Výsledky vyhledávání - "Wendy M, Havens"

Heterodimers as the Structural Unit of the T=1 Capsid of the Fungal Double-Stranded RNA Rosellinia necatrix Quadrivirus 1

Autor: Josué Gómez-Blanco, Benes L. Trus, Satoko Kanematsu, Daniel Luque, Joséa R. Castón, Carlos Alfonso, Carlos P. Mata, Germán Rivas, Wendy M. Havens, José M. González, Said A. Ghabrial, Nobuhiro Suzuki, Fernando González-Camacho

Publikováno v: Journal of Virology. 90:11220-11230

Most double-stranded RNA (dsRNA) viruses are transcribed and replicated in a specialized icosahedral capsid with a T=1 lattice consisting of 60 asymmetric capsid protein (CP) dimers. These capsids help to organize the viral genome and replicative com

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a21355a8fb97b91cff5e2149c1e831f
https://doi.org/10.1128/jvi.01013-16

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Overexpression ofGmCaM4in soybean enhances resistance to pathogens and tolerance to salt stress

Autor: Said A. Ghabrial, Glen L. Hartman, Schuyler S. Korban, Ajay Singh, Danman Zheng, J. S. Haudenshield, Mohamed H. El-Habbak, Suryadevara S. Rao, Laura Vaughn, Wendy M. Havens

Publikováno v: Molecular Plant Pathology. 15:145-160

Plant diseases inflict heavy losses on soybean yield, necessitating an understanding of the molecular mechanisms underlying biotic/abiotic stress responses. Ca(2) (+) is an important universal messenger, and protein sensors, prominently calmodulins (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1eb11e7feabac13e27c78826cf44b9a7
https://doi.org/10.1111/mpp.12075

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RNA Sequence Determinants of a Coupled Termination-Reinitiation Strategy for Downstream Open Reading Frame Translation in Helminthosporium victoriae Virus 190S and Other Victoriviruses (Family Totiviridae)

Autor: Hua Li, Wendy M. Havens, Max L. Nibert, Said A. Ghabrial

Publikováno v: Journal of Virology. 85:7343-7352

The genome-length, dicistronic mRNA of the double-stranded RNA fungal virus Helminthosporium victoriae virus 190S (genus Victorivirus , family Totiviridae ) contains two long open reading frames (ORFs) that overlap in the tetranucleotide AUGA. Transl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7adbe63770be207b2aac27e1995f27ef
https://doi.org/10.1128/jvi.00364-11

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Backbone Trace of Partitivirus Capsid Protein from Electron Cryomicroscopy and Homology Modeling

Autor: Yizhi Jane Tao, Max L. Nibert, Wendy M. Havens, Tom S. Y. Guu, Wendy F. Ochoa, Timothy S. Baker, Jinghua Tang, Said A. Ghabrial, Junhua Pan

Publikováno v: Biophysical Journal. 99:685-694

Most dsRNA viruses have a genome-enclosing capsid that comprises 120 copies of a single coat protein (CP). These 120 CP subunits are arranged as asymmetrical dimers that surround the icosahedral fivefold axes, forming pentamers of dimers that are tho

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https://doi.org/10.1016/j.bpj.2010.04.058

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Atomic structure reveals the unique capsid organization of a dsRNA virus

Autor: Said A. Ghabrial, Yizhi Jane Tao, Wendy M. Havens, Timothy S. Baker, Li Lin, Wendy F. Ochoa, Robert S. Sinkovits, Junhua Pan, Max L. Nibert, Liping Dong

Publikováno v: Proceedings of the National Academy of Sciences. 106:4225-4230

For most dsRNA viruses, the genome-enclosing capsid comprises 120 copies of a single capsid protein (CP) organized into 60 icosahedrally equivalent dimers, generally identified as 2 nonsymmetricallyinteracting CP molecules with extensive lateral cont

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c28bc0e7962e486203c8a57a823234e8
https://doi.org/10.1073/pnas.0812071106

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Partitivirus Structure Reveals a 120-Subunit, Helix-Rich Capsid with Distinctive Surface Arches Formed by Quasisymmetric Coat-Protein Dimers

Autor: Max L. Nibert, Said A. Ghabrial, Robert S. Sinkovits, Timothy S. Baker, Wendy F. Ochoa, Wendy M. Havens

Publikováno v: Structure. 16:776-786

Two distinct partitiviruses, Penicillium stoloniferum viruses S and F, can be isolated from the fungus Penicillium stoloniferum. The bisegmented dsRNA genomes of these viruses are separately packaged in icosahedral capsids containing 120 coat-protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c678d0d6807b5f7853d3921c761f4ff
https://doi.org/10.1016/j.str.2008.02.014

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The victorivirus Helminthosporium victoriae virus 190S is the primary cause of disease/hypovirulence in its natural host and a heterologous host

Autor: Yu Hsin Lin, Said A. Ghabrial, Jiatao Xie, Wendy M. Havens, Nobuhiro Suzuki

Publikováno v: Virus research. 213

A transmissible disease of the plant pathogenic fungus Helminthosporium victoriae, the causal agent of Victoria blight of oats, was reported more than 50 years ago. Diseased, but not normal, isolates, of H. victoriae contain two distinct viruses desi

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https://pubmed.ncbi.nlm.nih.gov/27208849

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Reprint of 'The victorivirus Helminthosporium victoriae virus 190S is the primary cause of disease/hypovirulence in its natural host and a heterologous host'

Autor: Jiatao Xie, Wendy M. Havens, Yu-Hsin Lin, Nobuhiro Suzuki, Said A. Ghabrial

Publikováno v: Virus research. 219

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https://pubmed.ncbi.nlm.nih.gov/26724750

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Disease Phenotype of Virus-Infected Helminthosporium victoriae Is Independent of Overexpression of the Cellular Alcohol Oxidase/RNA-Binding Protein Hv-p68

Autor: Wendy M. Havens, Said A. Ghabrial, Tianyong Zhao

Publikováno v: Phytopathology®. 96:326-332

The cellular protein Hv-p68 is a novel alcohol oxidase/RNA-binding protein that is overexpressed in virus-infected isolates of the plant-pathogenic fungus Helminthosporium victoriae (teleomorph: Cochliobolus victoriae). Overproduction of Hv-p68 has b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44ba128f68439351cdb45de22b030e4e
https://doi.org/10.1094/phyto-96-0326

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Cryo-EM near-atomic structure of a dsRNA fungal virus shows ancient structural motifs preserved in the dsRNA viral lineage

Autor: Axel F. Brilot, Daniel Luque, Wendy M. Havens, Said A. Ghabrial, Josué Gómez-Blanco, Benes L. Trus, Damià Garriga, José R. Castón, Núria Verdaguer, José L. Carrascosa, José M. González

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
Repisalud
Instituto de Salud Carlos III (ISCIII)

Viruses evolve so rapidly that sequence-based comparison is not suitable for detecting relatedness among distant viruses. Structure-based comparisons suggest that evolution led to a small number of viral classes or lineages that can be grouped by cap

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da5a8259805611cde9542dc769641c42
http://hdl.handle.net/10261/110125

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