- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Frontiers in microbiology. - 6 (2016) , 01515, ISSN: 1664-302X
- Ereignis
-
Veröffentlichung
- (wo)
-
Freiburg
- (wer)
-
Universität
- (wann)
-
2019
- Urheber
- DOI
-
10.3389/fmicb.2015.01515
- URN
-
urn:nbn:de:bsz:25-freidok-1337785
- Rechteinformation
-
Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:52 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
- Pohlschröder, Mecky
- Albers, Sonja Verena
- Universität
Entstanden
- 2019
Ähnliche Objekte (12)
Wie ein rotierender Typ-IV-Pilus Archaeen das Schwimmen beibrachte
Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in Sulfolobus acidocaldarius
The archaeal protein SepF is essential for cell division in Haloferax volcanii
Putative nucleotide-based second messengers in the archaeal model organisms Haloferax volcanii and Sulfolobus acidocaldarius
Enzymatic asymmetric reduction of unfunctionalized C=C Bonds with archaeal geranylgeranyl reductases
Protein phosphorylation and its role in archaeal signal transduction
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
Towards elucidating the rotary mechanism of the archaellum machinery
Taxis in archaea
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
Wie ein rotierender Typ-IV-Pilus Archaeen das Schwimmen beibrachte
Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in Sulfolobus acidocaldarius
The archaeal protein SepF is essential for cell division in Haloferax volcanii
Putative nucleotide-based second messengers in the archaeal model organisms Haloferax volcanii and Sulfolobus acidocaldarius
Enzymatic asymmetric reduction of unfunctionalized C=C Bonds with archaeal geranylgeranyl reductases
Protein phosphorylation and its role in archaeal signal transduction
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
Towards elucidating the rotary mechanism of the archaellum machinery
Taxis in archaea
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
Wie ein rotierender Typ-IV-Pilus Archaeen das Schwimmen beibrachte
Two membrane-bound transcription factors regulate expression of various type-IV-pili surface structures in Sulfolobus acidocaldarius
The archaeal protein SepF is essential for cell division in Haloferax volcanii
Putative nucleotide-based second messengers in the archaeal model organisms Haloferax volcanii and Sulfolobus acidocaldarius
Enzymatic asymmetric reduction of unfunctionalized C=C Bonds with archaeal geranylgeranyl reductases
Protein phosphorylation and its role in archaeal signal transduction
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
Towards elucidating the rotary mechanism of the archaellum machinery
Taxis in archaea