Dimerization of the human papillomavirus E7 oncoprotein in vivo.
about
Structure of the human Papillomavirus E7 oncoprotein and its mechanism for inactivation of the retinoblastoma tumor suppressorThe canine papillomavirus and gamma HPV E7 proteins use an alternative domain to bind and destabilize the retinoblastoma protein.The human papillomavirus E7 oncoprotein functionally interacts with the S4 subunit of the 26 S proteasome.Potent anti-tumor effect generated by a novel human papillomavirus (HPV) antagonist peptide reactivating the pRb/E2F pathway.The nuclear localization of low risk HPV11 E7 protein mediated by its zinc binding domain is independent of nuclear import receptors.Biological activities and molecular targets of the human papillomavirus E7 oncoprotein.The high-risk HPV16 E7 oncoprotein mediates interaction between the transcriptional coactivator CBP and the retinoblastoma protein pRb.Recombinant HPV16 E7 assembled into particles induces an immune response and specific tumour protection administered without adjuvant in an animal modelE6^E7, a novel splice isoform protein of human papillomavirus 16, stabilizes viral E6 and E7 oncoproteins via HSP90 and GRP78.Systematic analysis of the amino acid residues of human papillomavirus type 16 E7 conserved region 3 involved in dimerization and transformation.Analysis of the p53-mediated G1 growth arrest pathway in cells expressing the human papillomavirus type 16 E7 oncoproteinBoth conserved region 1 (CR1) and CR2 of the human papillomavirus type 16 E7 oncogene are required for induction of epidermal hyperplasia and tumor formation in transgenic mice.Mechanisms of human papillomavirus-induced oncogenesis.Human papillomavirus type 16 E7 oncoprotein associates with E2F6.Identification of the nuclear localization and export signals of high risk HPV16 E7 oncoprotein.The papillomavirus E7 proteins.The human papillomavirus E7 oncoprotein.The human papillomavirus E7 oncoprotein as a regulator of transcription.Human papillomavirus E7 proteins stimulate proliferation independently of their ability to associate with retinoblastoma protein.Structural basis for interaction between the Ubp3 deubiquitinating enzyme and its Bre5 cofactor.
P2860
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P2860
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@en
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@nl
type
label
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@en
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@nl
prefLabel
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@en
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@nl
P2093
P356
P1433
P1476
Dimerization of the human papillomavirus E7 oncoprotein in vivo.
@en
P2093
P304
P356
10.1006/VIRO.1995.9926
P407
P50
P577
1995-12-01T00:00:00Z