Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2041-1723
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels ; volume:9 ; number:1 ; day:26 ; month:11 ; year:2018 ; pages:1-10 ; date:12.2018
Nature Communications ; 9, Heft 1 (26.11.2018), 1-10, 12.2018
- Klassifikation
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Biowissenschaften, Biologie
- Urheber
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Stock, Charlott
Hielkema, L.
Tascón, I.
Wunnicke, D.
Oostergetel, G. T.
Azkargorta, M.
Batista Paulino, Cristina
Hänelt, Inga
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
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10.1038/s41467-018-07319-2
- URN
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urn:nbn:de:101:1-2019010323561331701736
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
- 14.08.2025, 10:49 MESZ
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Beteiligte
- Stock, Charlott
- Hielkema, L.
- Tascón, I.
- Wunnicke, D.
- Oostergetel, G. T.
- Azkargorta, M.
- Batista Paulino, Cristina
- Hänelt, Inga
- SpringerLink (Online service)
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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
Cryo-EM analysis of human small ribosomal subunit biogenesis
Statistical Inference of cryo-EM Maps
Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1
Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin
Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model
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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels
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Statistical Inference of cryo-EM Maps
Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1
Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin
Cryo-EM structures of the plant anion channel SLAC1 from Arabidopsis thaliana suggest a combined activation model
Cryo-EM structure of an early precursor of large ribosomal subunit reveals a half-assembled intermediate
Determining subunit-subunit interaction from statistics of cryo-EM images: observation of nearest-neighbor coupling in a circadian clock protein complex
Manifold methods for cryo-EM image denoising
Invariants for multireference alignment and cryo-EM
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