Tissue transglutaminase treatment leads to concentration-dependent changes in dendritic cell phenotype - implications for the role of transglutaminase in coeliac disease
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1471-2172
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Tissue transglutaminase treatment leads to concentration-dependent changes in dendritic cell phenotype - implications for the role of transglutaminase in coeliac disease ; volume:13 ; number:1 ; day:16 ; month:4 ; year:2012 ; pages:1-10 ; date:12.2012
BMC immunology ; 13, Heft 1 (16.4.2012), 1-10, 12.2012
- Creator
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Dalleywater, William J.
Chau, David YS
Ghaemmaghami, Amir M.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1186/1471-2172-13-20
- URN
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urn:nbn:de:101:1-2021080920362435553710
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:55 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
- Dalleywater, William J.
- Chau, David YS
- Ghaemmaghami, Amir M.
- SpringerLink (Online service)
Other Objects (12)
Transglutaminase-induzierte und Transglutaminase-unterstützte Gele aus Milchproteinen
Do cultured human skin explants elaborate coeliac antigen, possibly even Tissue-Transglutaminase?
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Einsatz der human rekombinanten Transglutaminase für die Bestimmung der Transglutaminase-Antikörper in der Zöliakiediagnostik
Transglutaminase Type 2-MITF axis regulates phenotype switching in skin cutaneous melanoma
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Demonstration of Transglutaminase Activity in Limulus Lysate
Optimierung einer mikrobiellen Transglutaminase mittels Random-Mutagenese
Transglutaminase 2 and Ferroptosis: a new liaison?
Transglutaminase-mediierte Serotonylierung neuronaler und glialer Proteine
Correction to: Separate Gut Plasma Cell Populations Produce Auto‐Antibodies against Transglutaminase 2 and Transglutaminase 3 in Dermatitis Herpetiformis
Transglutaminase-induzierte und Transglutaminase-unterstützte Gele aus Milchproteinen
Do cultured human skin explants elaborate coeliac antigen, possibly even Tissue-Transglutaminase?
Cross-linking with microbial transglutaminase
Einsatz der human rekombinanten Transglutaminase für die Bestimmung der Transglutaminase-Antikörper in der Zöliakiediagnostik
Transglutaminase Type 2-MITF axis regulates phenotype switching in skin cutaneous melanoma
Separate Gut Plasma Cell Populations Produce Auto‐Antibodies against Transglutaminase 2 and Transglutaminase 3 in Dermatitis Herpetiformis
Transglutaminase-mediierte Serotonylierung neuronaler und glialer Proteine
Demonstration of Transglutaminase Activity in Limulus Lysate
Optimierung einer mikrobiellen Transglutaminase mittels Random-Mutagenese
Transglutaminase 2 and Ferroptosis: a new liaison?
Transglutaminase-mediierte Serotonylierung neuronaler und glialer Proteine
Correction to: Separate Gut Plasma Cell Populations Produce Auto‐Antibodies against Transglutaminase 2 and Transglutaminase 3 in Dermatitis Herpetiformis
Transglutaminase-induzierte und Transglutaminase-unterstützte Gele aus Milchproteinen
Do cultured human skin explants elaborate coeliac antigen, possibly even Tissue-Transglutaminase?
Cross-linking with microbial transglutaminase
Einsatz der human rekombinanten Transglutaminase für die Bestimmung der Transglutaminase-Antikörper in der Zöliakiediagnostik
Transglutaminase Type 2-MITF axis regulates phenotype switching in skin cutaneous melanoma
Separate Gut Plasma Cell Populations Produce Auto‐Antibodies against Transglutaminase 2 and Transglutaminase 3 in Dermatitis Herpetiformis
Transglutaminase-mediierte Serotonylierung neuronaler und glialer Proteine
Demonstration of Transglutaminase Activity in Limulus Lysate
Optimierung einer mikrobiellen Transglutaminase mittels Random-Mutagenese
Transglutaminase 2 and Ferroptosis: a new liaison?
Transglutaminase-mediierte Serotonylierung neuronaler und glialer Proteine