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rice dwarf virus (rdv)  (ACADEMIC PRESS INC)

 
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    Structured Review

    ACADEMIC PRESS INC rice dwarf virus (rdv)
    Rice Dwarf Virus (Rdv), supplied by ACADEMIC PRESS INC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rice+dwarf+virus+(rdv)/rice+dwarf+virus++rdv+/pm18640559-11-5-2
    Average 90 stars, based on 1 article reviews
    rice dwarf virus (rdv) - by Bioz Stars, 2026-11
    90/100 stars

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    Related Articles

    Binding Assay:

    Article Title: The structure of rice dwarf virus determined by small-angle neutron scattering measurements.
    Article Snippet: The structure of rice dwarf virus (RDV) has been investigated by small-angle neutronscattering measurements using the contrast variation method.. The contrast match point gave an RNA content of about 20%) by weight.. The value of the neutron intensity scattered at zero angle in water divided by the virus concentration yielded a particle weight of 65.2 X 106.

    Article Title: Novel NTP binding property of rice dwarf phytoreovirus minor core protein P5.
    Article Snippet: These results may suggest that the minor core protein of RDV, which is coded by S5, is a candidate guanylyltransferase, although the biological significance of its ATP and UTP binding activities remains largely unknown. q 1996 Academic Press, Inc. Rice dwarf virus (RDV) (1), a species of the genus its GTP-PPi exchange activity (8–12).

    Virus:

    Article Title: The structure of rice dwarf virus determined by small-angle neutron scattering measurements.
    Article Snippet: The structure of rice dwarf virus (RDV) has been investigated by small-angle neutronscattering measurements using the contrast variation method.. The contrast match point gave an RNA content of about 20%) by weight.. The value of the neutron intensity scattered at zero angle in water divided by the virus concentration yielded a particle weight of 65.2 X 106.

    Article Title: Novel NTP binding property of rice dwarf phytoreovirus minor core protein P5.
    Article Snippet: These results may suggest that the minor core protein of RDV, which is coded by S5, is a candidate guanylyltransferase, although the biological significance of its ATP and UTP binding activities remains largely unknown. q 1996 Academic Press, Inc. Rice dwarf virus (RDV) (1), a species of the genus its GTP-PPi exchange activity (8–12).

    Activity Assay:

    Article Title: The structure of rice dwarf virus determined by small-angle neutron scattering measurements.
    Article Snippet: The structure of rice dwarf virus (RDV) has been investigated by small-angle neutronscattering measurements using the contrast variation method.. The contrast match point gave an RNA content of about 20%) by weight.. The value of the neutron intensity scattered at zero angle in water divided by the virus concentration yielded a particle weight of 65.2 X 106.

    Article Title: Novel NTP binding property of rice dwarf phytoreovirus minor core protein P5.
    Article Snippet: These results may suggest that the minor core protein of RDV, which is coded by S5, is a candidate guanylyltransferase, although the biological significance of its ATP and UTP binding activities remains largely unknown. q 1996 Academic Press, Inc. Rice dwarf virus (RDV) (1), a species of the genus its GTP-PPi exchange activity (8–12).



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    rna rdv rice dwarf virus sds page sodium dodecyl sulfate polyacrylamide gel electrophoresis 3d  (Thermo Fisher)
    99
    Thermo Fisher rna rdv rice dwarf virus sds page sodium dodecyl sulfate polyacrylamide gel electrophoresis 3d
    Overall structure of the isolated P2 protein. <t>(a)</t> <t>SDS-PAGE</t> of the structural proteins of <t>RDV</t> with and without CCl4 treatment. Intact RDV has seven kinds of proteins (Lane 2; P1–P3, P5, P7–P9 proteins). Lane 1, RDV particles lacking the P2 protein by CCl4 treatment used in the previous study (15); Lane 2, intact RDV particles containing the P2 protein (without CCl4 treatment) used in this study. P9 protein is appeared as several bands in SDS-PAGE (30). P9* is processed or degraded from a large polypeptide of P9 protein (P9). (b) SDS-PAGE and western blot analysis of the isolated P2 protein from intact RDV particles. The isolated P2 protein was separated by SDS-PAGE and then stained with Coomassie Brilliant Blue (left) or analysed by western blotting with RDV P2-specific antibodies (right). Lane 1, molecular weight markers; Lane 2, intact RDV particle; Lane 3, isolated P2 protein. (c) Electron micrograph of negatively stained P2 proteins isolated from intact RDV particles, which was recorded at a magnification of ×50,000 with an H7650 electron microscope (Hitachi, Japan). Small aggregated P2 proteins are also observed in the micrographs, which are indicated by arrowheads. The bar represents 50 nm. (d) Selected class-averaged images. The width of each image is 40.1 nm. A histogram of the lengths of the P2 proteins is presented later. The lengths of the P2 proteins were measured by tracing the centre of the filament in each class-averaged image. All 50 class-averaged images are shown in the Supplementary Data (Supplementary Fig. S2). (e) Schematic representation of the P2 structure.
    Rna Rdv Rice Dwarf Virus Sds Page Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis 3d, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rice+dwarf+virus+(rdv)/DODECYL+SULFATE+SODIUM+SALT/pmc04892776-330-13-9
    Average 99 stars, based on 1 article reviews
    rna rdv rice dwarf virus sds page sodium dodecyl sulfate polyacrylamide gel electrophoresis 3d - by Bioz Stars, 2026-11
    99/100 stars
    		  Buy from Supplier
    rice dwarf virus (rdv)  (ACADEMIC PRESS INC)
    90
    ACADEMIC PRESS INC rice dwarf virus (rdv)
    Overall structure of the isolated P2 protein. <t>(a)</t> <t>SDS-PAGE</t> of the structural proteins of <t>RDV</t> with and without CCl4 treatment. Intact RDV has seven kinds of proteins (Lane 2; P1–P3, P5, P7–P9 proteins). Lane 1, RDV particles lacking the P2 protein by CCl4 treatment used in the previous study (15); Lane 2, intact RDV particles containing the P2 protein (without CCl4 treatment) used in this study. P9 protein is appeared as several bands in SDS-PAGE (30). P9* is processed or degraded from a large polypeptide of P9 protein (P9). (b) SDS-PAGE and western blot analysis of the isolated P2 protein from intact RDV particles. The isolated P2 protein was separated by SDS-PAGE and then stained with Coomassie Brilliant Blue (left) or analysed by western blotting with RDV P2-specific antibodies (right). Lane 1, molecular weight markers; Lane 2, intact RDV particle; Lane 3, isolated P2 protein. (c) Electron micrograph of negatively stained P2 proteins isolated from intact RDV particles, which was recorded at a magnification of ×50,000 with an H7650 electron microscope (Hitachi, Japan). Small aggregated P2 proteins are also observed in the micrographs, which are indicated by arrowheads. The bar represents 50 nm. (d) Selected class-averaged images. The width of each image is 40.1 nm. A histogram of the lengths of the P2 proteins is presented later. The lengths of the P2 proteins were measured by tracing the centre of the filament in each class-averaged image. All 50 class-averaged images are shown in the Supplementary Data (Supplementary Fig. S2). (e) Schematic representation of the P2 structure.
    Rice Dwarf Virus (Rdv), supplied by ACADEMIC PRESS INC, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rice+dwarf+virus+(rdv)/rice+dwarf+virus++rdv+/pm18640559-11-5-2
    Average 90 stars, based on 1 article reviews
    rice dwarf virus (rdv) - by Bioz Stars, 2026-11
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Overall structure of the isolated P2 protein. (a) SDS-PAGE of the structural proteins of RDV with and without CCl4 treatment. Intact RDV has seven kinds of proteins (Lane 2; P1–P3, P5, P7–P9 proteins). Lane 1, RDV particles lacking the P2 protein by CCl4 treatment used in the previous study (15); Lane 2, intact RDV particles containing the P2 protein (without CCl4 treatment) used in this study. P9 protein is appeared as several bands in SDS-PAGE (30). P9* is processed or degraded from a large polypeptide of P9 protein (P9). (b) SDS-PAGE and western blot analysis of the isolated P2 protein from intact RDV particles. The isolated P2 protein was separated by SDS-PAGE and then stained with Coomassie Brilliant Blue (left) or analysed by western blotting with RDV P2-specific antibodies (right). Lane 1, molecular weight markers; Lane 2, intact RDV particle; Lane 3, isolated P2 protein. (c) Electron micrograph of negatively stained P2 proteins isolated from intact RDV particles, which was recorded at a magnification of ×50,000 with an H7650 electron microscope (Hitachi, Japan). Small aggregated P2 proteins are also observed in the micrographs, which are indicated by arrowheads. The bar represents 50 nm. (d) Selected class-averaged images. The width of each image is 40.1 nm. A histogram of the lengths of the P2 proteins is presented later. The lengths of the P2 proteins were measured by tracing the centre of the filament in each class-averaged image. All 50 class-averaged images are shown in the Supplementary Data (Supplementary Fig. S2). (e) Schematic representation of the P2 structure.

    Journal: Journal of Biochemistry

    Article Title: Electron microscopic imaging revealed the flexible filamentous structure of the cell attachment protein P2 of Rice dwarf virus located around the icosahedral 5-fold axes

    doi: 10.1093/jb/mvv092

    Figure Lengend Snippet: Overall structure of the isolated P2 protein. (a) SDS-PAGE of the structural proteins of RDV with and without CCl4 treatment. Intact RDV has seven kinds of proteins (Lane 2; P1–P3, P5, P7–P9 proteins). Lane 1, RDV particles lacking the P2 protein by CCl4 treatment used in the previous study (15); Lane 2, intact RDV particles containing the P2 protein (without CCl4 treatment) used in this study. P9 protein is appeared as several bands in SDS-PAGE (30). P9* is processed or degraded from a large polypeptide of P9 protein (P9). (b) SDS-PAGE and western blot analysis of the isolated P2 protein from intact RDV particles. The isolated P2 protein was separated by SDS-PAGE and then stained with Coomassie Brilliant Blue (left) or analysed by western blotting with RDV P2-specific antibodies (right). Lane 1, molecular weight markers; Lane 2, intact RDV particle; Lane 3, isolated P2 protein. (c) Electron micrograph of negatively stained P2 proteins isolated from intact RDV particles, which was recorded at a magnification of ×50,000 with an H7650 electron microscope (Hitachi, Japan). Small aggregated P2 proteins are also observed in the micrographs, which are indicated by arrowheads. The bar represents 50 nm. (d) Selected class-averaged images. The width of each image is 40.1 nm. A histogram of the lengths of the P2 proteins is presented later. The lengths of the P2 proteins were measured by tracing the centre of the filament in each class-averaged image. All 50 class-averaged images are shown in the Supplementary Data (Supplementary Fig. S2). (e) Schematic representation of the P2 structure.

    Article Snippet: Abbreviations CCD charge-coupled device CPV Cytoplasmic polyhedrosis virus cryo-EM cryo-electron microscopy dsRNA double-stranded RNA RDV Rice dwarf virus SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electrophoresis 3D three-dimensional

    Techniques: Isolation, SDS Page, Western Blot, Staining, Molecular Weight, Microscopy

    Proposed model of cell entry by Rice dwarf virus (RDV) P2 proteins with an L-shaped structure are docked in the large crevasses around icosahedral 5-fold axes. RDV particles attach to the host cellular membrane via interactions between the P2 proteins and as-yet unidentified receptor molecules. Then, the RDV particles enter the host cell via the clathrin-mediated endocytosis pathway (13).

    Journal: Journal of Biochemistry

    Article Title: Electron microscopic imaging revealed the flexible filamentous structure of the cell attachment protein P2 of Rice dwarf virus located around the icosahedral 5-fold axes

    doi: 10.1093/jb/mvv092

    Figure Lengend Snippet: Proposed model of cell entry by Rice dwarf virus (RDV) P2 proteins with an L-shaped structure are docked in the large crevasses around icosahedral 5-fold axes. RDV particles attach to the host cellular membrane via interactions between the P2 proteins and as-yet unidentified receptor molecules. Then, the RDV particles enter the host cell via the clathrin-mediated endocytosis pathway (13).

    Article Snippet: Abbreviations CCD charge-coupled device CPV Cytoplasmic polyhedrosis virus cryo-EM cryo-electron microscopy dsRNA double-stranded RNA RDV Rice dwarf virus SDS-PAGE sodium dodecyl sulfate-polyacrylamide gel electrophoresis 3D three-dimensional

    Techniques: