Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host.
about
Structural studies of the Sputnik virophageStructure of lactococcal phage p2 baseplate and its mechanism of activation.Asymmetric binding of transferrin receptor to parvovirus capsidsType VI secretion system: secretion by a contractile nanomachineStructure and function of bacteriophage T4Role of bacteriophage T4 baseplate in regulating assembly and infectionMechanism of membranous tunnelling nanotube formation in viral genome deliveryStructure of the type VI secretion system contractile sheath.Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage 29 tailThe tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria.Structural plasticity of the phage P22 tail needle gp26 probed with xenon gasType VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary originThe phage major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion systemStructural changes in a marine podovirus associated with release of its genome into ProchlorococcusStructure and Molecular Assignment of Lactococcal Phage TP901-1 BaseplateStructure of the bacteriophage T4 long tail fiber receptor-binding tipStructure of the Three N-Terminal Immunoglobulin Domains of the Highly Immunogenic Outer Capsid Protein from a T4-Like BacteriophageAtomic Structure of Bacteriophage Sf6 Tail Needle KnobStructural Conservation of the Myoviridae Phage Tail Sheath Protein FoldStructure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophagesThe Molecular Architecture of the Bacteriophage T4 NeckViral infection modulation and neutralization by camelid nanobodiesStructure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanismIcosahedral bacteriophage ΦX174 forms a tail for DNA transport during infectionStructure of the T4 baseplate and its function in triggering sheath contractionGG: a domain involved in phage LTF apparatus and implicated in human MEB and non-syndromic hearing loss diseasesTssA forms a gp6-like ring attached to the type VI secretion sheathStructure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular ChannelOutcome of the first electron microscopy validation task force meetingBacterial supersystem for alginate import/metabolism and its environmental and bioenergy applicationsConstructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteinsType VI secretion requires a dynamic contractile phage tail-like structure.Atomic structures of a bactericidal contractile nanotube in its pre- and postcontraction statesTail tip proteins related to bacteriophage λ gpL coordinate an iron-sulfur cluster.Three-dimensional structure of the bacteriophage P22 tail machine.Visualization of bacteriophage P1 infection by cryo-electron tomography of tiny Escherichia coliThe mechanism of DNA ejection in the Bacillus anthracis spore-binding phage 8a revealed by cryo-electron tomography.Structural study of the Serratia entomophila antifeeding prophage: three-dimensional structure of the helical sheath.Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitroGenome packaging in viruses.
P2860
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P2860
Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Three-dimensional rearrangemen ...... e T4 on infection of its host.
@en
type
label
Three-dimensional rearrangemen ...... e T4 on infection of its host.
@en
prefLabel
Three-dimensional rearrangemen ...... e T4 on infection of its host.
@en
P50
P1433
P1476
Three-dimensional rearrangemen ...... e T4 on infection of its host.
@en
P2093
Paul R Chipman
Vadim V Mesyanzhinov
P304
P356
10.1016/J.CELL.2004.07.022
P407
P577
2004-08-01T00:00:00Z