- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
Outer membrane protein assembly mediated by BAM-SurA complexes ; volume:15 ; number:1 ; day:1 ; month:9 ; year:2024 ; pages:1-17 ; date:12.2024
Nature Communications ; 15, Heft 1 (1.9.2024), 1-17, 12.2024
- Creator
-
Fenn, Katherine L.
Horne, Jim E.
Crossley, Joel A.
Böhringer, Nils
Horne, Romany J.
Schäberle, Till F.
Calabrese, Antonio N.
Radford, Sheena E.
Ranson, Neil A.
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41467-024-51358-x
- URN
-
urn:nbn:de:101:1-2411170052579.718987841918
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:22 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
- Fenn, Katherine L.
- Horne, Jim E.
- Crossley, Joel A.
- Böhringer, Nils
- Horne, Romany J.
- Schäberle, Till F.
- Calabrese, Antonio N.
- Radford, Sheena E.
- Ranson, Neil A.
- SpringerLink (Online service)
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The periplasmic domain of the barrel assembly machinery protein A (BamA) from Escherichia coli assists folding of outer membrane protein A
Machinery for protein sorting and assembly in the mitochondrial outer membrane
The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro
Lipopolysaccharide assembly in the bacterial outer membrane revealed by X-ray crystallography
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Outer Membrane Vesicle Vaccine Platforms
Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs
Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
Peptidoglycan maturation controls outer membrane protein assembly
Facilitating folding of outer membrane proteins, roles of the periplasmic chaperone Skp and the outer membrane lipoprotein BamD
Structure of BamA, an essential factor in outer membrane protein biogenesis
The periplasmic domain of the barrel assembly machinery protein A (BamA) from Escherichia coli assists folding of outer membrane protein A
Machinery for protein sorting and assembly in the mitochondrial outer membrane
The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro
Lipopolysaccharide assembly in the bacterial outer membrane revealed by X-ray crystallography
Outer membrane vesicles of bacteria
Assembling the mitochondrial outer membrane
Outer Membrane Vesicle Vaccine Platforms
Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs
Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies
Peptidoglycan maturation controls outer membrane protein assembly
Facilitating folding of outer membrane proteins, roles of the periplasmic chaperone Skp and the outer membrane lipoprotein BamD
Structure of BamA, an essential factor in outer membrane protein biogenesis
The periplasmic domain of the barrel assembly machinery protein A (BamA) from Escherichia coli assists folding of outer membrane protein A
Machinery for protein sorting and assembly in the mitochondrial outer membrane
The translocation assembly module (TAM) catalyzes the assembly of bacterial outer membrane proteins in vitro
Lipopolysaccharide assembly in the bacterial outer membrane revealed by X-ray crystallography
Outer membrane vesicles of bacteria
Assembling the mitochondrial outer membrane
Outer Membrane Vesicle Vaccine Platforms
Leptospira interrogans encodes a canonical BamA and three novel noNterm Omp85 outer membrane protein paralogs