- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: Frontiers in immunology, 13 (2022), 930882. https://doi.org/10.3389/fimmu.2022.930882. ISSN: 1664-3224
In: Frontiers in immunology
In: 13
In: 1664-3224
- Ereignis
-
Veröffentlichung
- (wo)
-
Hohenheim
- (wer)
-
Universität Hohenheim
- (wann)
-
2022
- Urheber
- DOI
-
10.3389/fimmu.2022.930882
- URN
-
urn:nbn:de:101:1-2503120127145.663394096355
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:32 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Kienes, Ioannis
- Johnston, Ella L.
- Bitto, Natalie J.
- Kaparakis-Liaskos, Maria
- Kufer, Thomas A.
- Universität Hohenheim
Entstanden
- 2022
Ähnliche Objekte (12)
Screening for components involved in NLR-mediated immune signalling
Diversification of molecular pattern recognition in bacterial NLR-like proteins
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity
Subversion of dendritic cell functions by bacterial pathogens
Structural basis of NLR activation and innate immune signalling in plants
Biochemical Basis of Autoactivity of a Pair of Plant NLR Immune Receptors
NLR stability predicts response to immune checkpoint inhibitors in advanced hepatocellular carcinoma
Structural basis for the inhibition of a bacterial NLR and insights into its activation
Subversion of immune cells by HCMV and HIV-1
Subversionen
Subversionen
Screening for components involved in NLR-mediated immune signalling
Diversification of molecular pattern recognition in bacterial NLR-like proteins
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity
Subversion of dendritic cell functions by bacterial pathogens
Structural basis of NLR activation and innate immune signalling in plants
Biochemical Basis of Autoactivity of a Pair of Plant NLR Immune Receptors
NLR stability predicts response to immune checkpoint inhibitors in advanced hepatocellular carcinoma
Structural basis for the inhibition of a bacterial NLR and insights into its activation
Subversion of immune cells by HCMV and HIV-1
Subversionen
Subversionen
Screening for components involved in NLR-mediated immune signalling
Diversification of molecular pattern recognition in bacterial NLR-like proteins
Oligomerization-mediated autoinhibition and cofactor binding of a plant NLR
TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity
Subversion of dendritic cell functions by bacterial pathogens
Structural basis of NLR activation and innate immune signalling in plants
Biochemical Basis of Autoactivity of a Pair of Plant NLR Immune Receptors
NLR stability predicts response to immune checkpoint inhibitors in advanced hepatocellular carcinoma
Structural basis for the inhibition of a bacterial NLR and insights into its activation
Subversion of immune cells by HCMV and HIV-1
Subversionen