Zobrazeno 1 - 10
of 145
pro vyhledávání: '"J.B. Bancroft"'
Subcellular Immunolocalization of the Coat Protein of Two Potexviruses in InfectedChenopodium quinoa
Publikováno v:
Virology. 214(1):314-318
The production of coat protein is necessary for cell-to-cell transport of potexviruses in plants. To investigate the role of coat protein in the movement process, the intracellular distribution of coat protein in tissues infected with either of two p
Publikováno v:
Virology. 204:254-265
The open reading frame 2 (ORF2) of the potexviral genome encodes a 24- to 26-kDa protein which is part of the "triple gene block," a group of overlapping ORFs also present in the genomes of the carla-, hordei-, and furoviruses. The product of these O
Publikováno v:
Virology. 197:695-703
The RNA-dependent RNA polymerase (RdRp) of foxtail mosaic virus (FMV) was partially purified from infected leaves of Chenopodium quinoa. The membrane fraction of crude plant extracts contained most of the FMV RdRp activity. Additional purification wa
Publikováno v:
Virology. 189:817-820
Biologically active in vitro transcripts were synthesized from a cloned cDNA of a defective RNA (D RNA) of clover yellow mosaic virus (CYMV) and were used to determine if a hexanucleotide motif (5′-ACUUAA) conserved in the 3′ noncoding region of
Publikováno v:
Journal of Virology. 66:3069-3076
Naturally occurring defective RNAs (D RNAs) derived from the potexvirus clover yellow mosaic virus (CYMV) contain large internal deletions yet maintain a single open reading frame (ORF) representing the in-frame fusion of 5' and 3' terminal ORFs. Cap
Publikováno v:
The Journal of general virology. 72
The nucleotide sequence of the RNA genome of foxtail mosaic virus (FMV), a member of the potexvirus family, is 6151 nucleotides long, exclusive of a poly(A) tail. The RNA contains five principal open reading frames (ORFs), designated from the 5′ te
Publikováno v:
Virology. 72:514-517
Protein isolated from papaya mosaic virus, which is a flexuous virus similar in morphology to potato virus X, will self-assemble into long helical particles in the absence of RNA. The significance of the conditions required for assembly are briefly c
Autor:
J.B. Bancroft, John W. Erickson
Publikováno v:
Virology. 90:36-46
The conditions for the in vitro reconstitution of papaya mosaic virus (PMV) from its isolated constituents are described and are related to the formation of coat protein subassembly products. PMV assembles best in 0.01 M , pH 8.0, Tris buffer at 25°
Publikováno v:
Virology. 118:241-245
The structure of unusual rod-shaped particles made from papaya mosaic virus protein in methylpentanediol is described. It is shown how the structural subunits group to form the morphological subunits observed on the particles.
Autor:
J.B. Bancroft, Anthony C.H. Durham
Publikováno v:
Virology. 93:246-252
Hydrogen-ion titration curves of papaya mosaic virus and its protein, with or without added CaCl 2 or MgCl 2 are presented and analysed. The virus particle contains three cation-binding sites per subunit, half protonated at pH values of 5.6, 7.0, and