A comparison of assays for the response of primary human T-cells upon stimulation with interleukin-2, interleukin-4 and interleukin-7
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: In: Eur. Cytokine Netw, 1992, 3, 2, S. 97-102
- Keyword
-
T-Lymphozyt
Interleukin 2
Interleukin 4
Interleukin 7
Immunologie
Immunsystem
Lymphozyt
Leukozyt
Immunität
Resistenz
Immunchemie
- Event
-
Veröffentlichung
- (where)
-
Würzburg
- (who)
-
Universität Würzburg
- (when)
-
2013
- Creator
-
Duschl, Albert
Jahn, Ute
Bertling, Claudia
Sebald, Walter
- URN
-
urn:nbn:de:bvb:20-opus-86750
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:59 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Duschl, Albert
- Jahn, Ute
- Bertling, Claudia
- Sebald, Walter
- Universität Würzburg
Time of origin
- 2013
Other Objects (12)
Design of human interleukin-4 antagonists inhibiting interleukin-4-dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency
Interleukin 4 drives phytohemagglutinin-activated T cells through several cell cycles: no synergism between interleukin 2 and interleukin 4
Interleukin 7 as interleukin 9 drives phytohemagglutinin-activated T cells through several cell cycles; no synergism between interleukin 7, interleukin 9 and interleukin 4
Mutant proteins of human interleukin 2. Renaturation yield, proliferative activity and receptor binding
Zur mitochondrialen Proteinsynthese : Über d. Einbau v. Aminosäuren in Mitochondrien aus d. Flugmuskel d. Wanderheuschrecke u. aus d. Wildtyp u. d. cytoplasmat. Mutante mi-1 v. Neurospora crassa in vitro und in vivo unter d. Wirkg v. Cycloheximid
Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement
Site-directed mutagenesis reveals the importance of disulfide bridges and aromatic residues for structure and proliferative activity of human interleukin-4
Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy
Neutralizing monoclonal antibodies define two different functional sites in human interleukin-4
Isolation of a functional human interleukin 2 gene from a cosmid library by recombination in vivo
Biogenesis of mitochondrial ATPase
Two distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation
Design of human interleukin-4 antagonists inhibiting interleukin-4-dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency
Interleukin 4 drives phytohemagglutinin-activated T cells through several cell cycles: no synergism between interleukin 2 and interleukin 4
Interleukin 7 as interleukin 9 drives phytohemagglutinin-activated T cells through several cell cycles; no synergism between interleukin 7, interleukin 9 and interleukin 4
Mutant proteins of human interleukin 2. Renaturation yield, proliferative activity and receptor binding
Zur mitochondrialen Proteinsynthese : Über d. Einbau v. Aminosäuren in Mitochondrien aus d. Flugmuskel d. Wanderheuschrecke u. aus d. Wildtyp u. d. cytoplasmat. Mutante mi-1 v. Neurospora crassa in vitro und in vivo unter d. Wirkg v. Cycloheximid
Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement
Site-directed mutagenesis reveals the importance of disulfide bridges and aromatic residues for structure and proliferative activity of human interleukin-4
Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy
Neutralizing monoclonal antibodies define two different functional sites in human interleukin-4
Isolation of a functional human interleukin 2 gene from a cosmid library by recombination in vivo
Biogenesis of mitochondrial ATPase
Two distinct functional sites of human interleukin 4 are identified by variants impaired in either receptor binding or receptor activation
Design of human interleukin-4 antagonists inhibiting interleukin-4-dependent and interleukin-13-dependent responses in T-cells and B-cells with high efficiency
Interleukin 4 drives phytohemagglutinin-activated T cells through several cell cycles: no synergism between interleukin 2 and interleukin 4
Interleukin 7 as interleukin 9 drives phytohemagglutinin-activated T cells through several cell cycles; no synergism between interleukin 7, interleukin 9 and interleukin 4
Mutant proteins of human interleukin 2. Renaturation yield, proliferative activity and receptor binding
Zur mitochondrialen Proteinsynthese : Über d. Einbau v. Aminosäuren in Mitochondrien aus d. Flugmuskel d. Wanderheuschrecke u. aus d. Wildtyp u. d. cytoplasmat. Mutante mi-1 v. Neurospora crassa in vitro und in vivo unter d. Wirkg v. Cycloheximid
Conversion of human interleukin-4 into a high affinity antagonist by a single amino acid replacement
Site-directed mutagenesis reveals the importance of disulfide bridges and aromatic residues for structure and proliferative activity of human interleukin-4
Aspects of receptor binding and signalling of interleukin-4 investigated by site-directed mutagenesis and NMR spectroscopy
Neutralizing monoclonal antibodies define two different functional sites in human interleukin-4
Isolation of a functional human interleukin 2 gene from a cosmid library by recombination in vivo
Biogenesis of mitochondrial ATPase