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  1. Book: Bispecific antibodies

    Kontermann, Roland

    2011  

    Author's details Roland E. Kontermann, ed
    Keywords Monoklonaler bispezifischer Antikörper
    Subject code 616.0798
    Language English
    Size XVII, 373 S. : Ill., graph. Darst., 25 cm
    Publisher Springer
    Publishing place Heidelberg u.a.
    Publishing country Germany
    Document type Book
    Note Literaturangaben
    HBZ-ID HT016942863
    ISBN 978-3-642-20909-3 ; 3-642-20909-2 ; 9783642209109 ; 3642209106
    Database Catalogue ZB MED Medicine, Health

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  2. Book: Therapeutic proteins

    Kontermann, Roland

    strategies to modulate their plasma half-lives

    2012  

    Author's details ed. by Roland Kontermann
    Keywords Proteine ; Arzneimittel ; Arzneimittelstabilität ; Biopharmazie
    Subject Biologische Pharmazie ; Fertigarzneimittel ; Therapeutikum ; Medikament ; Medukamente ; Pharmakon ; Pharmaka ; Arzneistoff ; Arzneimittelwirkstoff ; Arznei ; Pharmazeutikum ; Pharmazeutika ; Pharmazeutischer Wirkstoff ; Arzneidroge ; Eiweiss ; Protein
    Language English
    Size XVIII, 354 S. : Ill., graph. Darst., 24 cm
    Publisher Wiley-Blackwell
    Publishing place Weinheim
    Publishing country Germany
    Document type Book
    HBZ-ID HT017152471
    ISBN 978-3-527-32849-9 ; 3-527-32849-1 ; 9783527644797 ; 9783527644803 ; 9783527644827 ; 3527644792 ; 3527644806 ; 3527644822
    Database Catalogue ZB MED Medicine, Health

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  3. Book: Antibody engineering / 2

    Kontermann, Roland / Dübel, Stefan

    2010  

    Author's details Roland Kontermann ; Stefan Dübel (eds.)
    Collection Antibody engineering
    Language English
    Size XII, 589 S. : Ill., graph. Darst.
    Edition 2. ed.
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book
    HBZ-ID HT016449609
    ISBN 978-3-642-01146-7 ; 9783642011474 ; 3-642-01146-2 ; 3642011470
    Database Catalogue ZB MED Medicine, Health

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  4. Book: Antibody engineering / 1

    Kontermann, Roland / Dübel, Stefan

    2010  

    Author's details Roland Kontermann ; Stefan Dübel (eds.)
    Collection Antibody engineering
    Language English
    Size XIII, 788 S. : Ill., graph. Darst.
    Edition 2. ed.
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book
    HBZ-ID HT016449606
    ISBN 978-3-642-01143-6 ; 9783642011443 ; 3-642-01143-8 ; 3642011446
    Database Catalogue ZB MED Medicine, Health

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  5. Book ; Collection: Antibody engineering

    Kontermann, Roland / Dübel, Stefan

    (Springer protocols)

    2010  

    Author's details Roland Kontermann ; Stefan Dübel (eds.)
    Series title Springer protocols
    Keywords Antibodies / genetics ; DNA, Recombinant / immunology ; Antibody Formation / genetics ; Genetic Engineering / methods ; Antikörper ; Rekombinantes Protein ; Herstellung ; Labormedizin
    Subject Labordiagnostik ; Medizinische Labortechnik ; Laboratoriumsdiagnostik ; Laboratoriumsmedizin ; Erzeugung ; Anfertigung ; Rekombinante Substanz ; Hybrid-Protein ; Rekombiniertes Protein ; Fusionsprotein
    Language English
    Dates of publication 2010-9999
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book ; Collection (display volumes)
    HBZ-ID HT016449601
    Database Catalogue ZB MED Medicine, Health

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  6. Article ; Online: The present and future of bispecific antibodies for cancer therapy.

    Klein, Christian / Brinkmann, Ulrich / Reichert, Janice M / Kontermann, Roland E

    Nature reviews. Drug discovery

    2024  Volume 23, Issue 4, Page(s) 301–319

    Abstract: Bispecific antibodies (bsAbs) enable novel mechanisms of action and/or therapeutic applications that cannot be achieved using conventional IgG-based antibodies. Consequently, development of these molecules has garnered substantial interest in the past ... ...

    Abstract Bispecific antibodies (bsAbs) enable novel mechanisms of action and/or therapeutic applications that cannot be achieved using conventional IgG-based antibodies. Consequently, development of these molecules has garnered substantial interest in the past decade and, as of the end of 2023, 14 bsAbs have been approved: 11 for the treatment of cancer and 3 for non-oncology indications. bsAbs are available in different formats, address different targets and mediate anticancer function via different molecular mechanisms. Here, we provide an overview of recent developments in the field of bsAbs for cancer therapy. We focus on bsAbs that are approved or in clinical development, including bsAb-mediated dual modulators of signalling pathways, tumour-targeted receptor agonists, bsAb-drug conjugates, bispecific T cell, natural killer cell and innate immune cell engagers, and bispecific checkpoint inhibitors and co-stimulators. Finally, we provide an outlook into next-generation bsAbs in earlier stages of development, including trispecifics, bsAb prodrugs, bsAbs that induce degradation of tumour targets and bsAbs acting as cytokine mimetics.
    MeSH term(s) Humans ; Antibodies, Bispecific ; Neoplasms ; Signal Transduction
    Chemical Substances Antibodies, Bispecific
    Language English
    Publishing date 2024-03-06
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2062954-0
    ISSN 1474-1784 ; 1474-1776
    ISSN (online) 1474-1784
    ISSN 1474-1776
    DOI 10.1038/s41573-024-00896-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: GlycoTAIL and FlexiTAIL as Half-Life Extension Modules for Recombinant Antibody Fragments.

    Seifert, Oliver / Kontermann, Roland E

    Molecules (Basel, Switzerland)

    2022  Volume 27, Issue 10

    Abstract: Many therapeutic proteins are small in size and are rapidly cleared from circulation. Consequently, half-life extension strategies have emerged to improve pharmacokinetic properties, including fusion or binding to long-lasting serum proteins, chemical ... ...

    Abstract Many therapeutic proteins are small in size and are rapidly cleared from circulation. Consequently, half-life extension strategies have emerged to improve pharmacokinetic properties, including fusion or binding to long-lasting serum proteins, chemical modifications with hydrophilic polymers such as PEGylation, or, more recently, fusion to PEG mimetic polypeptides. In the present study, two different PEG mimetic approaches, the GlycoTAIL and the FlexiTAIL, were applied to increase the hydrodynamic radius of antibody fragments of different sizes and valencies, including scFv, diabody, and scFv-EHD2 fusion proteins. The GlycoTAIL and FlexiTAIL sequences of varying lengths are composed of aliphatic and hydrophilic residues, with the GlycoTAIL furthermore comprising N-glycosylation sites. All modified proteins could be produced in a mammalian expression system without reducing stability and antigen binding, and all modified proteins exhibited a prolonged half-life and increased drug disposition in mice. The strongest effects were observed for proteins comprising a FlexiTAIL of 248 residues. Thus, the GlycoTAIL and FlexiTAIL sequences represent a flexible and modular system to improve the pharmacokinetic properties of proteins.
    MeSH term(s) Animals ; Antibodies/chemistry ; Carrier Proteins ; Half-Life ; Immunoglobulin Fragments/chemistry ; Mice ; Recombinant Fusion Proteins/chemistry
    Chemical Substances Antibodies ; Carrier Proteins ; EHD2 protein, mouse ; Immunoglobulin Fragments ; Recombinant Fusion Proteins
    Language English
    Publishing date 2022-05-19
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules27103272
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Bispecific antibodies.

    Brinkmann, Ulrich / Kontermann, Roland E

    Science (New York, N.Y.)

    2021  Volume 372, Issue 6545, Page(s) 916–917

    MeSH term(s) Animals ; Antibodies, Bispecific/adverse effects ; Antibodies, Bispecific/immunology ; Antibodies, Bispecific/metabolism ; Antibodies, Bispecific/therapeutic use ; Antibody Affinity ; Antibody Specificity ; Binding Sites, Antibody ; CD3 Complex/immunology ; Cytokines/immunology ; Cytokines/metabolism ; Humans ; Immunotherapy ; Lymphocyte Activation ; Neoplasms/immunology ; Neoplasms/therapy ; Protein Engineering ; T-Lymphocytes/immunology
    Chemical Substances Antibodies, Bispecific ; CD3 Complex ; Cytokines
    Language English
    Publishing date 2021-05-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 128410-1
    ISSN 1095-9203 ; 0036-8075
    ISSN (online) 1095-9203
    ISSN 0036-8075
    DOI 10.1126/science.abg1209
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: GlycoTAIL and FlexiTAIL as Half-Life Extension Modules for Recombinant Antibody Fragments

    Oliver Seifert / Roland E. Kontermann

    Molecules, Vol 27, Iss 3272, p

    2022  Volume 3272

    Abstract: Many therapeutic proteins are small in size and are rapidly cleared from circulation. Consequently, half-life extension strategies have emerged to improve pharmacokinetic properties, including fusion or binding to long-lasting serum proteins, chemical ... ...

    Abstract Many therapeutic proteins are small in size and are rapidly cleared from circulation. Consequently, half-life extension strategies have emerged to improve pharmacokinetic properties, including fusion or binding to long-lasting serum proteins, chemical modifications with hydrophilic polymers such as PEGylation, or, more recently, fusion to PEG mimetic polypeptides. In the present study, two different PEG mimetic approaches, the GlycoTAIL and the FlexiTAIL, were applied to increase the hydrodynamic radius of antibody fragments of different sizes and valencies, including scFv, diabody, and scFv-EHD2 fusion proteins. The GlycoTAIL and FlexiTAIL sequences of varying lengths are composed of aliphatic and hydrophilic residues, with the GlycoTAIL furthermore comprising N-glycosylation sites. All modified proteins could be produced in a mammalian expression system without reducing stability and antigen binding, and all modified proteins exhibited a prolonged half-life and increased drug disposition in mice. The strongest effects were observed for proteins comprising a FlexiTAIL of 248 residues. Thus, the GlycoTAIL and FlexiTAIL sequences represent a flexible and modular system to improve the pharmacokinetic properties of proteins.
    Keywords scFv ; diabody ; scFv-EHD2 fusion protein ; CEA ; FAP ; hydrodynamic radius ; Organic chemistry ; QD241-441
    Subject code 572
    Language English
    Publishing date 2022-05-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Book: Antibody engineering

    Kontermann, Roland

    (Springer lab manuals)

    2001  

    Author's details Roland Kontermann ... (ed.)
    Series title Springer lab manuals
    Keywords Antibodies / genetics ; DNA, Recombinant / immunology ; Antibody Formation / genetics ; Genetic Engineering / methods ; Antikörper ; Rekombinantes Protein ; Herstellung ; Labormedizin
    Subject Labordiagnostik ; Medizinische Labortechnik ; Laboratoriumsdiagnostik ; Laboratoriumsmedizin ; Erzeugung ; Anfertigung ; Rekombinante Substanz ; Hybrid-Protein ; Rekombiniertes Protein ; Fusionsprotein
    Language English
    Size XII, 790 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place Berlin u.a.
    Publishing country Germany
    Document type Book
    Note Literaturangaben
    HBZ-ID HT013184954
    ISBN 3-540-41354-5 ; 978-3-540-41354-7
    Database Catalogue ZB MED Medicine, Health

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