Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Y. Vivienne Marsh"'
Autor:
Brian Bloor Schryver, Deborah A. Eppstein, Carole G. Kurahara, Y. Vivienne Marsh, Marjorie A. Larsen
Publikováno v:
Journal of Interferon Research. 3:305-311
The 5′ terminally-dephosphorylated "core" of the 2′-5′ linked adenylate oligomer ppp (A2′p)2A, termed 2-5A core [(A2′p)2A], exerts an antimitogenic effect when added to serum-stimulated 3T3 fibrobl...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4469f67a0e46596da80e036256e06a77
https://doi.org/10.1089/jir.1983.3.305
https://doi.org/10.1089/jir.1983.3.305
Publikováno v:
Antiviral Research. 5:137-144
The acyclic nucleoside 9-(1,3-dihydroxy-2-propoxymethyl)guanine (DHPG) and recombinant mouse interferon gamma (rMuIFN-gamma) were evaluated for their efficacy alone and in combination against a herpes simplex virus type 2 systemic infection in mice.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58a6b90144c4d8bc9615212f10c568bc
https://doi.org/10.1016/0166-3542(85)90046-4
https://doi.org/10.1016/0166-3542(85)90046-4
Autor:
Y. Vivienne Marsh, Deborah A. Eppstein
Publikováno v:
Journal of Interferon Research. 3:161-168
Murine fibroblast interferon (MuIFN, 90% beta, 10% alpha) was associated with both positively and negatively charged liposomes formed by reverse-phase evaporation. This interferon-liposome association occurred predominantly in a manner that resulted
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c88f49ea88612b89361f552a4a6ffa1
https://doi.org/10.1089/jir.1983.3.161
https://doi.org/10.1089/jir.1983.3.161
Autor:
Y. Vivienne Marsh, Deborah A. Eppstein
Publikováno v:
Biochemical and Biophysical Research Communications. 120:66-73
DHPG, an acyclic guanine nucleoside with the structure 9-[(1,3-dihydroxy-2-propoxy)methyl]-guanine], showed potent synergism with recombinant α of β interferons and modest synergism with γ interferon in inhibiting the replication of herpes simplex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::203175308eb374ebe962dbf4e7e7e3b3
https://doi.org/10.1016/0006-291x(84)91414-1
https://doi.org/10.1016/0006-291x(84)91414-1
Autor:
George J. Todaro, Sherry R. Newman, John J. Nestor, Alain B. Schreiber, Deborah A. Eppstein, Y. Vivienne Marsh
Publikováno v:
Nature. 318:663-665
Vaccinia virus encodes VGF, an early protein of relative molecular mass 19,000 (19K) which, from amino-acid residues 45 to 85, is homologous in 19 residues to epidermal growth factor (EGF), and transforming growth factor-alpha (TGF-alpha). The conser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1ea8c3aff946498cc4e50322937785b
https://doi.org/10.1038/318663a0
https://doi.org/10.1038/318663a0
Autor:
Gilles Gosselin, Abd El Fattah Haikal, Claude Chavis, Jean-Louis Imbach, Deborah A. Eppstein, Y. Vivienne Marsh, Brian B. Schryver
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a1cf5bb2c3133ca5f7382daca9c5a60
https://doi.org/10.1016/b978-0-12-587980-4.50014-5
https://doi.org/10.1016/b978-0-12-587980-4.50014-5
Publikováno v:
Virology. 131(2)
(XyloA2′p)2xyloA, the xyloadenosine core analog of the interferon mediator 2–5A [ppp(A2′p)2A], was found to exhibit potent antiviral activity against herpes simplex viruses 1 and 2 (D. A. Eppstein, J. W. Barnett, Y. V. Marsh, G. Goselin, and J.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::030098aa1093734cb9fd0b0476857f2e
https://pubmed.ncbi.nlm.nih.gov/6318435
https://pubmed.ncbi.nlm.nih.gov/6318435
Autor:
Deborah A. Eppstein, Y. Vivienne Marsh
Publikováno v:
Journal of cellular biochemistry. 34(4)
We previously demonstrated that occupancy of the epidermal growth factor (EGF) receptor reduced the ability of vaccinia virus to infect L cells [Eppstein et al: Nature 318:663, 1985]. This result suggested that vaccinia virus was utilizing the EGF re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::917eb53cf308448b57117a0f52b0a2f2
https://pubmed.ncbi.nlm.nih.gov/3497935
https://pubmed.ncbi.nlm.nih.gov/3497935