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1 BPV-1 E6 preferentially associated with membrane-bound A
2 BPV-1 E6 was further shown to be recruited to isolated G
3 BPV-1 E6 was introduced into C127 cells (PBE6) by retrov
4 BPV-1 E7 was observed in the cytoplasm of basal and lowe
5 BPV-1 efficiently induces anchorage-independent growth a
6 BPV-1 has served as the prototype for studies of the mol
7 BPV-1 Y102E was unable to bind E1 and did not replicate
8 BPV-1-induced papillomas show characteristics of repress
12 discovered that the bovine papillomavirus 1 (BPV-1) transcription and replication regulator E2 is pho
13 the hitchhiking of bovine papillomavirus-1 (BPV-1), and the viral protein E2 binds to both plasmids
14 lexes of the bovine papillomavirus strain 1 (BPV-1) E2 protein and DNA show that the protein does not
15 V-16) E2 and bovine papillomavirus strain 1 (BPV-1) E2 to discriminate among binding sites with diffe
17 product of the bovine papillomavirus type 1 (BPV-1) E1 translational open reading frame is required f
18 tion domain of bovine papillomavirus type 1 (BPV-1) E2 alone or this binding domain plus the adjacent
20 For example, bovine papillomavirus type 1 (BPV-1) E2 binds to all chromosomes as small speckles in
21 shown that the bovine papillomavirus type 1 (BPV-1) E6 and E7 genes independently sensitize mouse cel
22 pillomaviruses Bovine Papillomavirus Type 1 (BPV-1) E6 and human papillomavirus (HPV) types 1 and 8 (
30 containing the bovine papillomavirus type 1 (BPV-1) genome were reported to exhibit increased TNF sen
31 oncoprotein of bovine papillomavirus type 1 (BPV-1) has been shown to transform cells through a p53-i
34 E6 gene of the bovine papillomavirus type 1 (BPV-1) is expressed in fibropapillomas caused by BPV-1 a
35 oncoprotein of bovine papillomavirus type 1 (BPV-1) is required for the full transformation activity
38 selection of a bovine papillomavirus type 1 (BPV-1) late-specific splice site, and binding of SRp20 t
40 Furthermore, bovine papillomavirus type 1 (BPV-1) transformation was also suppressed in cells co-tr
41 nital HPV, and bovine papillomavirus type 1 (BPV-1), a papillomavirus known to be transmitted via fom
44 in, encoded by bovine papillomavirus type 1 (BPV-1), has been shown to interact with basal transcript
48 tion although this result also occurred in a BPV-1 E2 mutant lacking a previously identified phosphor
49 Deletion or mutation of either element in a BPV-1 late pre-mRNA switches splicing to the late-specif
54 he phospho-acceptor sites of both HPV-16 and BPV-1 L2 resulted in the production of infectious virus
55 Our studies thus categorize HPV-18 E2 and BPV-1 E2 in the same protein family, a finding consisten
58 n between Saccharomyces cerevisiae TFIIB and BPV-1 E2, an observation that is consistent with the imp
59 effector of NOTCH-induced transcription, and BPV-1 E6 represses synthetic NOTCH-responsive promoters,
60 n human TFIIB (hTFIIB) required for VP16 and BPV-1 E2 indicates that these acidic activators interact
65 uced transformation of cells expressing both BPV-1 E6 and E7, as well as E6 alone, suggesting that th
67 1) is expressed in fibropapillomas caused by BPV-1 and in tissue culture cells transformed by BPV-1.
76 together, our results suggest that cytosolic BPV-1 E6 is first recruited to the TGN, where it is then
77 tively active mutant form of FGFR3 decreased BPV-1 and HPV-31 transient replication although this res
79 oth forms have star-shaped capsomeres, as do BPV-1 and HPV-1, but the open CRPV capsids are approxima
81 selection of the proximal 3' splice site for BPV-1 RNA splicing in DT40-ASF cells, a genetically engi
83 DNA-binding domains of the E2 proteins from BPV-1 and human papillomavirus strain 16 (HPV-16) to a s
85 cteristic of many transformed cells, and, in BPV-1 transformed cells, may be mediated by BPV-1 E6 thr
87 ous residues required for E1 dimerization in BPV-1 and the low risk HPV-11 are also required for HPV-
90 or the processing of most BPV-1 pre-mRNAs in BPV-1-transformed C127 cells and at early to intermediat
91 We created a series of missense mutations in BPV-1 E1 at codons 295, 344-345, 446, 464, 466, 497-498,
93 pression, we investigated the role of p53 in BPV-1 E6 and E7 modulation of Fas-mediated apoptosis.
95 only one E2 tyrosine phosphorylation site in BPV-1 (tyrosine 102) and one in HPV-16/31 (tyrosine 138)
96 ereby papillomavirus oncoproteins, including BPV-1 E6, and the cancer-associated HPV-8 E6 repress NOT
99 ression of E7 and E5 in basal keratinocytes, BPV-1 E7 cooperated with E5 as well as E6 in an anchorag
100 d superficial differentiating keratinocytes, BPV-1 E7 is only observed in basal and lower spinous epi
102 nt) 3225, is used for the processing of most BPV-1 pre-mRNAs in BPV-1-transformed C127 cells and at e
110 ESS) is juxtaposed immediately downstream of BPV-1 splicing enhancer 1 and negatively modulates selec
111 Our studies indicate that expression of BPV-1 E7 induces DNA synthesis and stimulates cells to e
112 Our results indicate that expression of BPV-1 E7 sensitizes cells to tumor necrosis factor alpha
113 ysiological conditions for the expression of BPV-1 late RNAs and for selection of the proximal 3' spl
118 e actin fiber network, and overexpression of BPV-1 E6 led to disruption of actin fiber formation.
119 nhibit gene expression of the E6 promoter of BPV-1 (bovine papillomavirus type 1) and HPV types 16 an
121 embranes, suggesting that the recruitment of BPV-1 E6 and AP-1 to Golgi membranes involves a common f
123 the frequency of morphological reversion of BPV-1 transformed C127 cells resulting in the complete e
125 kles do not contain Brd4, and unlike that of BPV-1, the N-terminal Brd4-interacting domain of HPV-8 E
128 of the tumour viruses bovine papillomavirus (BPV-1) and Simian virus 40 (SV40) are the initiator prot
130 ta indicate the utility of ts against H-ras, BPV-1 and HPV-16 promoters and their respective oncogene
131 ious studies of the mechanisms that regulate BPV-1 alternative splicing identified three cis-acting e
142 6 E2 DNA binding domain (HPV16-E2/D) and the BPV-1 E2 DNA binding domain (BPV1-E2/D) to sites bearing
143 y, we demonstrate an interaction between the BPV-1 E6 protein and AP-1, the TGN (trans-Golgi network)
145 nstrated that suppression of splicing by the BPV-1 ESS requires an upstream suboptimal 3' splice site
146 rted downstream of the 3' splice site in the BPV-1 late pre-mRNA, Rous sarcoma virus src pre-mRNA, hu
148 us, these data suggest that selection of the BPV-1 nt 3225 3' splice site is regulated by both positi
149 SE2 are required for preferential use of the BPV-1 nucleotide (nt) 3225 3' splice site in nonpermissi
150 e cancer-related human papillomaviruses, the BPV-1 E7 protein does not associate efficiently with the
151 e-dependent DNA helicase, DNA binding to the BPV-1 origin of viral DNA replication, and association w
152 (HPV-16) p97 promoter has similarity to the BPV-1 p89 promoter, the ability of ts to suppress p97 wa
153 ptor 3 (FGFR3) coimmunoprecipitated with the BPV-1 E2 protein, as did human papillomavirus 31 (HPV-31
157 isingly, HPV-18 E2 behaves more similarly to BPV-1 E2 than HPV-16 E2 in its functional properties.
158 This study examines the mechanisms by which BPV-1 E6 association with the cellular focal adhesion ad
159 de mice, we have developed a system in which BPV-1 can replicate and produce infectious viral particl
160 urthermore, AP-1 proteins could compete with BPV-1 E6 for binding to Golgi membranes, suggesting that
161 also suppressed in cells co-transfected with BPV-1 plus ts and in ts expressing cell lines transfecte
163 tructure of the core domain contained within BPV-1 E2 is similar to the corresponding regions of othe