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1 three well-characterized model proteins and bacteriophage MS2.
2 o model microorganisms: Escherichia coli and bacteriophage MS2.
3 de display platform based on VLPs of the RNA bacteriophage MS2.
4 vaccine development based on the VLPs of RNA bacteriophage MS2.
5 translational operator stem-loop of the RNA bacteriophage MS2.
6 3 viral capsid, during reassembly of the RNA bacteriophage MS2.
7 esized and coupled to chymotrypsinogen A and bacteriophage MS2.
8 immunoassay has been developed for detecting bacteriophage MS2.
9 n the capsid proteins and the genomic RNA of bacteriophage MS2.
10 achieved by columns for the bacterial virus (bacteriophage) MS2 110 (+/-19)%, as model organism, as w
11 eating of a suspension of a model virus, RNA bacteriophage MS2, 13 chemical digestion products were d
12 (99.99%+), moderately effective in reducing bacteriophage MS2 (99%+), and somewhat effective against
14 f of concept for the label-free detection of bacteriophage MS2, a model indicator of microbiological
15 chitectures to develop immunosensors for the bacteriophage MS2, a virus often detected in sewage-impa
16 3 (PV3), adenovirus type 2 (HAdV2), and two bacteriophage (MS2 and PRD1) was investigated in an arra
17 the viral genome, as exemplified by the RNA bacteriophage MS2 and as proposed for other RNA viruses
19 ation allowed for the discrimination between bacteriophage MS2 and other closely related RNA bacterio
21 ruses (MHV and varphi6) and two nonenveloped bacteriophages (MS2 and T3) in raw wastewater samples.
23 igated the inactivation of Escherichia coli, bacteriophage MS2, and Bacillus subtilis spores as surro
24 strated here with tobacco mosaic virus U2, a bacteriophage MS2, and equine encephalitis TRD, is achie
25 s capsids, focusing on hepatitis B virus and bacteriophage MS2, and formation of glycoproteins in the
26 ularly imprinted polymer (MIP) targeting the bacteriophage MS2 as the template was investigated using
27 be the cryo-electron microscopy structure of bacteriophage MS2 bound to its receptor, the bacterial F
28 e, the detection limit for quantification of bacteriophage MS2 by quantitative reverse transcriptase
29 we demonstrated the DESI-MS detection of the bacteriophage MS2 capsid protein from crude samples with
31 the three-dimensional solution structure of bacteriophage MS2 capsids reassembled from recombinant p
32 single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the gen
33 mes containing binding sites for BglG or the bacteriophage MS2 coat protein along with 2 fluorescent
34 sible to generate crosslinks between the RNA bacteriophage MS2 coat protein and the initiator stem-lo
35 roteins containing an RS domain fused to the bacteriophage MS2 coat protein are sufficient to activat
36 red assembly and solubility properties using bacteriophage MS2 coat protein as a model self-associati
38 that such quasi-equivalent conformers of RNA bacteriophage MS2 coat protein dimers (CP(2)) can be swi
40 ay, in which a fusion protein of PTB and the bacteriophage MS2 coat protein is recruited to a splicin
41 en the F and G beta strands (FG loop) of the bacteriophage MS2 coat protein subunit forms inter-subun
42 ed the kinetics of complex formation between bacteriophage MS2 coat protein subunits and synthetic RN
44 of the high sequence coverage obtained, the bacteriophage MS2 coat protein was identified with high
45 ively expressing an ASH1 mRNA containing the bacteriophage MS2 coat-protein binding site adjacent to
47 recent cryo-electron microscopy structure of bacteriophage MS2, determined with only 5-fold symmetry
48 ystematically studied the adsorption of four bacteriophages (MS2, fr, GA, and Qbeta) to five model su
49 ynamics of negatively charged viruses (i.e., bacteriophages MS2, fr, GA, and Qbeta) and polystyrene n
51 one of four classes of biothreat agents, and bacteriophage MS2 has been used as a simulant for biothr
52 microorganisms, as well as for detection of bacteriophage MS2 in the presence of a large excess of E
53 w functionalization strategies, detection of bacteriophage MS2 is performed through either a direct a
54 zed using diverse techniques, the use of the bacteriophage MS2 method to encode genetically fluoresce
55 of 40 nm nominal pore size was used to study bacteriophage MS2 removal under different membrane condi
56 dated larger sample volumes in extraction of bacteriophage MS2 RNA from the various specimen matrices
57 sed RNA oligomer segments from the genome of bacteriophage MS2 to UV254, simulated sunlight, and sing
58 surrogate viruses murine norovirus (MNV) and bacteriophage MS2 under identical experimental condition
59 tivation rates for a common surrogate virus, bacteriophage MS2 (up to 270% compared to the unmodified
60 the total damage incurred by a model virus (bacteriophage MS2) upon inactivation induced by five com
61 ckaging of a representative ssRNA virus, the bacteriophage MS2, via a series of biomolecular simulati
62 + 8H]8+ to [M + 6H]6+ precursor ions of the bacteriophage MS2 viral coat protein following concentra
64 A full-length cDNA copy of the RNA genome of bacteriophage MS2 was assembled by the in-frame ligation
66 oop (TR) encompassing 19 nt of the genome of bacteriophage MS2 was shown to act as an allosteric effe
70 xtrinsic controls (phocine herpesvirus 1 and bacteriophage MS2) were included to ensure extraction an
71 case study, we consider the viral capsid of bacteriophage MS2, which is formed from 60 asymmetric (A
72 is system is the spherical protein capsid of bacteriophage MS2, which was used to house gold particle
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