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1 egions in the membrane fusion protein of the Visna virus.
2 er region of the prototype lentivirus, maedi visna virus.
3 protein (SU) gp135 of the lentiviruses maedi-visna virus and caprine arthritis-encephalitis virus (CA
4 s activators of two nonprimate lentiviruses, visna virus and equine infectious anemia virus, revealed
5 s), ERK-1/2, in primary cells susceptible to visna virus and report that virus infection induces and
6 unodeficiency virus, Jembrana disease virus, visna virus, and caprine arthritis encephalitis virus.
7 ases of human immunodeficiency virus type 1, visna virus, and Rous sarcoma virus exhibited different
8 ns of human immuno- deficiency virus type 1, visna virus, and Rous sarcoma virus exhibited distinct p
9 itive, biologically relevant system to study visna virus cell entry and envelope-receptor interaction
10 type viruses, supporting the notion that the visna virus cellular receptor is a widely expressed prot
11 Based on those results, additional HIV-1/visna virus chimeric integrases were designed and purifi
12 alpha- and gamma-retroviruses, and the maedi visna virus dimer linkage region is capable of forming h
13 virus (MuLV) particles pseudotyped with the visna virus envelope glycoprotein and encoding a green f
14 re obtained when the cytoplasmic tail of the visna virus envelope TM protein was truncated to 3, 7, o
15 s of human immunodeficiency virus type 1 and visna virus guided the quantitative testing of oligonucl
16 rs not only in cells classically infected by visna virus (i.e., macrophages and microglia), but also
18 of ERK-1/2 activation in brains derived from visna virus-infected sheep demonstrates a strong correla
21 substitutions at the analogous positions in visna virus integrase and Rous sarcoma virus integrase c
27 The small-ruminant lentiviruses ovine maedi-visna virus (MVV) and caprine arthritis-encephalitis vir
28 m bovine immunodeficiency virus (BIV), maedi-visna virus (MVV) and equine infectious anemia virus (EI
34 n interactions with cellular proteins at the visna virus promoter, we used an in vitro protein affini
39 inhibitor of the ERK/MAPK pathway, abolishes visna virus replication, as evidenced by extremely low l
40 cells not considered to be major targets of visna virus replication, suggesting that activation of t
41 at proximal to the viral TATA box, where the visna virus Tat activation domain could contact TBP to a
47 n in vivo two-hybrid assay, to show that the visna virus Tat protein specifically interacts with the
49 ike other lentiviral transactivators such as visna virus Tat, is unable to transactivate from minimal
50 from human immunodeficiency virus type 1 and visna virus were able to substitute for the EIAV slipper
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