ライフサイエンスコーパス: bacteriophage P22

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 paradigm for this class of viruses,

10 Bacteriophage P22, a podovirus infecting strains of Salm

11 Bacteriophage P22 Abc2 protein binds to the RecBCD enzym

12 ldtype homotrimeric tailspike protein of the bacteriophage P22 and its endorhamnosidase point mutant

13 In both bacteriophage P22 and the herpesviruses the extreme scaf

14 Arc-L1-Arc is a single-chain variant of bacteriophage P22 Arc repressor in which a 15 residue li

15 phage N15 Cro, bacteriophage lambda Cro, and bacteriophage P22 Arc) with related but divergent struct

16 The assembly intermediates of the Salmonella bacteriophage P22 are well defined but the molecular int

17 The Salmonella typhimurium bacteriophage P22 assembles an icosahedral capsid precur

18 The repressor protein of bacteriophage P22 binds to DNA as a homodimer.

19 acteriophage T7 tail protein gp11 and gp4 of bacteriophage P22, but TTPA contains an additional antip

20 ontainer based on the Salmonella typhimurium bacteriophage P22 capsid, genetically incorporating zico

21 In this study, we employed bacteriophage P22 challenge phages to determine which pr

22 The bacteriophage P22 coat protein has the common HK97-like

23 action sites of scaffolding protein with the bacteriophage P22 coat protein lattice, we have determin

24 o acid substitutions have been identified in bacteriophage P22 coat protein that are defective in fol

25 The I-domain is an insertion domain of the bacteriophage P22 coat protein that drives rapid folding

26 erature-sensitive-folding (tsf) phenotype to bacteriophage P22 coat protein.

27 Bacteriophage P22 contains 420 monomers of coat protein

28 eport the first accurate genome sequence for bacteriophage P22, correcting a 0.14% error rate in prev

29 ly directs lysogen formation for P22 R17 , a bacteriophage P22 derivative that carries the R17/MS2 RN

30 The scaffolding protein of bacteriophage P22 directs the assembly of an icosahedral

31 transcriptional antitermination protein N of bacteriophage P22, equipped with a luminescent DOTA[Tb(3

32 ural evidence that the portal protein of the bacteriophage P22 exists in two distinct dodecameric con

33 The Double-stranded DNA bacteriophage P22 has a ring-shaped dodecameric complex

34 Bacteriophage P22 has served as a model system for this

35 tral pH structure of three tail needles from bacteriophage P22, HK620, and Sf6.

36 igated determinants of polyhead formation in bacteriophage P22 in order to understand the molecular m

37 s are modified versions of the temperate DNA bacteriophage P22 in which post-transcriptional regulato

38 Bacteriophage P22 infects Salmonella enterica serovar Ty

39 To infect and replicate, bacteriophage P22 injects its 43 kbp genome across the c

40 Morphogenesis of bacteriophage P22 involves the packaging of double-stran

41 caffolding protein of Salmonella typhimurium bacteriophage P22 is a 33.6 kDa protein required both in

42 The Arc repressor of bacteriophage P22 is a dimeric member of the ribbon-heli

43 Arc repressor from bacteriophage P22 is a homodimeric member of the ribbon-

44 Bacteriophage P22 is a prototypical member of the Podovi

45 The tail of the bacteriophage P22 is composed of multiple protein compon

46 e DNA packaging machine (portal assembly) of bacteriophage P22 is constructed from 12 copies of a mul

47 in that is inserted into the coat protein of bacteriophage P22 is important in the process of proper

48 es have suggested that the portal protein of bacteriophage P22 is not essential for shell assembly; h

49 The dsDNA bacteriophage P22 is used as a model system to study the

50 haracterized the structure and regulation of bacteriophage P22 L-terminase (gp2).

51 In this work, we examine bacteriophage P22 morphogenesis by comparing three-dimen

52 In bacteriophage P22, only coat protein (gp5) and scaffoldi

53 The repressor of bacteriophage P22 (P22R) discriminates between its vario

54 cryomicroscopy to determine the structure of bacteriophage P22 portal protein in both the procapsid a

55 The assembly of bacteriophage P22 portal rings has been characterized in

56 Using 400-kV spot-scan images of the bacteriophage P22 procapsid, we have calculated an ampli

57 rangement of a mutant scaffolding within the bacteriophage P22 procapsid.

58 nstruction to obtain 15 A structures of both bacteriophage P22 procapsids and mature phage.

59 to study the three-dimensional structures of bacteriophage P22 procapsids containing wild-type and mu

60 Assembly of bacteriophage P22 procapsids has long served as a model

61 Assembly of the double-stranded DNA bacteriophage P22 procapsids requires the interaction of

62 Assembly of bacteriophage P22 procapsids requires the participation

63 The bacteriophage P22 R17 encodes a wild-type R17 operator s

64 ese methods to new cryoEM maps of the mature bacteriophage P22, reconstructed without imposing icosah

65 ion) accompanying DNA packaging in the dsDNA bacteriophage P22 represents an experimentally accessibl

66 Assembly of the bacteriophage P22 requires a 303 amino acid residue scaf

67 Here, we show that in bacteriophage P22, residue W61 at the tip of the E-loop

68 iometry and thermodynamics of binding of the bacteriophage P22 scaffolding protein within the procaps

69 Bacteriophage P22 scaffolding subunits are elongated mol

70 The bacteriophage P22 serves as a model for assembly of icos

71 Bacteriophage P22 serves as a model for the assembly and

72 ished calorimetric data of a closely related bacteriophage, P22, showed that capsid maturation was an

73 The trimeric bacteriophage P22 tailspike adhesin exhibits a domain in

74 esidue subunit of the Salmonella typhimurium bacteriophage P22 tailspike contains eight cysteine resi

75 found to have a structure homologous to the bacteriophage P22 tailspikes.

76 t evidence that su substitutions that rescue bacteriophage P22 temperature-sensitive-folding (tsf) co

77 NA challenge phages are modified versions of bacteriophage P22 that allow one to select directly for

78 RNA challenge phages are derivatives of bacteriophage P22 that enable direct genetic selection f

79 tudies of variants of the P(ant) promoter of bacteriophage P22, the Arc protein was found not only to

80 In bacteriophage P22, the association of scaffolding and co

81 great deal is known about the life cycle of bacteriophage P22, the mechanism of phage DNA transport

82 However, for bacteriophage P22, the role of its portal protein in ini

83 genase, sequestered within the capsid of the bacteriophage P22 through directed self-assembly.

84 ous virus-like particles (VLPs) derived from bacteriophage P22 to investigate the range of molecule s

85 y and helps to direct the temperate lambdoid bacteriophage P22 to the lysogenic developmental pathway

86 Mnt, a tetrameric repressor encoded by bacteriophage P22, uses N-domain dimers to contact each

87 stals confined inside genetically engineered bacteriophage P22 VLP using semiconducting CdS as a prot

88 were isolated and subjected to hydrolysis by bacteriophage P22, which contains endorhamnosidase activ

89 Viruses like bacteriophage P22, which have partially circularly permu

90 se exchanges detected in the packaged DNA of bacteriophage P22, which lacks a viral membrane.