Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Elisabeth, Lobner"'
Autor:
Benjamin Salzer, Christina M. Schueller, Charlotte U. Zajc, Timo Peters, Michael A. Schoeber, Boris Kovacic, Michelle C. Buri, Elisabeth Lobner, Omer Dushek, Johannes B. Huppa, Christian Obinger, Eva M. Putz, Wolfgang Holter, Michael W. Traxlmayr, Manfred Lehner
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
The lack of tumour-specific antigens and control over T-cell activity limits the development of CAR-T cell therapies for solid tumours. Here the authors present an avidity-controlled CAR platform with inducible logic control functions.
Externí odkaz:
https://doaj.org/article/8783689044924d8ba5fdd958f3eeabd4
Autor:
Elisabeth Lobner, Anna Wachernig, Venugopal Gudipati, Patrick Mayrhofer, Benjamin Salzer, Manfred Lehner, Johannes B. Huppa, Renate Kunert
Publikováno v:
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
The transmembrane protein CD19 is exclusively expressed on normal and malignant B cells and therefore constitutes the target of approved CAR-T cell-based cancer immunotherapies. Current efforts to assess CAR-T cell functionality in a quantitative fas
Externí odkaz:
https://doaj.org/article/0f365f4fccb444509b2ae58a3233f0cf
Autor:
Michael W. Traxlmayr, Omer Dushek, Eva Maria Putz, Benjamin Salzer, Johannes B. Huppa, Elisabeth Lobner, Michelle C. Buri, Manfred Lehner, Boris Kovacic, Michael A. Schoeber, Wolfgang Holter, Timo Peters, Christian Obinger, Charlotte U. Zajc, Christina M. Schueller
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
Nature Communications
Nature Communications
T cells engineered to express chimeric antigen receptors (CAR-T cells) have shown impressive clinical efficacy in the treatment of B cell malignancies. However, the development of CAR-T cell therapies for solid tumors is hampered by the lack of truly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f1d784a2a9d6ad0bced733c7e14ec9f
http://link.springer.com/article/10.1038/s41467-020-17970-3
http://link.springer.com/article/10.1038/s41467-020-17970-3
Autor:
Konstantin Kubinger, Elisabeth Lobner, Michael Kitzmüller, Georg Mlynek, Michael W. Traxlmayr, Anne-Sophie Humm, Christian Obinger, Kristina Djinović-Carugo
Publikováno v:
'mAbs ', vol: 9, pages: 1088-1104 (2017)
mAbs
mAbs
Fcabs (Fc domain with antigen-binding sites) are promising novel therapeutics. By engineering of the C-terminal loops of the CH3 domains, 2 antigen binding sites can be inserted in close proximity. To elucidate the binding mode(s) between homodimeric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2545e46b9596cd5d6b42b75b68ea6352
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:48462
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:48462
Autor:
Elisabeth Lobner, Anna Wachernig, Venugopal Gudipati, Patrick Mayrhofer, Benjamin Salzer, Manfred Lehner, Johannes B. Huppa, Renate Kunert
Publikováno v:
Frontiers in Bioengineering and Biotechnology
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
The transmembrane protein CD19 is exclusively expressed on normal and malignant B cells and therefore constitutes the target of approved CAR-T cell-based cancer immunotherapies. Current efforts to assess CAR-T cell functionality in a quantitative fas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::54300477b88fc4eb7332bd0239fddd00
https://pubmed.ncbi.nlm.nih.gov/32117929
https://pubmed.ncbi.nlm.nih.gov/32117929
Autor:
Alejandro A, Puchol Tarazona, Elisabeth, Lobner, Yvonne, Taubenschmid, Melanie, Paireder, Juan A, Torres Acosta, Kathrin, Göritzer, Herta, Steinkellner, Lukas, Mach
Publikováno v:
Biotechnology journal. 15(3)
Broadly neutralizing antibodies (bNAbs) to human immunodeficiency virus type 1 (HIV-1) hold great promise for immunoprophylaxis and the suppression of viremia in HIV-positive individuals. Several studies have demonstrated that plants as Nicotiana ben
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::760465863d5029cc2b6213ad651f9468
https://pubmed.ncbi.nlm.nih.gov/31657528
https://pubmed.ncbi.nlm.nih.gov/31657528
Autor:
Venugopal, Gudipati, Julian, Rydzek, Iago, Doel-Perez, Vasco Dos Reis, Gonçalves, Lydia, Scharf, Sebastian, Königsberger, Elisabeth, Lobner, Renate, Kunert, Hermann, Einsele, Hannes, Stockinger, Michael, Hudecek, Johannes B, Huppa
Publikováno v:
Nature immunology. 21(8)
Rational design of chimeric antigen receptors (CARs) with optimized anticancer performance mandates detailed knowledge of how CARs engage tumor antigens and how antigen engagement triggers activation. We analyzed CAR-mediated antigen recognition via
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::141087fba08d797158b1de20fd4ad780
https://pubmed.ncbi.nlm.nih.gov/32632290
https://pubmed.ncbi.nlm.nih.gov/32632290
Autor:
Florian Rüker, Christoph Hasenhindl, Elisabeth Lobner, Michael W. Traxlmayr, Kristina Djinović-Carugo, Christian Obinger, Georg Mlynek, Martin Puchinger, Anne-Sophie Humm, Kathrin Göritzer
Publikováno v:
Structure (London, England : 1993). 25(6)
The crystallizable fragment (Fc) of the immunoglobulin class G (IgG) is an attractive scaffold for the design of novel therapeutics. Upon engineering the C-terminal loops in the CH3 domains, Fcabs (Fc domain with antigen-binding sites) can be designe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61f71a2e33965160d8233ceb7400064d
https://pubmed.ncbi.nlm.nih.gov/28528777
https://pubmed.ncbi.nlm.nih.gov/28528777
Autor:
Kevin Moulder, Max Woisetschläger, Michael W. Traxlmayr, Manuela Kainer, Christian Obinger, Susanne Wiederkum, Gerhard Stadlmayr, Elisabeth Lobner, Christoph Hasenhindl, Florian Rüker, Bernhard Antes
Publikováno v:
Protein Engineering, Design and Selection. 26:255-265
An Fcab (Fc antigen binding) is a crystallizable fragment of IgG having C-terminal structural loops of CH3 domains engineered for antigen binding. Since introduction of novel binding sites might impair the immunoglobulin fold, repairing strategies ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99b93198e9c9c0e25b2aa338b9621b45
https://doi.org/10.1093/protein/gzs102
https://doi.org/10.1093/protein/gzs102
Autor:
Michael W, Traxlmayr, Jonathan D, Kiefer, Raja R, Srinivas, Elisabeth, Lobner, Alison W, Tisdale, Naveen K, Mehta, Nicole J, Yang, Bruce, Tidor, K Dane, Wittrup
Publikováno v:
The Journal of Biological Chemistry
The Sso7d protein from the hyperthermophilic archaeon Sulfolobus solfataricus is an attractive binding scaffold because of its small size (7 kDa), high thermal stability (Tm of 98 °C), and absence of cysteines and glycosylation sites. However, as a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::68477d6ad9e92e617299c2d203c4b50d
https://pubmed.ncbi.nlm.nih.gov/27582495
https://pubmed.ncbi.nlm.nih.gov/27582495