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  1. Book: Glyco-engineering

    Castilho, Alexandra

    methods and protocols

    (Methods in molecular biology ; 1321 ; Springer protocols)

    2015  

    Author's details ed. by Alexandra Castilho
    Series title Methods in molecular biology ; 1321
    Springer protocols
    Collection
    Keywords Glycosylation Laboratory manuals
    Language English
    Size XVI, 439 S. : Ill., graph. Darst.
    Publisher Humana Press
    Publishing place New York, NY u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT018848910
    ISBN 978-1-4939-2759-3 ; 1-4939-2759-0 ; 978-1-4939-2760-9 ; 1-4939-2760-4
    Database Catalogue ZB MED Nutrition, Environment, Agriculture

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    In stock of ZB MED Bonn / Germany

    Shelf markLoan statusLocation
    164/89 available for loan (reading room) Freihandmagazin (U1)

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  2. Article: Comparative analysis of plant transient expression vectors for targeted N-glycosylation.

    Eidenberger, Lukas / Eminger, Florian / Castilho, Alexandra / Steinkellner, Herta

    Frontiers in bioengineering and biotechnology

    2022  Volume 10, Page(s) 1073455

    Abstract: While plant-based transient expression systems have demonstrated their potency to rapidly express economically feasible quantities of complex human proteins, less is known about their compatibility with posttranslational modification control. Here we ... ...

    Abstract While plant-based transient expression systems have demonstrated their potency to rapidly express economically feasible quantities of complex human proteins, less is known about their compatibility with posttranslational modification control. Here we investigated three commonly used transient expression vectors, pEAQ, magnICON and pTra for their capability to express a multi-component protein with controlled and modified N-glycosylation. Cetuximab (Cx), a therapeutic IgG1 monoclonal antibody, which carries next to the conserved Fc an additional N-glycosylation site (GS) in the Fab-domain, was used as model. While pEAQ and pTra produce fully assembled Cx at similar levels in
    Language English
    Publishing date 2022-12-21
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2719493-0
    ISSN 2296-4185
    ISSN 2296-4185
    DOI 10.3389/fbioe.2022.1073455
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Glyco-Engineering. Preface.

    Castilho, Alexandra

    Methods in molecular biology (Clifton, N.J.)

    2015  Volume 1321, Page(s) v–vii

    MeSH term(s) Animals ; Bioengineering ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Glycosylation ; Humans
    Chemical Substances Glycoproteins
    Language English
    Publishing date 2015-09-09
    Publishing country United States
    Document type Introductory Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-2760-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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  4. Article ; Online: Assessment of transient expression strategies to sialylate recombinant proteins in N. benthamiana.

    Izadi, Shiva / Kunnummel, Vinny / Steinkellner, Herta / Werner, Stefan / Castilho, Alexandra

    Journal of biotechnology

    2023  Volume 365, Page(s) 48–53

    Abstract: There is a demand for increasing the current manufacturing capacities for recombinant protein-based drugs. Novel expression systems such as plants are being explored as faster, more flexible, and possibly cheaper platforms. Many of these therapeutic ... ...

    Abstract There is a demand for increasing the current manufacturing capacities for recombinant protein-based drugs. Novel expression systems such as plants are being explored as faster, more flexible, and possibly cheaper platforms. Many of these therapeutic proteins are glycosylated and require terminal sialylation to attain full biological activity. In planta protein sialylation has been achieved by the introduction of an entire mammalian biosynthetic pathway in Nicotiana benthamiana, comprising the coordinated expression of the genes for (i) biosynthesis, (ii) activation, (iii) transport, and (iv) transfer of Neu5Ac to terminal galactose. Here we address technical issues that can compromise the efficacy of protein sialylation and how they can be overcome. We used the same reporter protein to compared three strategies to transiently deliver the sialylation pathway-genes evaluating efficacy, heterogeneity and batch-to-batch consistency. In addition, we assess the ability of the single-step method to sialylated additional recombinant proteins with different complexity and number of glycosylation sites. Finally, we show that efficient protein sialylation can be up-scaled for large-scale production of sialylated proteins in plants.
    MeSH term(s) Animals ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Glycosylation ; Plants/metabolism ; Nicotiana/genetics ; Nicotiana/metabolism ; Mammals
    Chemical Substances Recombinant Proteins
    Language English
    Publishing date 2023-02-15
    Publishing country Netherlands
    Document type Journal Article ; Review
    ZDB-ID 843647-2
    ISSN 1873-4863 ; 0168-1656 ; 1389-0352
    ISSN (online) 1873-4863
    ISSN 0168-1656 ; 1389-0352
    DOI 10.1016/j.jbiotec.2023.02.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2299: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  5. Article: Antisclerostin Effect on Osseointegration and Bone Remodeling.

    Couto, Bárbara Alexandra do Amaral / Fernandes, Juliana Campos Hasse / Saavedra-Silva, Mariana / Roca, Hernan / Castilho, Rogério Moraes / Fernandes, Gustavo Vicentis de Oliveira

    Journal of clinical medicine

    2023  Volume 12, Issue 4

    Abstract: ... ...

    Abstract Objective
    Language English
    Publishing date 2023-02-06
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2662592-1
    ISSN 2077-0383
    ISSN 2077-0383
    DOI 10.3390/jcm12041294
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Book: Glyco-engineering

    Castilho, Alexandra

    methods and protocols

    (Methods in molecular biology, ; 1321 ; Springer protocols)

    2015  

    Abstract: Conceived with the intention of providing an array of strategies and technologies currently in use for glyco-engineering distinct living organisms, this book contains a wide range of methods being developed to control the composition of carbohydrates ... ...

    Author's details edited by Alexandra Castilho
    Series title Methods in molecular biology, ; 1321
    Springer protocols
    Abstract "Conceived with the intention of providing an array of strategies and technologies currently in use for glyco-engineering distinct living organisms, this book contains a wide range of methods being developed to control the composition of carbohydrates and the properties of proteins through manipulations on the production host rather than in the protein itself. The first five sections deal with host-specific glyco-engineering and contain chapters that provide protocols for modifications of the glycosylation pathway in bacteria, yeast, insect, plants, and mammalian cells, while the last two sections explore alternative approaches to host glyco-engineering and selected protocols for the analysis of the N-glycans and glyco-profiling by mass spectrometry. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and extensive, Glyco-Engineering: Methods and Protocols offers vast options to help researchers to choose the expression system and approach that best suits their intended protein research or applications."--Back cover.
    MeSH term(s) Glycosylation ; Glycoproteins
    Language English
    Size xvi, 439 pages :, illustrations (some color) ;, 27 cm.
    Document type Book
    ISBN 9781493927593 ; 1493927590 ; 9781493927609 ; 1493927604
    Database Catalogue of the US National Library of Medicine (NLM)

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    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  7. Book: Glyco-engineering

    Castilho, Alexandra

    methods and protocols

    (Methods in molecular biology, ; 1321 ; Springer protocols)

    2015  

    Abstract: Conceived with the intention of providing an array of strategies and technologies currently in use for glyco-engineering distinct living organisms, this book contains a wide range of methods being developed to control the composition of carbohydrates ... ...

    Author's details edited by Alexandra Castilho
    Series title Methods in molecular biology, ; 1321
    Springer protocols
    Abstract "Conceived with the intention of providing an array of strategies and technologies currently in use for glyco-engineering distinct living organisms, this book contains a wide range of methods being developed to control the composition of carbohydrates and the properties of proteins through manipulations on the production host rather than in the protein itself. The first five sections deal with host-specific glyco-engineering and contain chapters that provide protocols for modifications of the glycosylation pathway in bacteria, yeast, insect, plants, and mammalian cells, while the last two sections explore alternative approaches to host glyco-engineering and selected protocols for the analysis of the N-glycans and glyco-profiling by mass spectrometry. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and extensive, Glyco-Engineering: Methods and Protocols offers vast options to help researchers to choose the expression system and approach that best suits their intended protein research or applications."--Back cover.
    Keywords Glycosylation ; Glycosylation. ; glycosylation ; glycoproteins
    Language English
    Size xvi, 439 pages :, illustrations (some color) ;, 27 cm.
    Document type Book
    ISBN 9781493927593 ; 1493927590 ; 9781493927609 ; 1493927604
    Database NAL-Catalogue (AGRICOLA)

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  8. Article: The tobacco GNTI stem region harbors a strong motif for homomeric protein complex formation.

    Schoberer, Jennifer / Izadi, Shiva / Kierein, Carolina / Vavra, Ulrike / König-Beihammer, Julia / Ruocco, Valentina / Grünwald-Gruber, Clemens / Castilho, Alexandra / Strasser, Richard

    Frontiers in plant science

    2023  Volume 14, Page(s) 1320051

    Abstract: Introduction: The Golgi apparatus of plants is the central cellular organelle for glycan processing and polysaccharide biosynthesis. These essential processes are catalyzed by a large number of Golgi-resident glycosyltransferases and glycosidases whose ... ...

    Abstract Introduction: The Golgi apparatus of plants is the central cellular organelle for glycan processing and polysaccharide biosynthesis. These essential processes are catalyzed by a large number of Golgi-resident glycosyltransferases and glycosidases whose organization within the Golgi is still poorly understood.
    Methods: Here, we examined the role of the stem region of the
    Results: Transient expression of the N-terminal cytoplasmic, transmembrane, and stem (CTS) regions of GNTI leads to a block in N-glycan processing on a co-expressed recombinant glycoprotein. Overexpression of the CTS region from Golgi α-mannosidase I, which can form
    Discussion: Taken together, we have identified a conserved motif in the stem region of the key N-glycan processing enzyme GNTI. We propose that the identified sequence motif in the GNTI stem region acts as a dominant negative motif that can be used in transient glycoengineering approaches to produce recombinant glycoproteins with predominantly mannosidic N-glycans.
    Language English
    Publishing date 2023-11-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2613694-6
    ISSN 1664-462X
    ISSN 1664-462X
    DOI 10.3389/fpls.2023.1320051
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Reteplase Fc-fusions produced in N. benthamiana are able to dissolve blood clots ex vivo.

    Izadi, Shiva / Jalali Javaran, Mokhtar / Rashidi Monfared, Sajad / Castilho, Alexandra

    PloS one

    2021  Volume 16, Issue 11, Page(s) e0260796

    Abstract: Thrombolytic and fibrinolytic therapies are effective treatments to dissolve blood clots in stroke therapy. Thrombolytic drugs activate plasminogen to its cleaved form plasmin, a proteolytic enzyme that breaks the crosslinks between fibrin molecules. The ...

    Abstract Thrombolytic and fibrinolytic therapies are effective treatments to dissolve blood clots in stroke therapy. Thrombolytic drugs activate plasminogen to its cleaved form plasmin, a proteolytic enzyme that breaks the crosslinks between fibrin molecules. The FDA-approved human tissue plasminogen activator Reteplase (rPA) is a non-glycosylated protein produced in E. coli. rPA is a deletion mutant of the wild-type Alteplase that benefits from an extended plasma half-life, reduced fibrin specificity and the ability to better penetrate into blood clots. Different methods have been proposed to improve the production of rPA. Here we show for the first time the transient expression in Nicotiana benthamiana of rPA fused to the immunoglobulin fragment crystallizable (Fc) domain on an IgG1, a strategy commonly used to improve the stability of therapeutic proteins. Despite our success on the expression and purification of dimeric rPA-Fc fusions, protein instability results in high amounts of Fc-derived degradation products. We hypothesize that the "Y"- shape of dimeric Fc fusions cause steric hindrance between protein domains and leads to physical instability. Indeed, mutations of critical residues in the Fc dimerization interface allowed the expression of fully stable rPA monomeric Fc-fusions. The ability of rPA-Fc to convert plasminogen into plasmin was demonstrated by plasminogen zymography and clot lysis assay shows that rPA-Fc is able to dissolve blood clots ex vivo. Finally, we addressed concerns with the plant-specific glycosylation by modulating rPA-Fc glycosylation towards serum-like structures including α2,6-sialylated and α1,6-core fucosylated N-glycans completely devoid of plant core fucose and xylose residues.
    MeSH term(s) Fibrinolysis/drug effects ; Fibrinolytic Agents/chemistry ; Fibrinolytic Agents/pharmacology ; Humans ; Immunoglobulin Fc Fragments/biosynthesis ; Immunoglobulin Fc Fragments/chemistry ; Immunoglobulin Fc Fragments/genetics ; Immunoglobulin Fc Fragments/pharmacology ; Recombinant Fusion Proteins/biosynthesis ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/pharmacology ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/pharmacology ; Tissue Plasminogen Activator/biosynthesis ; Tissue Plasminogen Activator/chemistry ; Tissue Plasminogen Activator/genetics ; Tissue Plasminogen Activator/pharmacology ; Nicotiana/genetics ; Nicotiana/metabolism
    Chemical Substances Fibrinolytic Agents ; Immunoglobulin Fc Fragments ; Recombinant Fusion Proteins ; Recombinant Proteins ; reteplase (DQA630RIE9) ; Tissue Plasminogen Activator (EC 3.4.21.68)
    Language English
    Publishing date 2021-11-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0260796
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: The Instability of Dimeric Fc-Fusions Expressed in Plants Can Be Solved by Monomeric Fc Technology.

    Gattinger, Pia / Izadi, Shiva / Grünwald-Gruber, Clemens / Kallolimath, Somanath / Castilho, Alexandra

    Frontiers in plant science

    2021  Volume 12, Page(s) 671728

    Abstract: The potential therapeutic value of many proteins is ultimately limited by their ... ...

    Abstract The potential therapeutic value of many proteins is ultimately limited by their rapid
    Language English
    Publishing date 2021-07-09
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2613694-6
    ISSN 1664-462X
    ISSN 1664-462X
    DOI 10.3389/fpls.2021.671728
    Database MEDical Literature Analysis and Retrieval System OnLINE

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