <mixed-citation xml:lang="en">Zhang S., Nie S., Huang D., Huang J. [et al.] Polysaccharide from Ganoderma atrum evokes antitumor activity via Toll-like receptor 4-mediated NF-κB and mitogen-activated protein kinase signaling pathways. J. Agric. Food chem., 2013, vol. 61, no. 15, pp. 3676-3682.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B27">
    <label>27.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Yu Q., Nie S.-P., Wang J.-Q. [et al.] Signaling pathway involved in the immunomodulatory effect of Ganoderma atrum polysaccharide in spleen lymphocytes. J. Agric. Food chem., 2015, vol. 63, no. 10, pp. 2734-2740.</mixed-citation>
     <mixed-citation xml:lang="en">Yu Q., Nie S.-P., Wang J.-Q. [et al.] Signaling pathway involved in the immunomodulatory effect of Ganoderma atrum polysaccharide in spleen lymphocytes. J. Agric. Food chem., 2015, vol. 63, no. 10, pp. 2734-2740.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B28">
    <label>28.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Kumar H., Kawai T., Akira S. Pathogen recognition be the innate immune system. Int. Rev. Immunol., 2011, vol. 30, pp. 16-34.</mixed-citation>
     <mixed-citation xml:lang="en">Kumar H., Kawai T., Akira S. Pathogen recognition be the innate immune system. Int. Rev. Immunol., 2011, vol. 30, pp. 16-34.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B29">
    <label>29.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Rubino S.J., Selvanantham T., Girardin S.E., Philpott D.J. NOD-like receptors in the control of intestinal inflammation. Curr. Opin. Immunol., 2012, vol. 24, pp. 398-404.</mixed-citation>
     <mixed-citation xml:lang="en">Rubino S.J., Selvanantham T., Girardin S.E., Philpott D.J. NOD-like receptors in the control of intestinal inflammation. Curr. Opin. Immunol., 2012, vol. 24, pp. 398-404.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B30">
    <label>30.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Schneider M., Zimmermann A.G., Roberts R.A. [et al.] The innate immune sensor NLRC3 attenuates Toll-like receptor signaling via modification of the signaling adaptor TRAF6 and transcription factor NF-κB. Nat. Immunol., 2006, vol. 6, pp. 9-20.</mixed-citation>
     <mixed-citation xml:lang="en">Schneider M., Zimmermann A.G., Roberts R.A. [et al.] The innate immune sensor NLRC3 attenuates Toll-like receptor signaling via modification of the signaling adaptor TRAF6 and transcription factor NF-κB. Nat. Immunol., 2006, vol. 6, pp. 9-20.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B31">
    <label>31.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Selvanantham T., Escalante N.K., Cruz Tleugabulova M. [et al.] NOD1 and NOD2 enhance TLR-mediated invariant NKT cell activation during bacterial infection. The Journal of immunology, 2013, vol. 191, no. 11, pp. 5646-5654.</mixed-citation>
     <mixed-citation xml:lang="en">Selvanantham T., Escalante N.K., Cruz Tleugabulova M. [et al.] NOD1 and NOD2 enhance TLR-mediated invariant NKT cell activation during bacterial infection. The Journal of immunology, 2013, vol. 191, no. 11, pp. 5646-5654.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B32">
    <label>32.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Franchi L., Warner N., Viani K., Nuñez G. Function of Nod-like receptors in microbial recognition and host defense. Immunol. Rev., 2009, vol. 227, no. 1, pp. 106-128.</mixed-citation>
     <mixed-citation xml:lang="en">Franchi L., Warner N., Viani K., Nuñez G. Function of Nod-like receptors in microbial recognition and host defense. Immunol. Rev., 2009, vol. 227, no. 1, pp. 106-128.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B33">
    <label>33.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Juárez E., Carranza C., Hernández-Sánchez F. [et al.] Nucleotide-oligomerizing domain-1 (NOD1) receptor activation induces pro-inflammatory responses and autophagy in human alveolar macrophages. BMC Pulm. Med., 2014, vol. 14, no. 152. pp. 1-11, epub.</mixed-citation>
     <mixed-citation xml:lang="en">Juárez E., Carranza C., Hernández-Sánchez F. [et al.] Nucleotide-oligomerizing domain-1 (NOD1) receptor activation induces pro-inflammatory responses and autophagy in human alveolar macrophages. BMC Pulm. Med., 2014, vol. 14, no. 152. pp. 1-11, epub.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B34">
    <label>34.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Tian Z., Liu L., Yang B. Astagalus polysaccharide attenuates murine colitis through inhibiton of the NLRP3 inflammasome. Planta medica, 2016, vol. 83, no. 1, pp. 70-77.</mixed-citation>
     <mixed-citation xml:lang="en">Tian Z., Liu L., Yang B. Astagalus polysaccharide attenuates murine colitis through inhibiton of the NLRP3 inflammasome. Planta medica, 2016, vol. 83, no. 1, pp. 70-77.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B35">
    <label>35.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Iwabuchi K., Nakayama H., Oizumi A. [et al.] Role of Ceramide from glycosphingolipids and its metabolites in immunological and inflammatory responses in humans (Review). Mediators of Inflammation, 2015, vol. 2015, pp. 1-10.</mixed-citation>
     <mixed-citation xml:lang="en">Iwabuchi K., Nakayama H., Oizumi A. [et al.] Role of Ceramide from glycosphingolipids and its metabolites in immunological and inflammatory responses in humans (Review). Mediators of Inflammation, 2015, vol. 2015, pp. 1-10.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B36">
    <label>36.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Evans S.E., Hahn P.Y., McCann F. [et al.] Pneumocystis cell wall β-glucans stimulate alveolar epithelial cell chemokine generation through nuclear factor-κB-dependent mechanisms. Am. J. Respir. Cell Mol. Biol., 2005, vol. 32, no. 6, pp. 490-497.</mixed-citation>
     <mixed-citation xml:lang="en">Evans S.E., Hahn P.Y., McCann F. [et al.] Pneumocystis cell wall β-glucans stimulate alveolar epithelial cell chemokine generation through nuclear factor-κB-dependent mechanisms. Am. J. Respir. Cell Mol. Biol., 2005, vol. 32, no. 6, pp. 490-497.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B37">
    <label>37.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Iwabuchi K., Nagaoka I. Lactosylceramide-enriched glycosphingolipid signaling domain mediates superoxide generation from human neutrophils. Blood, 2002, vol. 100, pp. 1454-1464.</mixed-citation>
     <mixed-citation xml:lang="en">Iwabuchi K., Nagaoka I. Lactosylceramide-enriched glycosphingolipid signaling domain mediates superoxide generation from human neutrophils. Blood, 2002, vol. 100, pp. 1454-1464.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B38">
    <label>38.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Akramiene D., Kondrotas A., Didziapetriene J., Kevelaitis E. Effects of β-glucans on the immune system. Medicina (Kaunas), 2007, vol. 43, pp. 597-606.</mixed-citation>
     <mixed-citation xml:lang="en">Akramiene D., Kondrotas A., Didziapetriene J., Kevelaitis E. Effects of β-glucans on the immune system. Medicina (Kaunas), 2007, vol. 43, pp. 597-606.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B39">
    <label>39.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Legentil L., Paris F., Ballet C. [et al.] Molecular interactions of β-(1→3)-glucans with their receptors. Molecules, 2015, vol. 20, pp. 9745-9766.</mixed-citation>
     <mixed-citation xml:lang="en">Legentil L., Paris F., Ballet C. [et al.] Molecular interactions of β-(1→3)-glucans with their receptors. Molecules, 2015, vol. 20, pp. 9745-9766.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B40">
    <label>40.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Popa V. Polysaccharides in Medicinal and Pharmaceutical Applications. Smithers Rapra, 2011, 408 p.</mixed-citation>
     <mixed-citation xml:lang="en">Popa V. Polysaccharides in Medicinal and Pharmaceutical Applications. Smithers Rapra, 2011, 408 p.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B41">
    <label>41.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Nakayama H., Kurihara H., Morita Y.S. [et al.] Lipoarabinomannan binding to lactosylceramide in lipid rafts is essential for the phagocytosis of mycobacteria by human neutrophils. Sci. Signal, 2016, vol. 9, ra101, pp. 1-15.</mixed-citation>
     <mixed-citation xml:lang="en">Nakayama H., Kurihara H., Morita Y.S. [et al.] Lipoarabinomannan binding to lactosylceramide in lipid rafts is essential for the phagocytosis of mycobacteria by human neutrophils. Sci. Signal, 2016, vol. 9, ra101, pp. 1-15.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B42">
    <label>42.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Rice P.J., Kelley J.L., Kogan G. [et al.] Human monocyte scavenger receptors are pattern recognition receptors for (1→3)-β-d-glucans. J. Leukoc. Biol., 2002, vol. 72, pp. 140-146.</mixed-citation>
     <mixed-citation xml:lang="en">Rice P.J., Kelley J.L., Kogan G. [et al.] Human monocyte scavenger receptors are pattern recognition receptors for (1→3)-β-d-glucans. J. Leukoc. Biol., 2002, vol. 72, pp. 140-146.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B43">
    <label>43.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Yu H., Ha T., Liu L. [et al.] Scavenger receptor A (SR-A) is required for LPS-induced TLR4 mediated NF-κB activation in macrophages. Biochim. Biophys. Acta, 2012, vol. 1823, no. 7, pp. 1192-1198.</mixed-citation>
     <mixed-citation xml:lang="en">Yu H., Ha T., Liu L. [et al.] Scavenger receptor A (SR-A) is required for LPS-induced TLR4 mediated NF-κB activation in macrophages. Biochim. Biophys. Acta, 2012, vol. 1823, no. 7, pp. 1192-1198.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B44">
    <label>44.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Větvička V., Novák M. Biology and chemistry of beta glucan: beta glucans - mechanisms of action. Bentham science publishers, 2011, 83 p.</mixed-citation>
     <mixed-citation xml:lang="en">Větvička V., Novák M. Biology and chemistry of beta glucan: beta glucans - mechanisms of action. Bentham science publishers, 2011, 83 p.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B45">
    <label>45.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Li B., Allendorf D.J., Hansen R. [et al.] Yeast beta-glucan amplifies phagocyte killing of iC3b-opsonized tumor cells via complement receptor 3-Syk-phosphatidylinositol 3-kinase pathway. J. Immunol, 2006, vol. 177, no. 3, pp. 1661-1669.</mixed-citation>
     <mixed-citation xml:lang="en">Li B., Allendorf D.J., Hansen R. [et al.] Yeast beta-glucan amplifies phagocyte killing of iC3b-opsonized tumor cells via complement receptor 3-Syk-phosphatidylinositol 3-kinase pathway. J. Immunol, 2006, vol. 177, no. 3, pp. 1661-1669.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B46">
    <label>46.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Yan J., Allendorf D.J., Li B. [et al.] The role of membrane complement regulatory proteins in cancer immunotherapy. Advances in experimental medicine and biology, 2008, vol. 8, no. 3, pp. 218-225.</mixed-citation>
     <mixed-citation xml:lang="en">Yan J., Allendorf D.J., Li B. [et al.] The role of membrane complement regulatory proteins in cancer immunotherapy. Advances in experimental medicine and biology, 2008, vol. 8, no. 3, pp. 218-225.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B47">
    <label>47.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hong F., Yan J., Baran T.J. [et al.] Mechanism by which orally administered β-1,3-glucans enhance the tumoricidal activity of antitumor monoclonal antibodies in murine tumor models. The journal of immunology, 2004, vol. 173, pp. 797-806.</mixed-citation>
     <mixed-citation xml:lang="en">Hong F., Yan J., Baran T.J. [et al.] Mechanism by which orally administered β-1,3-glucans enhance the tumoricidal activity of antitumor monoclonal antibodies in murine tumor models. The journal of immunology, 2004, vol. 173, pp. 797-806.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B48">
    <label>48.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Zelensky A.N., Gready J.E. The C-type lectin like domain superfamily. The FEBS J., 2005, vol. 272, pp. 6179-6217.</mixed-citation>
     <mixed-citation xml:lang="en">Zelensky A.N., Gready J.E. The C-type lectin like domain superfamily. The FEBS J., 2005, vol. 272, pp. 6179-6217.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B49">
    <label>49.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Sancho D., Reise e Sousa C. Signaling by myeloid C-type lectin receptors in immunity and homeostasis. Ann. Rev. Immunol., 2012, vol. 30, pp. 491-529.</mixed-citation>
     <mixed-citation xml:lang="en">Sancho D., Reise e Sousa C. Signaling by myeloid C-type lectin receptors in immunity and homeostasis. Ann. Rev. Immunol., 2012, vol. 30, pp. 491-529.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B50">
    <label>50.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hong W.-P.P., Nguyen S., Young S. [et al.] Identification of the Optimal DC-SIGN Binding Site on Human Immunodeficiency Virus Type 1 gp120. J. Virol., 2007, vol. 81, no. 15, pp. 8325-8336.</mixed-citation>
     <mixed-citation xml:lang="en">Hong W.-P.P., Nguyen S., Young S. [et al.] Identification of the Optimal DC-SIGN Binding Site on Human Immunodeficiency Virus Type 1 gp120. J. Virol., 2007, vol. 81, no. 15, pp. 8325-8336.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B51">
    <label>51.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hollmig S.T., Ariizumi K., Cruz D.P. Recognition of non-self-polysaccharides by C-type lectin receptors dectin-1 and dectin-2 Jr. Glycobiology, 2009, vol. 19, no. 6, pp. 568-575.</mixed-citation>
     <mixed-citation xml:lang="en">Hollmig S.T., Ariizumi K., Cruz D.P. Recognition of non-self-polysaccharides by C-type lectin receptors dectin-1 and dectin-2 Jr. Glycobiology, 2009, vol. 19, no. 6, pp. 568-575.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B52">
    <label>52.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Ruiz-Herrera J. Dimorphic fungi: their importance as models for differentiation and fungal pathogenesis. Bentham Science Publishers, 2012, 150 p.</mixed-citation>
     <mixed-citation xml:lang="en">Ruiz-Herrera J. Dimorphic fungi: their importance as models for differentiation and fungal pathogenesis. Bentham Science Publishers, 2012, 150 p.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B53">
    <label>53.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">van den Berg L.M., Zijlstra-Willems E.M., Richters C.D. [et al.] Dectin-1 activation induces proliferation and migration of human keratinocytes enhancing wound re-epithelization. Cellular immunology, 2014, vol. 289, pp. 49-54.</mixed-citation>
     <mixed-citation xml:lang="en">van den Berg L.M., Zijlstra-Willems E.M., Richters C.D. [et al.] Dectin-1 activation induces proliferation and migration of human keratinocytes enhancing wound re-epithelization. Cellular immunology, 2014, vol. 289, pp. 49-54.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B54">
    <label>54.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Brown G.D. Dectin-1: A signaling non-TLR pattern-recognition receptor. Nat. Rev. Immunol., 2006, vol. 6, pp. 33-44.</mixed-citation>
     <mixed-citation xml:lang="en">Brown G.D. Dectin-1: A signaling non-TLR pattern-recognition receptor. Nat. Rev. Immunol., 2006, vol. 6, pp. 33-44.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B55">
    <label>55.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Huysamen C., Brown G.D. The fungal pattern-recognition receptor, Dectin-1, and the associated cluster of C-type lectin like receptors. FEMS Microbiol. Lett., 2009, vol. 290, pp. 121-128.</mixed-citation>
     <mixed-citation xml:lang="en">Huysamen C., Brown G.D. The fungal pattern-recognition receptor, Dectin-1, and the associated cluster of C-type lectin like receptors. FEMS Microbiol. Lett., 2009, vol. 290, pp. 121-128.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B56">
    <label>56.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Kimberg M., Brown G.D. Dectin-1 and its role in antifungal immunity. Medical mycology, 2008, vol. 46, no. 7, pp. 631-636.</mixed-citation>
     <mixed-citation xml:lang="en">Kimberg M., Brown G.D. Dectin-1 and its role in antifungal immunity. Medical mycology, 2008, vol. 46, no. 7, pp. 631-636.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B57">
    <label>57.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Kerrigan A.M., Brown G.D. Syk-coupled C-type lectins in immunity. Trends immunol., 2011, vol. 32, pp. 151-156.</mixed-citation>
     <mixed-citation xml:lang="en">Kerrigan A.M., Brown G.D. Syk-coupled C-type lectins in immunity. Trends immunol., 2011, vol. 32, pp. 151-156.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B58">
    <label>58.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Chen H., Cai H., Chen L. [et al.] H. N-glycan-defective breast cancer cells induce a phenotypic switch in polarization of bone marrow-derived macrophages. Clin. Invest. Med., 2011, vol. 34, no. 2, pp. 71-81.</mixed-citation>
     <mixed-citation xml:lang="en">Chen H., Cai H., Chen L. [et al.] H. N-glycan-defective breast cancer cells induce a phenotypic switch in polarization of bone marrow-derived macrophages. Clin. Invest. Med., 2011, vol. 34, no. 2, pp. 71-81.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B59">
    <label>59.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hardison S.E., Brown G.D. C-type lectin orchestrate antifungal immunity. Nat. immunol., 2012, vol. 13, pp. 817-822.</mixed-citation>
     <mixed-citation xml:lang="en">Hardison S.E., Brown G.D. C-type lectin orchestrate antifungal immunity. Nat. immunol., 2012, vol. 13, pp. 817-822.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B60">
    <label>60.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Dennehy K.M., Ferwerda G., Faro-Trindade I. [et al.] Syk kinase is required for collaborative cytokine production induced through Dectin-1 and Toll-like receptors. Eur. J. Immunol., 2008, vol. 38, no. 2, pp. 500-506.</mixed-citation>
     <mixed-citation xml:lang="en">Dennehy K.M., Ferwerda G., Faro-Trindade I. [et al.] Syk kinase is required for collaborative cytokine production induced through Dectin-1 and Toll-like receptors. Eur. J. Immunol., 2008, vol. 38, no. 2, pp. 500-506.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B61">
    <label>61.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Reid D.M., Gow A.R.N., Brown G.D. Pattern recognition: recent insights from Dectin-1. Curr. Opin. Immunol., 2009, vol. 21, no. 1, pp. 30-37.</mixed-citation>
     <mixed-citation xml:lang="en">Reid D.M., Gow A.R.N., Brown G.D. Pattern recognition: recent insights from Dectin-1. Curr. Opin. Immunol., 2009, vol. 21, no. 1, pp. 30-37.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B62">
    <label>62.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Kerscher B., Willment J.A., Brown G.D. The Dectin-2 family of C-type lectin-like receptors: an update. Int. Immunol., 2013, vol. 25, no. 5, pp. 271-277.</mixed-citation>
     <mixed-citation xml:lang="en">Kerscher B., Willment J.A., Brown G.D. The Dectin-2 family of C-type lectin-like receptors: an update. Int. Immunol., 2013, vol. 25, no. 5, pp. 271-277.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B63">
    <label>63.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Lambert A.A., Gilbert C., Richard M. [et al.] The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans- and cis-infection pathways. Blood, 2008, vol. 112, no. 4, pp. 1299-1307.</mixed-citation>
     <mixed-citation xml:lang="en">Lambert A.A., Gilbert C., Richard M. [et al.] The C-type lectin surface receptor DCIR acts as a new attachment factor for HIV-1 in dendritic cells and contributes to trans- and cis-infection pathways. Blood, 2008, vol. 112, no. 4, pp. 1299-1307.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B64">
    <label>64.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Laura A.A., Luke Y.P., Krasimira T.-A. Bifurcation analysis of a two-compartment hippocampal pyramidal cell model. J. Comput. Neurosci., 2016, vol. 41, pp. 91-106.</mixed-citation>
     <mixed-citation xml:lang="en">Laura A.A., Luke Y.P., Krasimira T.-A. Bifurcation analysis of a two-compartment hippocampal pyramidal cell model. J. Comput. Neurosci., 2016, vol. 41, pp. 91-106.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B65">
    <label>65.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Otte S., Berg S., Luther S., Parlitz U. Bifurcations, chaos, and sensitivity to parameter variations in the Sato cardiac cell model Author links open overlay panel. Communications in nonlinear science and numerical simulation, 2016, vol. 37, pp. 265-281.</mixed-citation>
     <mixed-citation xml:lang="en">Otte S., Berg S., Luther S., Parlitz U. Bifurcations, chaos, and sensitivity to parameter variations in the Sato cardiac cell model Author links open overlay panel. Communications in nonlinear science and numerical simulation, 2016, vol. 37, pp. 265-281.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B66">
    <label>66.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Generalov E.A., Levashova N.T., Sidorova A.E. [et al.] An autowave model of the bifurcation behavior of transformed cells in response to polysaccharide. Biophysics, 2017, vol. 62, no. 5, pp. 717-721.</mixed-citation>
     <mixed-citation xml:lang="en">Generalov E.A., Levashova N.T., Sidorova A.E. [et al.] An autowave model of the bifurcation behavior of transformed cells in response to polysaccharide. Biophysics, 2017, vol. 62, no. 5, pp. 717-721.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B67">
    <label>67.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Stephen T.L., Groneck L., Kalka-Moll W.M. The modulation of adaptive immune responses by bacterial zwitterionic polysaccharides. International journal of microbiology, 2010, vol. 2010, pp. 1-12, epub.</mixed-citation>
     <mixed-citation xml:lang="en">Stephen T.L., Groneck L., Kalka-Moll W.M. The modulation of adaptive immune responses by bacterial zwitterionic polysaccharides. International journal of microbiology, 2010, vol. 2010, pp. 1-12, epub.</mixed-citation>
    </citation-alternatives>
   </ref>
  </ref-list>
 </back>
</article>
