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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.
8 d assembly that utilizes the coat protein of bacteriophage P22, a naturally occurring substrate of Gr
11 ldtype homotrimeric tailspike protein of the bacteriophage P22 and its endorhamnosidase point mutant
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
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
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
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
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
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
40 caffolding protein of Salmonella typhimurium bacteriophage P22 is a 33.6 kDa protein required both in
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
52 cryomicroscopy to determine the structure of bacteriophage P22 portal protein in both the procapsid a
57 to study the three-dimensional structures of bacteriophage P22 procapsids containing wild-type and mu
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
65 iometry and thermodynamics of binding of the bacteriophage P22 scaffolding protein within the procaps
69 ished calorimetric data of a closely related bacteriophage, P22, showed that capsid maturation was an
71 esidue subunit of the Salmonella typhimurium bacteriophage P22 tailspike contains eight cysteine resi
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
76 tudies of variants of the P(ant) promoter of bacteriophage P22, the Arc protein was found not only to
78 great deal is known about the life cycle of bacteriophage P22, the mechanism of phage DNA transport
80 y and helps to direct the temperate lambdoid bacteriophage P22 to the lysogenic developmental pathway
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
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