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  1. Book: Tag based next generation sequencing

    Harbers, Matthias / Kahl, Günter

    2012  

    Title variant Tag-based next generation sequencing
    Author's details ed. by Matthias Harbers and Günter Kahl
    Keywords Sequenzanalyse
    Subject Chemische Analyse ; Sequenzierung
    Language English
    Size XXV, 581 S. : Ill., graph. Darst., 240 mm x 170 mm
    Publisher Wiley-Blackwell
    Publishing place Weinheim u.a.
    Publishing country Germany
    Document type Book
    HBZ-ID HT016988286
    ISBN 978-3-527-32819-2 ; 3-527-32819-X ; 9783527644575 ; 9783527644582 ; 9783527644773 ; 3527644571 ; 352764458X ; 3527644776
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2012 A 117 order for loan Magazin

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  2. Article ; Online: Shift-Western Blotting: Separate Analysis of Protein and DNA from Protein-DNA Complexes.

    Harbers, Matthias

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

    2015  Volume 1312, Page(s) 355–373

    Abstract: The electrophoretic mobility shift assay (EMSA) is the most frequently used experiment for studying protein-DNA interactions and to identify DNA-binding proteins. Protein-DNA complexes formed during EMSA experiments can be further analyzed by shift- ... ...

    Abstract The electrophoretic mobility shift assay (EMSA) is the most frequently used experiment for studying protein-DNA interactions and to identify DNA-binding proteins. Protein-DNA complexes formed during EMSA experiments can be further analyzed by shift-western blotting, where the protein and DNA components contained in a polyacrylamide gel are transferred to stacked membranes: First a nitrocellulose membrane retains the proteins while double-stranded DNA passes through the nitrocellulose membrane and binds only to a charged membrane placed below. Immobilized proteins can then be stained with specific antibodies while the DNA can be detected by a radioactive label or a nonradioactive detection system. Shift-western blotting can overcome many limitations of supershift experiments and allows for the analysis of complex protein-DNA complexes containing multiple protein factors. Moreover, proteins and/or DNA may be recovered from membranes after the blotting step for further analysis by other means.
    MeSH term(s) Animals ; Blotting, Western/methods ; Cattle ; Cell Line ; DNA/chemistry ; DNA/isolation & purification ; DNA/metabolism ; DNA Probes/chemistry ; DNA-Binding Proteins/isolation & purification ; DNA-Binding Proteins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Electrophoretic Mobility Shift Assay/methods ; Humans ; Mice ; Rats
    Chemical Substances DNA Probes ; DNA-Binding Proteins ; DNA (9007-49-2)
    Language English
    Publishing date 2015
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-2694-7_36
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Wheat germ systems for cell-free protein expression.

    Harbers, Matthias

    FEBS letters

    2014  Volume 588, Issue 17, Page(s) 2762–2773

    Abstract: Cell-free protein expression plays an important role in biochemical research. However, only recent developments led to new methods to rapidly synthesize preparative amounts of protein that make cell-free protein expression an attractive alternative to ... ...

    Abstract Cell-free protein expression plays an important role in biochemical research. However, only recent developments led to new methods to rapidly synthesize preparative amounts of protein that make cell-free protein expression an attractive alternative to cell-based methods. In particular the wheat germ system provides the highest translation efficiency among eukaryotic cell-free protein expression approaches and has a very high success rate for the expression of soluble proteins of good quality. As an open in vitro method, the wheat germ system is a preferable choice for many applications in protein research including options for protein labeling and the expression of difficult-to-express proteins like membrane proteins and multiple protein complexes. Here I describe wheat germ cell-free protein expression systems and give examples how they have been used in genome-wide expression studies, preparation of labeled proteins for structural genomics and protein mass spectroscopy, automated protein synthesis, and screening of enzymatic activities. Future directions for the use of cell-free expression methods are discussed.
    MeSH term(s) Animals ; Cell-Free System ; Humans ; Protein Biosynthesis ; Robotics ; Triticum/chemistry ; Triticum/metabolism
    Language English
    Publishing date 2014-08-25
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2014.05.061
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: Wheat germ systems for cell-free protein expression

    Harbers, Matthias

    Federation of European Biochemical Societies FEBS letters. 2014 Aug. 25, v. 588, no. 17

    2014  

    Abstract: Cell-free protein expression plays an important role in biochemical research. However, only recent developments led to new methods to rapidly synthesize preparative amounts of protein that make cell-free protein expression an attractive alternative to ... ...

    Abstract Cell-free protein expression plays an important role in biochemical research. However, only recent developments led to new methods to rapidly synthesize preparative amounts of protein that make cell-free protein expression an attractive alternative to cell-based methods. In particular the wheat germ system provides the highest translation efficiency among eukaryotic cell-free protein expression approaches and has a very high success rate for the expression of soluble proteins of good quality. As an open in vitro method, the wheat germ system is a preferable choice for many applications in protein research including options for protein labeling and the expression of difficult-to-express proteins like membrane proteins and multiple protein complexes. Here I describe wheat germ cell-free protein expression systems and give examples how they have been used in genome-wide expression studies, preparation of labeled proteins for structural genomics and protein mass spectroscopy, automated protein synthesis, and screening of enzymatic activities. Future directions for the use of cell-free expression methods are discussed.
    Keywords cell-free protein synthesis ; enzyme activity ; genomics ; in vitro studies ; mass spectrometry ; membrane proteins ; screening ; structural proteins ; wheat germ
    Language English
    Dates of publication 2014-0825
    Size p. 2762-2773.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2014.05.061
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/702: Show issues
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  5. Article: Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology.

    Fogeron, Marie-Laure / Lecoq, Lauriane / Cole, Laura / Harbers, Matthias / Böckmann, Anja

    Frontiers in molecular biosciences

    2021  Volume 8, Page(s) 639587

    Abstract: Cell-free protein synthesis (CFPS) systems are gaining more importance as universal tools for basic research, applied sciences, and product development with new technologies emerging for their application. Huge progress was made in the field of synthetic ...

    Abstract Cell-free protein synthesis (CFPS) systems are gaining more importance as universal tools for basic research, applied sciences, and product development with new technologies emerging for their application. Huge progress was made in the field of synthetic biology using CFPS to develop new proteins for technical applications and therapy. Out of the available CFPS systems, wheat germ cell-free protein synthesis (WG-CFPS) merges the highest yields with the use of a eukaryotic ribosome, making it an excellent approach for the synthesis of complex eukaryotic proteins including, for example, protein complexes and membrane proteins. Separating the translation reaction from other cellular processes, CFPS offers a flexible means to adapt translation reactions to protein needs. There is a large demand for such potent, easy-to-use, rapid protein expression systems, which are optimally serving protein requirements to drive biochemical and structural biology research. We summarize here a general workflow for a wheat germ system providing examples from the literature, as well as applications used for our own studies in structural biology. With this review, we want to highlight the tremendous potential of the rapidly evolving and highly versatile CFPS systems, making them more widely used as common tools to recombinantly prepare particularly challenging recombinant eukaryotic proteins.
    Language English
    Publishing date 2021-03-25
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2814330-9
    ISSN 2296-889X
    ISSN 2296-889X
    DOI 10.3389/fmolb.2021.639587
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The current status of cDNA cloning.

    Harbers, Matthias

    Genomics

    2008  Volume 91, Issue 3, Page(s) 232–242

    Abstract: The cloning of cDNAs, copies of cellular RNA, is one of the classical technologies in molecular biology. Over the past 30 years cDNA cloning technologies have been improved to enable the cloning of large cDNA collections, which are fundamental to today's ...

    Abstract The cloning of cDNAs, copies of cellular RNA, is one of the classical technologies in molecular biology. Over the past 30 years cDNA cloning technologies have been improved to enable the cloning of large cDNA collections, which are fundamental to today's understanding of the utilization of genetic information. With the discovery of noncoding RNAs, additional new approaches to the cloning of short RNAs have been developed. However, with the realization that much larger portions of genomes are transcribed than anticipated from genome annotations, cDNA cloning faces new challenges to uncover rare transcripts and to make the corresponding cDNAs available for functional studies. This review provides an overview on the current status of cDNA cloning and possibilities for the discovery and characterization of new RNA families.
    MeSH term(s) Animals ; Cloning, Molecular/methods ; DNA, Complementary/genetics ; Databases, Nucleic Acid ; Gene Library ; Genetic Techniques/trends ; Genetic Vectors ; Humans ; RNA/genetics ; RNA Splicing
    Chemical Substances DNA, Complementary ; RNA (63231-63-0)
    Language English
    Publishing date 2008-03
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 356334-0
    ISSN 1089-8646 ; 0888-7543
    ISSN (online) 1089-8646
    ISSN 0888-7543
    DOI 10.1016/j.ygeno.2007.11.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2367: 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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  7. Article ; Online: Easy Synthesis of Complex Biomolecular Assemblies

    Marie-Laure Fogeron / Lauriane Lecoq / Laura Cole / Matthias Harbers / Anja Böckmann

    Frontiers in Molecular Biosciences, Vol

    Wheat Germ Cell-Free Protein Expression in Structural Biology

    2021  Volume 8

    Abstract: Cell-free protein synthesis (CFPS) systems are gaining more importance as universal tools for basic research, applied sciences, and product development with new technologies emerging for their application. Huge progress was made in the field of synthetic ...

    Abstract Cell-free protein synthesis (CFPS) systems are gaining more importance as universal tools for basic research, applied sciences, and product development with new technologies emerging for their application. Huge progress was made in the field of synthetic biology using CFPS to develop new proteins for technical applications and therapy. Out of the available CFPS systems, wheat germ cell-free protein synthesis (WG-CFPS) merges the highest yields with the use of a eukaryotic ribosome, making it an excellent approach for the synthesis of complex eukaryotic proteins including, for example, protein complexes and membrane proteins. Separating the translation reaction from other cellular processes, CFPS offers a flexible means to adapt translation reactions to protein needs. There is a large demand for such potent, easy-to-use, rapid protein expression systems, which are optimally serving protein requirements to drive biochemical and structural biology research. We summarize here a general workflow for a wheat germ system providing examples from the literature, as well as applications used for our own studies in structural biology. With this review, we want to highlight the tremendous potential of the rapidly evolving and highly versatile CFPS systems, making them more widely used as common tools to recombinantly prepare particularly challenging recombinant eukaryotic proteins.
    Keywords cell-free protein expression ; wheat germ ; structural biology ; NMR ; labeling ; Biology (General) ; QH301-705.5
    Subject code 612
    Language English
    Publishing date 2021-03-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Assessment of IgG3 as a serological exposure marker for

    Tayipto, Yanie / Rosado, Jason / Gamboa, Dionicia / White, Michael T / Kiniboro, Benson / Healer, Julie / Opi, D Herbert / Beeson, James G / Takashima, Eizo / Tsuboi, Takafumi / Harbers, Matthias / Robinson, Leanne / Mueller, Ivo / Longley, Rhea J

    Frontiers in cellular and infection microbiology

    2022  Volume 12, Page(s) 950909

    Abstract: A more sensitive surveillance tool is needed to ... ...

    Abstract A more sensitive surveillance tool is needed to identify
    MeSH term(s) Adolescent ; Adult ; Aged ; Aged, 80 and over ; Antibodies, Protozoan ; Asymptomatic Infections ; Biomarkers ; Child ; Child, Preschool ; Humans ; Immunoglobulin G ; Immunoglobulin M ; Malaria ; Malaria, Falciparum ; Malaria, Vivax/diagnosis ; Middle Aged ; Plasmodium falciparum ; Plasmodium vivax ; Young Adult
    Chemical Substances Antibodies, Protozoan ; Biomarkers ; Immunoglobulin G ; Immunoglobulin M
    Language English
    Publishing date 2022-08-09
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2022.950909
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Book: Tag-based next generation sequencing

    Harbers, Matthias / Kahl, Günter

    2012  

    Author's details edited by Matthias Harbers and Günter Kahl
    MeSH term(s) Sequence Analysis, DNA/methods ; Chromosome Mapping/methods ; Genomics/methods ; Sequence Tagged Sites
    Language English
    Size xxv, 581 p. :, ill.
    Publisher Wiley-Blackwell
    Publishing place Weinheim
    Document type Book
    ISBN 9783527328192 ; 9783527644773 ; 9783527644582 ; 9783527644575 ; 352732819X ; 3527644776 ; 352764458X ; 3527644571
    Database Catalogue of the US National Library of Medicine (NLM)

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  10. Article ; Online: Naturally acquired antibody kinetics against Plasmodium vivax antigens in people from a low malaria transmission region in western Thailand.

    Liu, Zoe Shih-Jung / Sattabongkot, Jetsumon / White, Michael / Chotirat, Sadudee / Kumpitak, Chalermpon / Takashima, Eizo / Harbers, Matthias / Tham, Wai-Hong / Healer, Julie / Chitnis, Chetan E / Tsuboi, Takafumi / Mueller, Ivo / Longley, Rhea J

    BMC medicine

    2022  Volume 20, Issue 1, Page(s) 89

    Abstract: Background: Plasmodium vivax (P. vivax) is the dominant Plasmodium spp. causing the disease malaria in low-transmission regions outside of Africa. These regions often feature high proportions of asymptomatic patients with sub-microscopic parasitaemia ... ...

    Abstract Background: Plasmodium vivax (P. vivax) is the dominant Plasmodium spp. causing the disease malaria in low-transmission regions outside of Africa. These regions often feature high proportions of asymptomatic patients with sub-microscopic parasitaemia and relapses. Naturally acquired antibody responses are induced after Plasmodium infection, providing partial protection against high parasitaemia and clinical episodes. However, previous work has failed to address the presence and maintenance of such antibody responses to P. vivax particularly in low-transmission regions.
    Methods: We followed 34 patients in western Thailand after symptomatic P. vivax infections to monitor antibody kinetics over 9 months, during which no recurrent infections occurred. We assessed total IgG, IgG subclass and IgM levels to up to 52 P. vivax proteins every 2-4 weeks using a multiplexed Luminex® assay and identified protein-specific variation in antibody longevity. Mathematical modelling was used to generate the estimated half-life of antibodies, long-, and short-lived antibody-secreting cells.
    Results: Generally, an increase in antibody level was observed within 1-week post symptomatic infection, followed by an exponential decay of different rates. We observed mostly IgG1 dominance and IgG3 sub-dominance in this population. IgM responses followed similar kinetic patterns to IgG, with some proteins unexpectedly inducing long-lived IgM responses. We also monitored antibody responses against 27 IgG-immunogenic antigens in 30 asymptomatic individuals from a similar region. Our results demonstrate that most antigens induced robust and long-lived total IgG responses following asymptomatic infections in the absence of (detected) boosting infections.
    Conclusions: Our work provides new insights into the development and maintenance of naturally acquired immunity to P. vivax and will guide the potential use of serology to indicate immune status and/or identify populations at risk.
    MeSH term(s) Antibodies, Protozoan ; Antigens, Protozoan ; Humans ; Kinetics ; Malaria ; Malaria, Vivax/epidemiology ; Plasmodium vivax ; Protozoan Proteins ; Thailand/epidemiology
    Chemical Substances Antibodies, Protozoan ; Antigens, Protozoan ; Protozoan Proteins
    Language English
    Publishing date 2022-03-09
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2131669-7
    ISSN 1741-7015 ; 1741-7015
    ISSN (online) 1741-7015
    ISSN 1741-7015
    DOI 10.1186/s12916-022-02281-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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