CkP1 bacteriophage, a S16-like myovirus that recognizes Citrobacter koseri lipopolysaccharide through its long tail fibers
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource, 1 online resource.
- Language
-
Englisch
- Bibliographic citation
-
CkP1 bacteriophage, a S16-like myovirus that recognizes Citrobacter koseri lipopolysaccharide through its long tail fibers ; volume:107 ; number:11 ; day:3 ; month:5 ; year:2023 ; pages:3621-3636 ; date:6.2023
Applied microbiology and biotechnology ; 107, Heft 11 (3.5.2023), 3621-3636, 6.2023
- Creator
-
Oliveira, Hugo
Santos, Sílvio
Pires, Diana P.
Boeckaerts, Dimitri
Pinto, Graça
Domingues, Rita
Otero, Jennifer
Briers, Yves
Lavigne, Rob
Schmelcher, Mathias
Dötsch, Andreas
Azeredo, Joana
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1007/s00253-023-12547-8
- URN
-
urn:nbn:de:101:1-2023090713321379269067
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:46 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
- Oliveira, Hugo
- Santos, Sílvio
- Pires, Diana P.
- Boeckaerts, Dimitri
- Pinto, Graça
- Domingues, Rita
- Otero, Jennifer
- Briers, Yves
- Lavigne, Rob
- Schmelcher, Mathias
- Dötsch, Andreas
- Azeredo, Joana
- SpringerLink (Online service)
Other Objects (12)
Bacteriophage P1
Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity
Architecture of the flexible tail tube of bacteriophage SPP1
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers
Simultaneous display of two large proteins on the head and tail of bacteriophage lambda
P1
P1
Preiskarteiblatt für... (P1/41/1977, P1 43/1977, P1/52/1977)
Bacteriophage P1
Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity
Architecture of the flexible tail tube of bacteriophage SPP1
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers
Simultaneous display of two large proteins on the head and tail of bacteriophage lambda
P1
P1
Preiskarteiblatt für... (P1/41/1977, P1 43/1977, P1/52/1977)
Bacteriophage P1
Dual function of a highly conserved bacteriophage tail completion protein essential for bacteriophage infectivity
Architecture of the flexible tail tube of bacteriophage SPP1
Nearly complete structure of bacteriophage DT57C reveals architecture of head-to-tail interface and lateral tail fibers
Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
Bacteriophage Tail‐Tube Assembly Studied by Proton‐Detected 4D Solid‐State NMR
High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers
Simultaneous display of two large proteins on the head and tail of bacteriophage lambda
P1
P1