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1 ared exon led to greatly decreased levels of Pol protein.
2 pression, cleavage, and incorporation of the Pol protein.
3 ate a panel of six MAbs directed against HBV Pol protein.
4 ive if they are synthesized as part of a Gag-Pol protein.
5 pparently normal levels of processed Gag and Pol proteins.
6 with similarity to mammalian retroviral Gag-Pol proteins.
7 33 amino acid sequences from the retroviral Pol proteins.
8 ev and simian immunodeficiency virus Gag and Pol proteins.
9 y active response, recognizing gag, env, and pol proteins.
10 ed to be essential for processing of Gag and Pol proteins.
11 ay be exploited to study the function of the Pol proteins.
12 We found that efficient intracellular Gag-Pol protein accumulation required the region between the
13 (HIV) virions have a lattice of Gag and Gag-Pol proteins anchored to the lumen of their envelope.
14 s, among which unspliced RNA encodes Gag and Pol proteins and a singly spliced mRNA encodes Env prote
15 that express the JSRV Env and the MoMLV Gag-Pol proteins and can produce JSRV-pseudotype vectors at
16 rmine the cleavage sites in the WDSV Pro and Pol proteins and to characterize the viral protease (PR)
21 velope [ENV]) and nonstructural (polymerase [POL]) proteins at the CD8+ cytotoxic T lymphocyte (CTL)
22 nts determines the ratio of viral Gag to Gag-Pol proteins available for viral particle morphogenesis,
24 e or absence of the spliced Pol, the PFV Gag-Pol proteins can assemble into virus-like particles (VLP
27 cines expressing structurally intact gag and pol proteins drive immunofocused CD8 responses that redu
32 f, Vpr, and Vpu), in addition to the Gag and Pol proteins, for particle formation and virus stock pro
34 irus system via coexpression of HBV core and Pol proteins from either a single RNA (i.e., in cis) or
38 ate levels of Gag-Pol precursors and cleaved Pol proteins in the transfected cells were not affected
39 tion, which include the packaging of cleaved Pol proteins in viral particles, a process which may inv
43 ic studies presented here establish how Prim-Pol proteins instigate primer synthesis, revealing the r
44 target dominant negative mutants of the HIV Pol proteins into virions, we fused HIV-2 Vpx with an en
50 n in trans between murine leukemia virus Gag-Pol proteins lacking polymerase and RNase H activities r
51 showed an approximately 16-fold reduction in Pol protein levels, whereas the levels of Pol proteins w
53 composed of conserved regions of the Gag and Pol proteins matched to at least 80% globally circulatin
54 ions, including dominant negative mutants of Pol proteins, may provide new opportunities for applicat
55 the simian immunodeficiency virus (SIV) Gag-Pol proteins (MVA-gag-pol) was explored in rhesus monkey
57 ed and either are used to encode Gag and Gag-Pol proteins or are packaged into virions as genomic RNA
59 crease in antibody reactivity to HIV Gag and Pol proteins, patients with advanced HIV-1 infection rem
60 and E(1419)/G(1420)) within the 75.7-kDa Pro-Pol protein previously mapped in bacterial expression st
62 frameshifting event required to express the Pol proteins protease, integrase, and reverse transcript
63 ytic domain is conserved in other PP2Cs, the POL protein represents a unique subclass of plant PP2Cs.
66 of VSV vectors expressing SHIV Env, Gag, and Pol proteins to that of a protocol consisting of a VSV v
68 core protein, and functional domains of the Pol protein were highly conserved in all of the new isol
69 in Pol protein levels, whereas the levels of Pol proteins were only marginally reduced in mutant viri
71 , encodes homologs of retroviral Gag and Gag-Pol proteins, which, together with genomic RNA, assemble
72 f the spliced Pol, coexpression of a PFV Gag-Pol protein with Gag can produce infectious virions.
73 n alter its sequence within both the Gag and Pol proteins with potential functional consequences for
74 ng immunizations of DNA encoding SIV Gag and Pol proteins, with control macaques receiving vector DNA
76 mutants expressing Gag and Pol only as a Gag-Pol protein without the spliced Pol contain protease act