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<article article-type="research-article" dtd-version="1.3" 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" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">fcmedicine</journal-id><journal-title-group><journal-title xml:lang="ru">Фундаментальная и клиническая медицина</journal-title><trans-title-group xml:lang="en"><trans-title>Fundamental and Clinical Medicine</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2500-0764</issn><issn pub-type="epub">2542-0941</issn><publisher><publisher-name>КемГМУ</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.23946/2500-0764-2020-5-2-112-118</article-id><article-id custom-type="elpub" pub-id-type="custom">fcmedicine-270</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ОБЗОРНЫЕ СТАТЬИ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>REVIEW ARTICLES</subject></subj-group></article-categories><title-group><article-title>Перспективы использования сиалированных иммуноглобулинов в терапии различных заболеваний</article-title><trans-title-group xml:lang="en"><trans-title>Prospects for the use of sialylated immunoglobulins in the treatment of different diseases</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-3781-6340</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Маркина</surname><given-names>Ю. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Markina</surname><given-names>Yu. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Маркина Юлия Владимировна - кандидат медицинских наук, научный сотрудник лаборатории инфекционной патологии и молекулярной микроэкологии.</p><p>117418, Россия, Москва, ул. Цюрупы, д. 3</p></bio><bio xml:lang="en"><p>Dr. Yulia V. Markina - MD, PhD, Research Fellow, Laboratory of Infectious Pathology and Molecular Microecology.</p><p>3, Tsyurupy Street, 117418, Moscow, Russian Federation</p></bio><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-6649-7924</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Маркин</surname><given-names>А. М.</given-names></name><name name-style="western" xml:lang="en"><surname>Markin</surname><given-names>A. M.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Маркин Александр Михайлович - кандидат медицинских наук, научный сотрудник лаборатории инфекционной патологии и молекулярной микроэкологии.</p><p>117418, Россия, Москва, ул. Цюрупы, д. 3</p></bio><bio xml:lang="en"><p>Dr. Alexander M. Markin - MD, PhD, Research Fellow, Laboratory of Infectious Pathology and Molecular Microecology.</p><p>3, Tsyurupy Street, 117418, Moscow, Russian Federation</p></bio><email xlink:type="simple">alexander.markin.34@gmail.com</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-0978-6444</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Собенин</surname><given-names>И. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Sobenin</surname><given-names>I. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Собенин Игорь Александрович - доктор медицинских наук, руководитель лаборатории медицинской генетики.</p><p>121552, Россия, г. Москва, ул. 3-я Черепковская 15а</p></bio><bio xml:lang="en"><p>Dr. Igor A. Sobenin - MD, DSc, Head of the Laboratory for Medical Genetics.</p><p>15A, 3rd Cherepkovskaya Street, 121552, Moscow, Russian Federation</p></bio><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Орехов</surname><given-names>А. H.</given-names></name><name name-style="western" xml:lang="en"><surname>Orekhov</surname><given-names>A. N.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Орехов Александр Николаевич - доктор биологических наук, профессор, заведующий лабораторией ангиопатологии; ведущий научный сотрудник лаборатории инфекционной патологии и молекулярной микроэкологии.</p><p>125315, Россия, ул. Балтийская, 8</p><p>117418, Россия, Москва, ул. Цюрупы, д. 3</p></bio><bio xml:lang="en"><p>Prof. Alexander N. Orekhov - MD, DSc, Professor, Head of the Laboratory of Angiopathology; Senior Researcher, Laboratory of Infectious Pathology and Molecular Microecology.</p><p>8, Baltiyskaya Street, 125315, Moscow, Russian Federation</p><p>3, Tsyurupy Street, 117418, Moscow, Russian Federation</p></bio><xref ref-type="aff" rid="aff-3"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>ФГБНУ «Научно-исследовательский институт морфологии человека»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Research Institute of Human Morphology</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>ФГБНУ «Национальный медицинский исследовательский центр кардиологии» Министерства здравоохранения Российской Федерации</institution><country>Россия</country></aff><aff xml:lang="en"><institution>National Medical Cardiology Research Center</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru"><institution>ФГБНУ «Научно-исследовательский институт морфологии человека»; ФГБНУ «Научно-исследовательский институт общей патологии и патофизиологии»</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Research Institute of Human Morphology; Research Institute of Pathology and Pathophysiology</institution><country>Russian Federation</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2020</year></pub-date><pub-date pub-type="epub"><day>27</day><month>06</month><year>2020</year></pub-date><volume>5</volume><issue>2</issue><fpage>112</fpage><lpage>118</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Маркина Ю.В., Маркин А.М., Собенин И.А., Орехов А.H., 2020</copyright-statement><copyright-year>2020</copyright-year><copyright-holder xml:lang="ru">Маркина Ю.В., Маркин А.М., Собенин И.А., Орехов А.H.</copyright-holder><copyright-holder xml:lang="en">Markina Y.V., Markin A.M., Sobenin I.A., Orekhov A.N.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://fcm.kemsmu.ru/jour/article/view/270">https://fcm.kemsmu.ru/jour/article/view/270</self-uri><abstract><p>Ключевую роль в борьбе с различными патогенами, направленную на выживание клеток и организма в целом играют иммуноглобулины. Данные о центральной роли гликозилирования были подтверждены в ходе многочисленных исследований течения множества заболеваний человека. В частности, изменение профиля гликозилирования антител наблюдается при воспалительных заболеваниях (аутоиммунитет, злокачественные новообразования), а также инфекционных и онкологических заболеваниях. Можно смело утверждать, что анализ гликозилирования антител может стать многообещающим дополнением для совершенствования существующих стратегий диагностики различных заболеваний. В дополнение к этому, специфические изменения молекул гликанов иммуноглобулинов можно использовать в терапии заболеваний различного рода моноклональными антителами, что подчеркивает важную роль гликанов в формировании эффекторной функции антител. Всё это будет способствовать очередному прорыву в области разработки терапевтических препаратов и вакцин следующего поколения.</p></abstract><trans-abstract xml:lang="en"><p>The central role of glycosylation has been well confirmed in numerous studies. In particular, a change in the glycosylation profile of antibodies is observed in infectious diseases, autoimmune disorders and cancer. The analysis of antibody glycosylation can lead to a promising improvement of existing strategies for the disease diagnosis. Specific changes in immunoglobulin glycan molecules can be used in the targeted therapy of multiple diseases, emphasizing the importance of glycans in antibody effector function. Altogether, use of sialylated immunoglobulins may contribute to the next breakthrough in the development of therapeutic drugs and vaccines of the next generation.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>гликаны</kwd><kwd>иммуноглобулины</kwd><kwd>антитела</kwd><kwd>воспаление</kwd><kwd>сиалирование</kwd></kwd-group><kwd-group xml:lang="en"><kwd>Glycans</kwd><kwd>immunoglobulins</kwd><kwd>antibodies</kwd><kwd>inflammation</kwd><kwd>sialylation</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Cooper MD, Alder MN. The evolution of adaptive immune systems. Cell. 2006;124(4):815-822. https://doi.org/10.1016/j.cell.2006.02.001</mixed-citation><mixed-citation xml:lang="en">Cooper MD, Alder MN. The evolution of adaptive immune systems. Cell. 2006;124(4):815-822. https://doi.org/10.1016/j.cell.2006.02.001</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Schroeder HW Jr, Cavacini L. Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010;125(2):41-52. https://doi.org/10.1016/j.jaci.2009.09.046</mixed-citation><mixed-citation xml:lang="en">Schroeder HW Jr, Cavacini L. Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010;125(2):41-52. https://doi.org/10.1016/j.jaci.2009.09.046</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Vidarsson G, Dekkers G, Rispens T. IgG subclasses and allotypes: from structure to effector functions. Front Immunol. 2014;5:520. https://doi.org/ 10.3389/fimmu.2014.00520</mixed-citation><mixed-citation xml:lang="en">Vidarsson G, Dekkers G, Rispens T. IgG subclasses and allotypes: from structure to effector functions. Front Immunol. 2014;5:520. https://doi.org/ 10.3389/fimmu.2014.00520</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Market E, Papavasiliou FN. V(D)J recombination and the evolution of the adaptive immune system. PLoS Biol. 2003;1(1):E16. https://doi.org/10.1371/journal.pbio.0000016</mixed-citation><mixed-citation xml:lang="en">Market E, Papavasiliou FN. V(D)J recombination and the evolution of the adaptive immune system. PLoS Biol. 2003;1(1):E16. https://doi.org/10.1371/journal.pbio.0000016</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Bournazos S, Ravetch JV. Fcgamma receptor function and the design of vaccination strategies. Immunity. 2017;47(2):224-233. https://doi.org/10.1016/j.immuni.2017.07.009</mixed-citation><mixed-citation xml:lang="en">Bournazos S, Ravetch JV. Fcgamma receptor function and the design of vaccination strategies. Immunity. 2017;47(2):224-233. https://doi.org/10.1016/j.immuni.2017.07.009</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Rajewsky K, Forster I, Cumano A. Evolutionary and somatic selection of the antibody repertoire in the mouse. Science. 1987;238(4830):1088-1094. https://doi.org/10.1126/science.3317826</mixed-citation><mixed-citation xml:lang="en">Rajewsky K, Forster I, Cumano A. Evolutionary and somatic selection of the antibody repertoire in the mouse. Science. 1987;238(4830):1088-1094. https://doi.org/10.1126/science.3317826</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Nimmerjahn F, Ravetch JV. Divergent immunoglobulin g subclass activity through selective Fc receptor binding. Science. 2005;310(5753):1510-1512. https://doi.org/10.1126/science.1118948</mixed-citation><mixed-citation xml:lang="en">Nimmerjahn F, Ravetch JV. Divergent immunoglobulin g subclass activity through selective Fc receptor binding. Science. 2005;310(5753):1510-1512. https://doi.org/10.1126/science.1118948</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Dwek RA. Biological importance of glycosylation. Dev Biol Stand. 1998;96:43-47.</mixed-citation><mixed-citation xml:lang="en">Dwek RA. Biological importance of glycosylation. Dev Biol Stand. 1998;96:43-47.</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol. 2007;25:21-50. https://doi.org/10.1146/annurev.immunol.25.022106.141702</mixed-citation><mixed-citation xml:lang="en">Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol. 2007;25:21-50. https://doi.org/10.1146/annurev.immunol.25.022106.141702</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Jennewein MF, Alter G. The immunoregulatory roles of antibody glycosylation. Trends Immunol. 2017;38(5):358-372. https://doi.org/10.1016/j.it.2017.02.004</mixed-citation><mixed-citation xml:lang="en">Jennewein MF, Alter G. The immunoregulatory roles of antibody glycosylation. Trends Immunol. 2017;38(5):358-372. https://doi.org/10.1016/j.it.2017.02.004</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Goulabchand R, Vincent T, Batteux F, Eliaou JF, Guilpain P. Impact of autoantibody glycosylation in autoimmune diseases. Autoimmun. 2014;13(7):742-750. https://doi.org/10.1016/j.autrev.2014.02.005</mixed-citation><mixed-citation xml:lang="en">Goulabchand R, Vincent T, Batteux F, Eliaou JF, Guilpain P. Impact of autoantibody glycosylation in autoimmune diseases. Autoimmun. 2014;13(7):742-750. https://doi.org/10.1016/j.autrev.2014.02.005</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Schwab I, Nimmerjahn F. Intravenous immunoglobulin therapy: how does IgG modulate the immune system? Nat Rev Immunol. 2013;13(3):176-189. https://doi.org/10.1038/nri3401</mixed-citation><mixed-citation xml:lang="en">Schwab I, Nimmerjahn F. Intravenous immunoglobulin therapy: how does IgG modulate the immune system? Nat Rev Immunol. 2013;13(3):176-189. https://doi.org/10.1038/nri3401</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Seeling M, Bruckner C, Nimmerjahn F. Differential antibody glycosylation in autoimmunity: sweet biomarker or modulator of disease activity? Nat Rev Rheumatol. 2017;13(3):621-630. https://doi.org/10.1038/nrrheum.2017.146</mixed-citation><mixed-citation xml:lang="en">Seeling M, Bruckner C, Nimmerjahn F. Differential antibody glycosylation in autoimmunity: sweet biomarker or modulator of disease activity? Nat Rev Rheumatol. 2017;13(3):621-630. https://doi.org/10.1038/nrrheum.2017.146</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Parekh RB, Dwek RA, Sutton BJ, Fernandes D., Leung A, Stanworth D, Rademacher TW, Mizuochi T, Taniguchi T, Matsuta K. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature. 1985;316(6027):452-457. https://doi.org/10.1038/316452a0</mixed-citation><mixed-citation xml:lang="en">Parekh RB, Dwek RA, Sutton BJ, Fernandes D., Leung A, Stanworth D, Rademacher TW, Mizuochi T, Taniguchi T, Matsuta K. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature. 1985;316(6027):452-457. https://doi.org/10.1038/316452a0</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Gudelj I, Salo PP, Trbojevic-Akmacic I, Albers M, Primorac D, Perola M, Lauc G. Low galactosylation of IgG associates with higher risk for future diagnosis of rheumatoid arthritis during 10years of follow-up. Biochim Biophys Acta Mol Basis Dis. 2018;1864(6 PtA):2034-2039. https://doi.org/10.1016/j.bbadis.2018.03.018</mixed-citation><mixed-citation xml:lang="en">Gudelj I, Salo PP, Trbojevic-Akmacic I, Albers M, Primorac D, Perola M, Lauc G. Low galactosylation of IgG associates with higher risk for future diagnosis of rheumatoid arthritis during 10years of follow-up. Biochim Biophys Acta Mol Basis Dis. 2018;1864(6 PtA):2034-2039. https://doi.org/10.1016/j.bbadis.2018.03.018</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Rombouts Y, Ewing E, van de Stadt LA, Selman MH, Trouw LA, Deelder A, Huizinga TW, Wuhrer M, van Schaardenburg D, Toes RE, Scherer HU. Anti-citrullinated protein antibodies acquire a pro-inflammatory Fc glycosylation phenotype prior to the onset of rheumatoid arthritis. Ann Rheumatic Dis. 2015;74(1):234-241. https://doi.org/10.1136/annrheumdis-2013-203565</mixed-citation><mixed-citation xml:lang="en">Rombouts Y, Ewing E, van de Stadt LA, Selman MH, Trouw LA, Deelder A, Huizinga TW, Wuhrer M, van Schaardenburg D, Toes RE, Scherer HU. Anti-citrullinated protein antibodies acquire a pro-inflammatory Fc glycosylation phenotype prior to the onset of rheumatoid arthritis. Ann Rheumatic Dis. 2015;74(1):234-241. https://doi.org/10.1136/annrheumdis-2013-203565</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Fokkink WJ, Selman MH, Dortland JR, Durmus B, Kuitwaard K, Huizinga R, van Rijs W, Tio-Gillen AP, van Doorn PA, Deelder AM, Wuhrer M, Jacobs BC. IgG Fc N-glycosylation in Guillain- Barre syndrome treated with immunoglobulins. J Proteome Res. 2014;13(3):1722-1730. https://doi.org/10.1021/pr401213z</mixed-citation><mixed-citation xml:lang="en">Fokkink WJ, Selman MH, Dortland JR, Durmus B, Kuitwaard K, Huizinga R, van Rijs W, Tio-Gillen AP, van Doorn PA, Deelder AM, Wuhrer M, Jacobs BC. IgG Fc N-glycosylation in Guillain- Barre syndrome treated with immunoglobulins. J Proteome Res. 2014;13(3):1722-1730. https://doi.org/10.1021/pr401213z</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Trbojevic Akmacic I, Ventham NT, Theodoratou E, Vuckovic F, Kennedy N., Kristic J, Nimmo ER, Kalla R, Drummond H, Stambuk J, Dunlop MG, Novokmet M, Aulchenko Y, Gornik O, Campbell H, Pucic Bakovic M, Satsangi J, Lauc G; IBDBIOM Consortium. Inflammatory bowel disease associates with proinflammatory potential of the immunoglobulin G glycome. Inflammatory Bowel Dis. 2015;21(6):1237-1247. https://doi.org/10.1097/MIB.0000000000000372</mixed-citation><mixed-citation xml:lang="en">Trbojevic Akmacic I, Ventham NT, Theodoratou E, Vuckovic F, Kennedy N., Kristic J, Nimmo ER, Kalla R, Drummond H, Stambuk J, Dunlop MG, Novokmet M, Aulchenko Y, Gornik O, Campbell H, Pucic Bakovic M, Satsangi J, Lauc G; IBDBIOM Consortium. Inflammatory bowel disease associates with proinflammatory potential of the immunoglobulin G glycome. Inflammatory Bowel Dis. 2015;21(6):1237-1247. https://doi.org/10.1097/MIB.0000000000000372</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Strassheim D, Karoor V, Stenmark K, Verin A, Gerasimovskaya E. A current view of G protein-coupled receptor-mediated signaling in pulmonary hypertension: finding opportunities for therapeutic intervention. Vessel Plus. 2018;2. pii: 29. https://doi.org/10.20517/2574-1209.2018.44</mixed-citation><mixed-citation xml:lang="en">Strassheim D, Karoor V, Stenmark K, Verin A, Gerasimovskaya E. A current view of G protein-coupled receptor-mediated signaling in pulmonary hypertension: finding opportunities for therapeutic intervention. Vessel Plus. 2018;2. pii: 29. https://doi.org/10.20517/2574-1209.2018.44</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Troelsen LN, Jacobsen S, Abrahams JL, Royle L, Rudd PM, Narvestad E, Heegaard NH, Garred P. IgG glycosylation changes and MBL2 polymorphisms: associations with markers of systemic inflammation and joint destruction in rheumatoid arthritis. J Rheumatol. 2012;39:463-469. https://doi.org/10.3899/jrheum.110584</mixed-citation><mixed-citation xml:lang="en">Troelsen LN, Jacobsen S, Abrahams JL, Royle L, Rudd PM, Narvestad E, Heegaard NH, Garred P. IgG glycosylation changes and MBL2 polymorphisms: associations with markers of systemic inflammation and joint destruction in rheumatoid arthritis. J Rheumatol. 2012;39:463-469. https://doi.org/10.3899/jrheum.110584</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Mihai S, Nimmerjahn F. The role of Fc receptors and complement in autoimmunity. Autoimmun Rev. 2013;12(6):657-60. https://doi.org/10.1016/j.autrev.2012.10.008</mixed-citation><mixed-citation xml:lang="en">Mihai S, Nimmerjahn F. The role of Fc receptors and complement in autoimmunity. Autoimmun Rev. 2013;12(6):657-60. https://doi.org/10.1016/j.autrev.2012.10.008</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Engdahl C, Bondt A, Harre U, Raufer J, Pfeifle R, Camponeschi A, Wuhrer M, Seeling M, Martensson IL, Nimmerjahn F, Kronke G, Scherer HU, Forsblad-d'Elia H, Schett G. Estrogen induces St6gal1 expression and increases IgG sialylation in mice and patients with rheumatoid arthritis: a potential explanation for the increased risk of rheumatoid arthritis in postmenopausal women. Arthritis Res Ther. 2018;20(1):84. https://doi.org/10.1186/s13075-018-1586-z</mixed-citation><mixed-citation xml:lang="en">Engdahl C, Bondt A, Harre U, Raufer J, Pfeifle R, Camponeschi A, Wuhrer M, Seeling M, Martensson IL, Nimmerjahn F, Kronke G, Scherer HU, Forsblad-d'Elia H, Schett G. Estrogen induces St6gal1 expression and increases IgG sialylation in mice and patients with rheumatoid arthritis: a potential explanation for the increased risk of rheumatoid arthritis in postmenopausal women. Arthritis Res Ther. 2018;20(1):84. https://doi.org/10.1186/s13075-018-1586-z</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Matsumoto A, Shikata K, Takeuchi F, Kojima N, Mizuochi T. Autoantibody activity of IgG rheumatoid factor increases with decreasing levels of galactosylation and sialylation. J Biochem. 2000;128(4):621-628. https://doi.org/10.1093/oxfordjournals.jbchem.a022794</mixed-citation><mixed-citation xml:lang="en">Matsumoto A, Shikata K, Takeuchi F, Kojima N, Mizuochi T. Autoantibody activity of IgG rheumatoid factor increases with decreasing levels of galactosylation and sialylation. J Biochem. 2000;128(4):621-628. https://doi.org/10.1093/oxfordjournals.jbchem.a022794</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Fokkink WJ, Selman MH, Dortland JR, Durmus B, Kuitwaard K, Huizinga R, van Rijs W, Tio-Gillen AP, van Doorn PA, Deelder AM, Wuhrer M, Jacobs BC. IgG Fc N-glycosylation in Guillain- Barre syndrome treated with immunoglobulins. J Proteome Res. 2014;13(3):1722-1730. https://doi.org/10.1021/pr401213z</mixed-citation><mixed-citation xml:lang="en">Fokkink WJ, Selman MH, Dortland JR, Durmus B, Kuitwaard K, Huizinga R, van Rijs W, Tio-Gillen AP, van Doorn PA, Deelder AM, Wuhrer M, Jacobs BC. IgG Fc N-glycosylation in Guillain- Barre syndrome treated with immunoglobulins. J Proteome Res. 2014;13(3):1722-1730. https://doi.org/10.1021/pr401213z</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Kemna MJ, Plomp R, van Paassen P, Koeleman CAM, Jansen BC, Damoiseaux J, Cohen Tervaert JW, Wuhrer M. Galactosylation and sialylation levels of IgG predict relapse in patients with PR3-ANCA associated vasculitis. EBioMedicine. 2017;17:108-118. https://doi.org/10.1016/j.ebiom.2017.01.033</mixed-citation><mixed-citation xml:lang="en">Kemna MJ, Plomp R, van Paassen P, Koeleman CAM, Jansen BC, Damoiseaux J, Cohen Tervaert JW, Wuhrer M. Galactosylation and sialylation levels of IgG predict relapse in patients with PR3-ANCA associated vasculitis. EBioMedicine. 2017;17:108-118. https://doi.org/10.1016/j.ebiom.2017.01.033</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Ogata S, Shimizu C, Franco A, Touma R, Kanegaye JT, Choudhury BP, Naidu NN, Kanda Y, Hoang LT, Hibberd ML, Tremoulet AH, Varki A, Burns JC. Treatment response in kawasaki disease is associated with sialylation levels of endogenous but not therapeutic intravenous immunoglobulin g. PLoS One. 2013;8(12):e81448. https://doi.org/10.1371/journal.pone.0081448</mixed-citation><mixed-citation xml:lang="en">Ogata S, Shimizu C, Franco A, Touma R, Kanegaye JT, Choudhury BP, Naidu NN, Kanda Y, Hoang LT, Hibberd ML, Tremoulet AH, Varki A, Burns JC. Treatment response in kawasaki disease is associated with sialylation levels of endogenous but not therapeutic intravenous immunoglobulin g. PLoS One. 2013;8(12):e81448. https://doi.org/10.1371/journal.pone.0081448</mixed-citation></citation-alternatives></ref><ref id="cit27"><label>27</label><citation-alternatives><mixed-citation xml:lang="ru">Anthony RM, Nimmerjahn F, Ashline DJ, Reinhold VN, Paulson JC, Ravetch JV. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science. 2008;320(5874):373-376. https://doi.org/10.1126/science.1154315</mixed-citation><mixed-citation xml:lang="en">Anthony RM, Nimmerjahn F, Ashline DJ, Reinhold VN, Paulson JC, Ravetch JV. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science. 2008;320(5874):373-376. https://doi.org/10.1126/science.1154315</mixed-citation></citation-alternatives></ref><ref id="cit28"><label>28</label><citation-alternatives><mixed-citation xml:lang="ru">Mehta AS, Long RE, Comunale MA, Wang M, Rodemich L, Krakover J, Philip R, Marrero JA, Dwek RA, Block TM. Increased levels of galactose-deficient anti-Gal immunoglobulin G in the sera of hepatitis C virus-infected individuals with fibrosis and cirrhosis. J Virol. 2008;82(3):1259-1270. https://doi.org/10.1128/JVI.01600-07</mixed-citation><mixed-citation xml:lang="en">Mehta AS, Long RE, Comunale MA, Wang M, Rodemich L, Krakover J, Philip R, Marrero JA, Dwek RA, Block TM. Increased levels of galactose-deficient anti-Gal immunoglobulin G in the sera of hepatitis C virus-infected individuals with fibrosis and cirrhosis. J Virol. 2008;82(3):1259-1270. https://doi.org/10.1128/JVI.01600-07</mixed-citation></citation-alternatives></ref><ref id="cit29"><label>29</label><citation-alternatives><mixed-citation xml:lang="ru">Ackerman ME, Crispin M, Yu X, Baruah K, Boesch AW, Harvey DJ, Dugast AS, Heizen EL, Ercan A, Choi I, Streeck H, Nigrovic PA, Bailey-Kellogg C, Scanlan C, Alter G. Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest. 2013;123(5):2183-2192. https://doi.org/10.1172/JCI65708</mixed-citation><mixed-citation xml:lang="en">Ackerman ME, Crispin M, Yu X, Baruah K, Boesch AW, Harvey DJ, Dugast AS, Heizen EL, Ercan A, Choi I, Streeck H, Nigrovic PA, Bailey-Kellogg C, Scanlan C, Alter G. Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J Clin Invest. 2013;123(5):2183-2192. https://doi.org/10.1172/JCI65708</mixed-citation></citation-alternatives></ref><ref id="cit30"><label>30</label><citation-alternatives><mixed-citation xml:lang="ru">Aurer I, Lauc G, Dumic J, Rendic D, Matisic D, Milos M, Heffer- Lauc M, Flogel M, Labar B. Aberrant glycosylation of Igg heavy chain in multiple myeloma. Collegium Antropologicum. 2007;31(1):247-251.</mixed-citation><mixed-citation xml:lang="en">Aurer I, Lauc G, Dumic J, Rendic D, Matisic D, Milos M, Heffer- Lauc M, Flogel M, Labar B. Aberrant glycosylation of Igg heavy chain in multiple myeloma. Collegium Antropologicum. 2007;31(1):247-251.</mixed-citation></citation-alternatives></ref><ref id="cit31"><label>31</label><citation-alternatives><mixed-citation xml:lang="ru">Fleming SC, Smith S, Knowles D, Skillen A, Self CH. Increased sialylation of oligosaccharides on IgG paraproteins - a potential new tumour marker in multiple myeloma. J Clin Pathol. 1998;51(11):825-830. https://doi.org/10.1136/jcp.51.11.825</mixed-citation><mixed-citation xml:lang="en">Fleming SC, Smith S, Knowles D, Skillen A, Self CH. Increased sialylation of oligosaccharides on IgG paraproteins - a potential new tumour marker in multiple myeloma. J Clin Pathol. 1998;51(11):825-830. https://doi.org/10.1136/jcp.51.11.825</mixed-citation></citation-alternatives></ref><ref id="cit32"><label>32</label><citation-alternatives><mixed-citation xml:lang="ru">Mimura Y, Ashton PR, Takahashi N, Harvey DJ, Jefferis R. Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry. J Immunol Methods. 2007;326(1-2):116-126. https://doi.org/10.1016/j.jim.2007.07.014</mixed-citation><mixed-citation xml:lang="en">Mimura Y, Ashton PR, Takahashi N, Harvey DJ, Jefferis R. Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry. J Immunol Methods. 2007;326(1-2):116-126. https://doi.org/10.1016/j.jim.2007.07.014</mixed-citation></citation-alternatives></ref><ref id="cit33"><label>33</label><citation-alternatives><mixed-citation xml:lang="ru">Mittermayr S, Le GN, Clarke C, Millan Martin S, Larkin AM, O'Gorman P, Bones J. Polyclonal Immunoglobulin G N-Glycosylation in the pathogenesis of plasma cell disorders. J Proteome Res. 2017;16(2):748-762. https://doi.org/10.1021/acs.jproteome.6b00768</mixed-citation><mixed-citation xml:lang="en">Mittermayr S, Le GN, Clarke C, Millan Martin S, Larkin AM, O'Gorman P, Bones J. Polyclonal Immunoglobulin G N-Glycosylation in the pathogenesis of plasma cell disorders. J Proteome Res. 2017;16(2):748-762. https://doi.org/10.1021/acs.jproteome.6b00768</mixed-citation></citation-alternatives></ref><ref id="cit34"><label>34</label><citation-alternatives><mixed-citation xml:lang="ru">Arnold JN, Saldova R, Galligan MC, Murphy TB, Mimura-Kimura Y, Telford JE, Godwin AK, Rudd PM. Novel glycan biomarkers for the detection of lung cancer. J Proteome Res. 2011;10(4):1755-1764. https://doi.org/10.1021/pr101034t</mixed-citation><mixed-citation xml:lang="en">Arnold JN, Saldova R, Galligan MC, Murphy TB, Mimura-Kimura Y, Telford JE, Godwin AK, Rudd PM. Novel glycan biomarkers for the detection of lung cancer. J Proteome Res. 2011;10(4):1755-1764. https://doi.org/10.1021/pr101034t</mixed-citation></citation-alternatives></ref><ref id="cit35"><label>35</label><citation-alternatives><mixed-citation xml:lang="ru">Alley WR Jr, Vasseur JA, Goetz JA, Svoboda M, Mann BF, Matei DE, Menning N, Hussein A, Mechref Y, Novotny MV. N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients. J Proteome Res. 2012;11:2282-2300. https://doi.org/10.1021/pr201070k</mixed-citation><mixed-citation xml:lang="en">Alley WR Jr, Vasseur JA, Goetz JA, Svoboda M, Mann BF, Matei DE, Menning N, Hussein A, Mechref Y, Novotny MV. N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients. J Proteome Res. 2012;11:2282-2300. https://doi.org/10.1021/pr201070k</mixed-citation></citation-alternatives></ref><ref id="cit36"><label>36</label><citation-alternatives><mixed-citation xml:lang="ru">van de Bovenkamp FS, Hafkenscheid L, Rispens T, Rombouts Y. The emerging importance of IgG fab glycosylation in immunity. J Immunol. 2016;196(4):1435-1441. https://doi.org/10.4049/jimmunol.1502136</mixed-citation><mixed-citation xml:lang="en">van de Bovenkamp FS, Hafkenscheid L, Rispens T, Rombouts Y. The emerging importance of IgG fab glycosylation in immunity. J Immunol. 2016;196(4):1435-1441. https://doi.org/10.4049/jimmunol.1502136</mixed-citation></citation-alternatives></ref><ref id="cit37"><label>37</label><citation-alternatives><mixed-citation xml:lang="ru">Hashimoto R, Toda T, Tsutsumi H, Ohta M, Mori M. Abnormal N-glycosylation of the immunoglobulin G kappa chain in a multiple myeloma patient with crystalglobulinemia: case report. Int J Hematol. 2007;85(3):203-206. https://doi.org/10.1532/IJH97.06074</mixed-citation><mixed-citation xml:lang="en">Hashimoto R, Toda T, Tsutsumi H, Ohta M, Mori M. Abnormal N-glycosylation of the immunoglobulin G kappa chain in a multiple myeloma patient with crystalglobulinemia: case report. Int J Hematol. 2007;85(3):203-206. https://doi.org/10.1532/IJH97.06074</mixed-citation></citation-alternatives></ref><ref id="cit38"><label>38</label><citation-alternatives><mixed-citation xml:lang="ru">Käsermann F, Boerema DJ, Rüegsegger M, Hofmann A, Wymann S, Zuercher AW, Miescher S. Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation. PLoS One. 2012;7(6):e37243. https://doi.org/10.1371/journal.pone.0037243</mixed-citation><mixed-citation xml:lang="en">Käsermann F, Boerema DJ, Rüegsegger M, Hofmann A, Wymann S, Zuercher AW, Miescher S. Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation. PLoS One. 2012;7(6):e37243. https://doi.org/10.1371/journal.pone.0037243</mixed-citation></citation-alternatives></ref><ref id="cit39"><label>39</label><citation-alternatives><mixed-citation xml:lang="ru">Wiedeman AE, Santer DM, Yan W, Miescher S, Käsermann F, Elkon KB. Contrasting mechanisms of interferon-alpha inhibi-tion by intravenous immunoglobulin after induction by immune complexes versus Toll-like receptor agonists. Arthritis Rheum. 2013;65(10):2713-2723. https://doi.org/10.1002/art.38082</mixed-citation><mixed-citation xml:lang="en">Wiedeman AE, Santer DM, Yan W, Miescher S, Käsermann F, Elkon KB. Contrasting mechanisms of interferon-alpha inhibi-tion by intravenous immunoglobulin after induction by immune complexes versus Toll-like receptor agonists. Arthritis Rheum. 2013;65(10):2713-2723. https://doi.org/10.1002/art.38082</mixed-citation></citation-alternatives></ref><ref id="cit40"><label>40</label><citation-alternatives><mixed-citation xml:lang="ru">Takai T. Roles of Fc receptors in autoimmunity. Nat Rev Immunol. 2002;2(8):580-592. https://doi.org/10.1038/nri856</mixed-citation><mixed-citation xml:lang="en">Takai T. Roles of Fc receptors in autoimmunity. Nat Rev Immunol. 2002;2(8):580-592. https://doi.org/10.1038/nri856</mixed-citation></citation-alternatives></ref><ref id="cit41"><label>41</label><citation-alternatives><mixed-citation xml:lang="ru">Pincetic A, Bournazos S, DiLillo D. Maamary J, Wang TT, Dahan R, Fiebiger BM, Ravetch JV. Type I and type II Fc receptors regulate innate and adaptive immunity. Nat Immunol. 2014;15(8):707-716. https://doi.org/10.1038/ni.2939</mixed-citation><mixed-citation xml:lang="en">Pincetic A, Bournazos S, DiLillo D. Maamary J, Wang TT, Dahan R, Fiebiger BM, Ravetch JV. Type I and type II Fc receptors regulate innate and adaptive immunity. Nat Immunol. 2014;15(8):707-716. https://doi.org/10.1038/ni.2939</mixed-citation></citation-alternatives></ref><ref id="cit42"><label>42</label><citation-alternatives><mixed-citation xml:lang="ru">Debre M, Bonnet MC, Fridman WH, Carosella E, Philippe N, Reinert P, Vilmer E, Kaplan C, Teillaud JL, Griscelli C. Infusion of Fc gamma fragments for treatment of children with acute immune thrombocytopenic purpura. Lancet. 1993;342(8877):945-949. https://doi.org/10.1016/0140-6736(93)92000-j</mixed-citation><mixed-citation xml:lang="en">Debre M, Bonnet MC, Fridman WH, Carosella E, Philippe N, Reinert P, Vilmer E, Kaplan C, Teillaud JL, Griscelli C. Infusion of Fc gamma fragments for treatment of children with acute immune thrombocytopenic purpura. Lancet. 1993;342(8877):945-949. https://doi.org/10.1016/0140-6736(93)92000-j</mixed-citation></citation-alternatives></ref><ref id="cit43"><label>43</label><citation-alternatives><mixed-citation xml:lang="ru">Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006;313(5787):670-673. https://doi.org/10.1126/science.1129594</mixed-citation><mixed-citation xml:lang="en">Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006;313(5787):670-673. https://doi.org/10.1126/science.1129594</mixed-citation></citation-alternatives></ref><ref id="cit44"><label>44</label><citation-alternatives><mixed-citation xml:lang="ru">Washburn N, Schwab I, Ortiz D, Bhatnagar N, Lansing JC, Medeiros A, Tyler S, Mekala D, Cochran E, Sarvaiya H, Garofalo K, Meccariello R, Meador JW, Rutitzky L, Schultes BC, Ling L, Avery W, Nimmerjahn F, Manning AM, Kaundinya GV, Bosques CJ. Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity. Proc Natl Acad Sci U S A. 2015;112(11):E1297-306. https://doi.org/10.1073/pnas.1422481112</mixed-citation><mixed-citation xml:lang="en">Washburn N, Schwab I, Ortiz D, Bhatnagar N, Lansing JC, Medeiros A, Tyler S, Mekala D, Cochran E, Sarvaiya H, Garofalo K, Meccariello R, Meador JW, Rutitzky L, Schultes BC, Ling L, Avery W, Nimmerjahn F, Manning AM, Kaundinya GV, Bosques CJ. Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity. Proc Natl Acad Sci U S A. 2015;112(11):E1297-306. https://doi.org/10.1073/pnas.1422481112</mixed-citation></citation-alternatives></ref><ref id="cit45"><label>45</label><citation-alternatives><mixed-citation xml:lang="ru">Anthony RM, Kobayashi T, Wermeling F, Ravetch JV. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature. 2011;475(7354):110-113. https://doi.org/10.1038/nature10134</mixed-citation><mixed-citation xml:lang="en">Anthony RM, Kobayashi T, Wermeling F, Ravetch JV. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature. 2011;475(7354):110-113. https://doi.org/10.1038/nature10134</mixed-citation></citation-alternatives></ref><ref id="cit46"><label>46</label><citation-alternatives><mixed-citation xml:lang="ru">Ahmed AA, Giddens J, Pincetic A, Lomino JV, Ravetch JV, Wang LX, Bjorkman PJ. Structural characterization of anti-inflammatory immunoglobulin G Fc proteins. J Mol Biol. 2014;426(18):3166-3179. https://doi.org/10.1016/j.jmb.2014.07.006</mixed-citation><mixed-citation xml:lang="en">Ahmed AA, Giddens J, Pincetic A, Lomino JV, Ravetch JV, Wang LX, Bjorkman PJ. Structural characterization of anti-inflammatory immunoglobulin G Fc proteins. J Mol Biol. 2014;426(18):3166-3179. https://doi.org/10.1016/j.jmb.2014.07.006</mixed-citation></citation-alternatives></ref><ref id="cit47"><label>47</label><citation-alternatives><mixed-citation xml:lang="ru">Yu X, Vasiljevic S, Mitchell DA, Crispin M, Scanlan CN. Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain. J Mol Biol. 2013;425(8):1253-1258. https://doi.org/10.1016/j.jmb.2013.02.006</mixed-citation><mixed-citation xml:lang="en">Yu X, Vasiljevic S, Mitchell DA, Crispin M, Scanlan CN. Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain. J Mol Biol. 2013;425(8):1253-1258. https://doi.org/10.1016/j.jmb.2013.02.006</mixed-citation></citation-alternatives></ref><ref id="cit48"><label>48</label><citation-alternatives><mixed-citation xml:lang="ru">Seite JF, Cornec D, Renaudineau Y, Youinou P, Mageed RA, Hillion S. IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes. Blood. 2010;116(10):1698-1704. https://doi.org/10.1182/blood-2009-12-261461</mixed-citation><mixed-citation xml:lang="en">Seite JF, Cornec D, Renaudineau Y, Youinou P, Mageed RA, Hillion S. IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes. Blood. 2010;116(10):1698-1704. https://doi.org/10.1182/blood-2009-12-261461</mixed-citation></citation-alternatives></ref><ref id="cit49"><label>49</label><citation-alternatives><mixed-citation xml:lang="ru">Massoud AH, Yona M, Xue D, Chouiali F, Alturaihi H, Ablona A, Mourad W, Piccirillo CA, Mazer BD. Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells. J Allergy Clin Immunol. 2014;133(3):853-863.e5. https://doi.org/10.1016/j.jaci.2013.09.029</mixed-citation><mixed-citation xml:lang="en">Massoud AH, Yona M, Xue D, Chouiali F, Alturaihi H, Ablona A, Mourad W, Piccirillo CA, Mazer BD. Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells. J Allergy Clin Immunol. 2014;133(3):853-863.e5. https://doi.org/10.1016/j.jaci.2013.09.029</mixed-citation></citation-alternatives></ref><ref id="cit50"><label>50</label><citation-alternatives><mixed-citation xml:lang="ru">Haga CL, Ehrhardt GR, Boohaker RJ, Davis RS, Cooper MD. Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment. Proc Natl Acad Sci U S A. 2007;104(23):9770-9775. https://doi.org/10.1073/pnas.0703354104</mixed-citation><mixed-citation xml:lang="en">Haga CL, Ehrhardt GR, Boohaker RJ, Davis RS, Cooper MD. Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment. Proc Natl Acad Sci U S A. 2007;104(23):9770-9775. https://doi.org/10.1073/pnas.0703354104</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
