Výsledky vyhledávání

Vaccinia Virus Glycoproteins A33, A34, and B5 Form a Complex for Efficient Endoplasmic Reticulum to trans -Golgi Network Transport

Autor: Amalia K. Earley, Brian M. Ward, Stephanie R. Monticelli, Raychel Stone, Christopher C. Norbury

Publikováno v: Journal of Virology. 94

Orthopoxviruses produce two, antigenically distinct, infectious enveloped virions termed intracellular mature virions and extracellular virions. Extracellular virions are required for cell-to-cell spread and pathogenesis. Specific to the extracellula

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7b88abd47707eacd9e1e35cf8b3c3f02
https://doi.org/10.1128/jvi.02155-19

Zobrazit plný text záznamu

Vaccinia Virus Glycoproteins A33, A34, and B5 Form a Complex for Efficient Endoplasmic Reticulum to

Autor: Stephanie R, Monticelli, Amalia K, Earley, Raychel, Stone, Christopher C, Norbury, Brian M, Ward

Publikováno v: J Virol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::60ad803dcd5972f864317e506df8c68a
https://pubmed.ncbi.nlm.nih.gov/31941777

Zobrazit plný text záznamu

The Ectodomain of the Vaccinia Virus Glycoprotein A34 Is Required for Cell Binding by Extracellular Virions and Contains a Large Region Capable of Interaction with Glycoprotein B5

Autor: Jessica Tate, Amalia K. Earley, Brian M. Ward, Stephanie R. Monticelli

Publikováno v: Journal of Virology. 93

An interaction between the orthopoxvirus glycoproteins A34 and B5 has been reported. The transmembrane and ectodomain of A34 are sufficient for interaction with B5, localization of B5 to the site of intracellular wrapping, and subsequent incorporatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24c7a99f938f1924395bd490b6a750db
https://doi.org/10.1128/jvi.01343-18

Zobrazit plný text záznamu

Influenza and respiratory syncytial virus detection in clinical specimens without nucleic acid extraction using FOCUS direct disc assay is substantially equivalent to the traditional methods and the FOCUS nucleic acid extraction–dependent RT-PCR assay

Autor: Anami Patel, Amy Leber, David Tierney, Dipeshkumar Jaiswal, Amalia K. Earley, Suresh B. Selvaraju, Marilyn A. Menegus

Publikováno v: Diagnostic Microbiology and Infectious Disease. 78:232-236

In this study, we evaluated FOCUS diagnostic's Flu A/B & RSV direct kit (Direct Disc assay), designed to detect influenza (FLU) and respiratory syncytial viruses (RSV) directly in clinical specimens without nucleic acid extraction. This novel 'sample

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48dd15f56538ba7e4efdee998ef55f6a
https://doi.org/10.1016/j.diagmicrobio.2013.11.016

Zobrazit plný text záznamu

Isolation of the mutagenic and DNA adduct-inducing components from a commercial preparation of HC Blue 1 using Salmonella (TA98) bioassay-directed HPLC fractionation

Autor: C.W. Jameson, A. Abu-Shakra, Ramesh C. Gupta, F.W. Kari, K. Earley, L. Johnson, Robert Langenbach

Publikováno v: Mutation Research/Genetic Toxicology. 260:377-385

In the present study we report the separation of the mutagenic impurities from the nitrophenylenediamine hair dye HC Blue 1. This was accomplished by bioassay-directed HPLC fractionation, using Salmonella strain TA98 and reverse phase HPLC analysis.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae5db00586711752fa0c895b85c11f70
https://doi.org/10.1016/0165-1218(91)90023-f

Zobrazit plný text záznamu

The vaccinia virus B5 protein requires A34 for efficient intracellular trafficking from the endoplasmic reticulum to the site of wrapping and incorporation into progeny virions

Autor: Brian M. Ward, Amalia K. Earley, Winnie M. Chan

Publikováno v: Journal of virology. 82(5)

The glycoproteins encoded by the vaccinia virus A34R and B5R genes are involved in intracellular envelope virus formation and are highly conserved among orthopoxviruses. A recombinant virus that has the A34R gene deleted and the B5R gene replaced wit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30dc74b8e8fe3de40ea86be53f4dd0de
https://pubmed.ncbi.nlm.nih.gov/18094183

Zobrazit plný text záznamu

Structural analysis of the C-CAM1 molecule for its tumor suppression function in human prostate cancer

Autor: J T, Hsieh, K, Earley, R C, Pong, Y, Wang, N T, Van, S H, Lin

Publikováno v: The Prostate. 41(1)

Recently, we demonstrated that expression of C-CAM1, an immunoglobulin (Ig)-like cell adhesion molecule (CAM), was diminished in both prostate intraepithelial neoplasia and cancer lesions, indicating that loss of C-CAM1 expression may be involved in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc8d71753f0dbf03396b0b6afc510d3d
https://pubmed.ncbi.nlm.nih.gov/10440873

Zobrazit plný text záznamu

Cell-CAM105 isoforms with different adhesion functions are coexpressed in adult rat tissues and during liver development

Autor: P H, Cheung, N L, Thompson, K, Earley, O, Culic, D, Hixson, S H, Lin

Publikováno v: The Journal of biological chemistry. 268(9)

The rat hepatocyte cell adhesion molecule cell-CAM105 has recently been shown to be composed of at least two isoforms. Expression of the two isoforms in different tissues and during fetal liver development in rats was studied by RNase protection usin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::def6fe0c69ed641278d3d7ba6435363a
https://pubmed.ncbi.nlm.nih.gov/8454589

Zobrazit plný text záznamu

DNA adducts of the antitumor agent diaziquone

Autor: R C, Gupta, A, Garg, K, Earley, S C, Agarwal, G R, Lambert, S, Nesnow

Publikováno v: Cancer research. 51(19)

We have studied adduct formation of the antineoplastic agent diaziquone (AZQ; NSC 182986) with DNA and nucleotides in vitro. The aziridine moieties of AZQ can be expected to interact covalently with DNA which, in turn, presumably elicits the antitumo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7a9c6c11e21d297f54cbb8db2302075f
https://pubmed.ncbi.nlm.nih.gov/1913643

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání