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1 is a close relative of the very well studied bacteriophage P22.
2 r of Salmonella enterica serovar Typhimurium bacteriophage P22.
3 bly intermediates of the double-stranded DNA bacteriophage P22.
4 , Pant and Pmnt, in the immunity I operon of bacteriophage P22.
5 mbly intermediates in Salmonella typhimurium bacteriophage P22.
6                                              Bacteriophage P22, a double-stranded DNA (dsDNA) virus,
7                               In the case of bacteriophage P22, a model in which the scaffolding prot
8 d assembly that utilizes the coat protein of bacteriophage P22, a naturally occurring substrate of Gr
9                                              Bacteriophage P22, a podovirus infecting strains of Salm
10                                              Bacteriophage P22 Abc2 protein binds to the RecBCD enzym
11 ldtype homotrimeric tailspike protein of the bacteriophage P22 and its endorhamnosidase point mutant
12                                      In both bacteriophage P22 and the herpesviruses the extreme scaf
13      Arc-L1-Arc is a single-chain variant of bacteriophage P22 Arc repressor in which a 15 residue li
14 phage N15 Cro, bacteriophage lambda Cro, and bacteriophage P22 Arc) with related but divergent struct
15 The assembly intermediates of the Salmonella bacteriophage P22 are well defined but the molecular int
16                   The Salmonella typhimurium bacteriophage P22 assembles an icosahedral capsid precur
17                     The repressor protein of bacteriophage P22 binds to DNA as a homodimer.
18 acteriophage T7 tail protein gp11 and gp4 of bacteriophage P22, but TTPA contains an additional antip
19 ontainer based on the Salmonella typhimurium bacteriophage P22 capsid, genetically incorporating zico
20                   In this study, we employed bacteriophage P22 challenge phages to determine which pr
21                                          The bacteriophage P22 coat protein has the common HK97-like
22 action sites of scaffolding protein with the bacteriophage P22 coat protein lattice, we have determin
23 o acid substitutions have been identified in bacteriophage P22 coat protein that are defective in fol
24   The I-domain is an insertion domain of the bacteriophage P22 coat protein that drives rapid folding
25 erature-sensitive-folding (tsf) phenotype to bacteriophage P22 coat protein.
26                                              Bacteriophage P22 contains 420 monomers of coat protein
27 eport the first accurate genome sequence for bacteriophage P22, correcting a 0.14% error rate in prev
28 ly directs lysogen formation for P22 R17 , a bacteriophage P22 derivative that carries the R17/MS2 RN
29                   The scaffolding protein of bacteriophage P22 directs the assembly of an icosahedral
30 transcriptional antitermination protein N of bacteriophage P22, equipped with a luminescent DOTA[Tb(3
31 ural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric con
32                      The Double-stranded DNA bacteriophage P22 has a ring-shaped dodecameric complex
33                                              Bacteriophage P22 has served as a model system for this
34 tral pH structure of three tail needles from bacteriophage P22, HK620, and Sf6.
35 igated determinants of polyhead formation in bacteriophage P22 in order to understand the molecular m
36 s are modified versions of the temperate DNA bacteriophage P22 in which post-transcriptional regulato
37                                              Bacteriophage P22 infects Salmonella enterica serovar Ty
38                     To infect and replicate, bacteriophage P22 injects its 43 kbp genome across the c
39                             Morphogenesis of bacteriophage P22 involves the packaging of double-stran
40 caffolding protein of Salmonella typhimurium bacteriophage P22 is a 33.6 kDa protein required both in
41                         The Arc repressor of bacteriophage P22 is a dimeric member of the ribbon-heli
42                           Arc repressor from bacteriophage P22 is a homodimeric member of the ribbon-
43                              The tail of the bacteriophage P22 is composed of multiple protein compon
44 e DNA packaging machine (portal assembly) of bacteriophage P22 is constructed from 12 copies of a mul
45 in that is inserted into the coat protein of bacteriophage P22 is important in the process of proper
46 es have suggested that the portal protein of bacteriophage P22 is not essential for shell assembly; h
47                                    The dsDNA bacteriophage P22 is used as a model system to study the
48 haracterized the structure and regulation of bacteriophage P22 L-terminase (gp2).
49                     In this work, we examine bacteriophage P22 morphogenesis by comparing three-dimen
50                                           In bacteriophage P22, only coat protein (gp5) and scaffoldi
51                             The repressor of bacteriophage P22 (P22R) discriminates between its vario
52 cryomicroscopy to determine the structure of bacteriophage P22 portal protein in both the procapsid a
53                              The assembly of bacteriophage P22 portal rings has been characterized in
54         Using 400-kV spot-scan images of the bacteriophage P22 procapsid, we have calculated an ampli
55 rangement of a mutant scaffolding within the bacteriophage P22 procapsid.
56 nstruction to obtain 15 A structures of both bacteriophage P22 procapsids and mature phage.
57 to study the three-dimensional structures of bacteriophage P22 procapsids containing wild-type and mu
58                                  Assembly of bacteriophage P22 procapsids has long served as a model
59          Assembly of the double-stranded DNA bacteriophage P22 procapsids requires the interaction of
60                                  Assembly of bacteriophage P22 procapsids requires the participation
61                                          The bacteriophage P22 R17 encodes a wild-type R17 operator s
62 ese methods to new cryoEM maps of the mature bacteriophage P22, reconstructed without imposing icosah
63 ion) accompanying DNA packaging in the dsDNA bacteriophage P22 represents an experimentally accessibl
64                              Assembly of the bacteriophage P22 requires a 303 amino acid residue scaf
65 iometry and thermodynamics of binding of the bacteriophage P22 scaffolding protein within the procaps
66                                              Bacteriophage P22 scaffolding subunits are elongated mol
67                                          The bacteriophage P22 serves as a model for assembly of icos
68                                              Bacteriophage P22 serves as a model for the assembly and
69 ished calorimetric data of a closely related bacteriophage, P22, showed that capsid maturation was an
70                                 The trimeric bacteriophage P22 tailspike adhesin exhibits a domain in
71 esidue subunit of the Salmonella typhimurium bacteriophage P22 tailspike contains eight cysteine resi
72  found to have a structure homologous to the bacteriophage P22 tailspikes.
73 t evidence that su substitutions that rescue bacteriophage P22 temperature-sensitive-folding (tsf) co
74 NA challenge phages are modified versions of bacteriophage P22 that allow one to select directly for
75      RNA challenge phages are derivatives of bacteriophage P22 that enable direct genetic selection f
76 tudies of variants of the P(ant) promoter of bacteriophage P22, the Arc protein was found not only to
77                                           In bacteriophage P22, the association of scaffolding and co
78  great deal is known about the life cycle of bacteriophage P22, the mechanism of phage DNA transport
79 genase, sequestered within the capsid of the bacteriophage P22 through directed self-assembly.
80 y and helps to direct the temperate lambdoid bacteriophage P22 to the lysogenic developmental pathway
81       Mnt, a tetrameric repressor encoded by bacteriophage P22, uses N-domain dimers to contact each
82 stals confined inside genetically engineered bacteriophage P22 VLP using semiconducting CdS as a prot
83 were isolated and subjected to hydrolysis by bacteriophage P22, which contains endorhamnosidase activ
84                                 Viruses like bacteriophage P22, which have partially circularly permu
85 se exchanges detected in the packaged DNA of bacteriophage P22, which lacks a viral membrane.

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