- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Nature Communications, 13.2022, art. 2857, S. 1-12
- Event
-
Veröffentlichung
- (where)
-
Frankfurt am Main
- (who)
-
Universitätsbibliothek Johann Christian Senckenberg
- (when)
-
2022
- Creator
- DOI
-
10.1038/s41467-022-30358-9
- URN
-
urn:nbn:de:hebis:30:3-632608
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:23 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
- Altegoer, Florian
- Quax, Tessa
- Weiland, Paul
- Nußbaum, Phillip
- Giammarinaro, Pietro Ivan
- Patro, Megha
- Li, Zhengqun
- Oesterhelt, Dieter
- Grininger, Martin
- Albers, Sonja Verena
- Bange, Gert
- Universitätsbibliothek Johann Christian Senckenberg
Time of origin
- 2022
Other Objects (12)
Structural insights into the mechanism of archaellar rotational switching
Structural insights into the mechanism of archaellar rotational switching
Towards elucidating the rotary mechanism of the archaellum machinery
Editorial: Archaeal cell envelope and surface structures
Wie ein rotierender Typ-IV-Pilus Archaeen das Schwimmen beibrachte
Diversity and evolution of type IV pili systems in archaea
A comprehensive history of motility and Archaellation in Archaea
Characterization of the ATPase FlaI of the motor complex of the Pyrococcus furiosus archaellum and its interactions between the ATP-binding protein FlaH
Taxis in archaea
Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in Sulfolobus acidocaldarius
AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7
SaUspA, the universal stress protein of Sulfolobus acidocaldarius stimulates the activity of the PP2A phosphatase and is involved in growth at high salinity
Structural insights into the mechanism of archaellar rotational switching
Structural insights into the mechanism of archaellar rotational switching
Towards elucidating the rotary mechanism of the archaellum machinery
Editorial: Archaeal cell envelope and surface structures
Wie ein rotierender Typ-IV-Pilus Archaeen das Schwimmen beibrachte
Diversity and evolution of type IV pili systems in archaea
A comprehensive history of motility and Archaellation in Archaea
Characterization of the ATPase FlaI of the motor complex of the Pyrococcus furiosus archaellum and its interactions between the ATP-binding protein FlaH
Taxis in archaea
Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in Sulfolobus acidocaldarius
AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7
SaUspA, the universal stress protein of Sulfolobus acidocaldarius stimulates the activity of the PP2A phosphatase and is involved in growth at high salinity
Structural insights into the mechanism of archaellar rotational switching
Structural insights into the mechanism of archaellar rotational switching
Towards elucidating the rotary mechanism of the archaellum machinery
Editorial: Archaeal cell envelope and surface structures
Wie ein rotierender Typ-IV-Pilus Archaeen das Schwimmen beibrachte
Diversity and evolution of type IV pili systems in archaea
A comprehensive history of motility and Archaellation in Archaea
Characterization of the ATPase FlaI of the motor complex of the Pyrococcus furiosus archaellum and its interactions between the ATP-binding protein FlaH
Taxis in archaea
Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in Sulfolobus acidocaldarius
AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7