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  <titleInfo>
    <title>Therapeutic proteins : strategies to modulate their plasma half-lives</title>
  </titleInfo>
  <name type="personal">
    <namePart>Kontermann, Roland</namePart>
    <namePart type="date">1961-</namePart>
    <role>
      <roleTerm type="text">editor.</roleTerm>
    </role>
  </name>
  <typeOfResource>text</typeOfResource>
  <genre authority="marc">bibliography</genre>
  <genre authority="">Electronic books.</genre>
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    <dateIssued encoding="marc">2012</dateIssued>
    <copyrightDate encoding="marc">2012</copyrightDate>
    <issuance>monographic</issuance>
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  <language>
    <languageTerm authority="iso639-2b" type="code">eng</languageTerm>
  </language>
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    <form authority="gmd">electronic resource</form>
    <extent>1 online resource (374 pages) : illustrations (some color)</extent>
  </physicalDescription>
  <abstract>For this ready reference, the internationally renowned authority in the field, Roland Kontermann, has assembled a team of outstanding contributors from industry and academia to convey the worldwide knowledge on modifying therapeutic proteins in order to optimize their pharmacological potential. The result is a comprehensive work covering all approaches and aspects of the topic in one handy volume, making this indispensable reading for companies and research institutions working on the development of biopharmaceuticals.</abstract>
  <tableOfContents>General information -- Half-life modulating strategies : an introduction -- Pharmacokinetics and half-life of protein therapeutics -- Half-life extension through chemical and post-translational modifications -- Half-life extension through PEGylation -- Half-life extension of therapeutic proteins via genetic fusion to recombinant PEG mimetics -- Half-life extension through O-glycosylation -- Polysialic acid and polysialylation to modulate antibody pharmacokinetics -- Half-life extension through HESylation -- Half-life modulation involving recycling by the neonatal Fc receptor -- The biology of the neonatal Fc receptor (FcRn) -- half-life extension by fusion to the Fc region -- Monomeric Fc fusion technology: an approach to create long-lasting clotting factors -- The diverse roles of FcRn: implications for antibody engineering -- Half-life extension by fusion to recombinant albumin -- AlbudAb technology platform: versatile albumin binding domains for the development of therapeutics with tunable half-lives -- Half-life extension by binding to albumin through an albumin binding domain -- Half-life extension by binding to albumin through small molecules -- Half-life extension with pharmaceutical formulations -- Half-life extension with pharmaceutical formulations: liposomes -- Half-life extension with pharmaceutical formulations: nanoparticles by the miniemulsion process.</tableOfContents>
  <note type="statement of responsibility">edited by Roland Kontermann.</note>
  <note>Includes bibliographical references and index.</note>
  <subject authority="lcsh">
    <topic>Protein drugs</topic>
    <topic>Design</topic>
  </subject>
  <subject authority="lcsh">
    <topic>Proteins</topic>
    <topic>Therapeutic use</topic>
  </subject>
  <subject authority="mesh">
    <topic>Proteins</topic>
    <topic>pharmacokinetics</topic>
  </subject>
  <subject authority="mesh">
    <topic>Half-Life</topic>
  </subject>
  <subject authority="bisacsh">
    <topic>MEDICAL</topic>
    <topic>Pharmacology</topic>
  </subject>
  <subject authority="fast">
    <topic>Protein drugs</topic>
    <topic>Design</topic>
  </subject>
  <subject authority="fast">
    <topic>Proteins</topic>
    <topic>Therapeutic use</topic>
  </subject>
  <classification authority="lcc">RS431.P75</classification>
  <classification authority="ddc" edition="23">615.3</classification>
  <classification authority="nlm">QU 55</classification>
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      <title>Therapeutic proteins</title>
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      <publisher>Weinheim, Germany : Wiley-VCH, ©2011</publisher>
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    <identifier type="local">(DLC)  2012540834</identifier>
    <identifier type="local">(OCoLC)768072878</identifier>
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  <identifier type="stock number">10.1002/9783527644827 Wiley InterScience</identifier>
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    <recordIdentifier source="OCoLC">ocn779616898</recordIdentifier>
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