CoChat
Sign Up
Cited by 285

The DOI matches its Crossref record, with a small difference in title or year; 3 of the 3 references it cites were found in a registry or an index.

Inactivation of Interferon Regulatory Factor-1 Tumor Suppressor Protein by HPV E7 Oncoprotein

Park, Jong-Sup, Kim, Eun-Joo, Kwon, Ho-Jeong, Hwang, Eun-Seong, Namkoong, Sung-Eun, Um, Soo-Jong·2000·Journal of Biological Chemistry
DOI 10.1074/jbc.275.10.6764
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1074/jbc.275.10.6764

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Figures

FIG. 1 The interaction of IRF-1 with HPV E7. A , HPV-16 E7 specifically interacts with IRF-1 in yeast. B , both HPV-16 and HPV-11 E7 interacts with transcriptional activation domain ( TAD : 217-325) of IRF-1. Combinations of LexA DNA-binding domain fusions (IRF-1, IRF-1(1-166), IRF-1(217-325)) and VP16 transactivation domain fusions (16E6, 16E7, 11E7, 16E6/E7) were shown. The strength of interaction was analyzed by b -galactosidase assay. Units ( U ) are expressed in nmol/min/mg of total protein. C , physical interaction of HPV-16 E7 with IRF-1 in vitro . The GST pull-down assay was performed using purified GST-E7 protein and in vitro translated 35 S-labeled IRF-1. L indicates loading material used for binding assay. D , the interaction of IRF-1 with HPV E7 in mammalian cells. Transient transfections were performed in NIH-3T3 cells using (17 mer) 5 TATACAT reporter plasmid, Gal4 (DBD)-E7, and/or VP16 (TAD)-IRF-1 expression vector. After transfections, cells were harvested and extracted. The protein concentration and b -galactosidase activity were determined for the normalization of the CAT assay. Fold stimulation was calculated from the amount of CAT enzyme determined by CAT ELISA.
FIG. 1 The interaction of IRF-1 with HPV E7. A , HPV-16 E7 specifically interacts with IRF-1 in yeast. B , both HPV-16 and HPV-11 E7 interacts with transcriptional activation domain ( TAD : 217-325) of IRF-1. Combinations of LexA DNA-binding domain fusions (IRF-1, IRF-1(1-166), IRF-1(217-325)) and VP16 transactivation domain fusions (16E6, 16E7, 11E7, 16E6/E7) were shown. The strength of interaction was analyzed by b -galactosidase assay. Units ( U ) are expressed in nmol/min/mg of total protein. C , physical interaction of HPV-16 E7 with IRF-1 in vitro . The GST pull-down assay was performed using purified GST-E7 protein and in vitro translated 35 S-labeled IRF-1. L indicates loading material used for binding assay. D , the interaction of IRF-1 with HPV E7 in mammalian cells. Transient transfections were performed in NIH-3T3 cells using (17 mer) 5 TATACAT reporter plasmid, Gal4 (DBD)-E7, and/or VP16 (TAD)-IRF-1 expression vector. After transfections, cells were harvested and extracted. The protein concentration and b -galactosidase activity were determined for the normalization of the CAT assay. Fold stimulation was calculated from the amount of CAT enzyme determined by CAT ELISA.CC-BY · From the PDF
FIG. 2 HPV-E7 interferes with transcriptional activity of IRF-1. Mouse NIH-3T3 cells were transfected with combinations of IRF-1, HPV-16, and/or HPV-11 E7 expression vectors together with IRF-1-responsive IFNb promoter-CAT reporter plasmid. Data represent the mean 6 SD of at least three independent transfections. Fold stimulation was calculated by dividing the amount of CAT enzyme of treated cells by that of untreated control cells.
FIG. 2 HPV-E7 interferes with transcriptional activity of IRF-1. Mouse NIH-3T3 cells were transfected with combinations of IRF-1, HPV-16, and/or HPV-11 E7 expression vectors together with IRF-1-responsive IFNb promoter-CAT reporter plasmid. Data represent the mean 6 SD of at least three independent transfections. Fold stimulation was calculated by dividing the amount of CAT enzyme of treated cells by that of untreated control cells.CC-BY · From the PDF
FIG. 3 The amino-terminal domain of HPV-16 E7 is critical for the repression of IRF-1. A , the structure of HPV-16 E7 protein, where two amino-terminal deletion mutants of E7 are shown. B , transient transfections were performed in NIH-3T3 cells using IFNb promoterCAT reporter and indicated E7 mutants (E7wt, wild type; E7 D 6-10, deletion of amino acids 6-10; E7 D 21-24, deletion of amino acids 21-24, defective in pRb-binding). CAT ELISA was performed as described. C , the amino-terminal domain of HPV-16 E7 is required for the interaction with IRF-1. Yeast two-hybrid and b -galactosidase assays were performed as described.
FIG. 3 The amino-terminal domain of HPV-16 E7 is critical for the repression of IRF-1. A , the structure of HPV-16 E7 protein, where two amino-terminal deletion mutants of E7 are shown. B , transient transfections were performed in NIH-3T3 cells using IFNb promoterCAT reporter and indicated E7 mutants (E7wt, wild type; E7 D 6-10, deletion of amino acids 6-10; E7 D 21-24, deletion of amino acids 21-24, defective in pRb-binding). CAT ELISA was performed as described. C , the amino-terminal domain of HPV-16 E7 is required for the interaction with IRF-1. Yeast two-hybrid and b -galactosidase assays were performed as described.CC-BY · From the PDF
Image 4
CC-BY · From the PDF
Image 5
CC-BY · From the PDF
FIG. 4 HDAC is involved in the repression of IRF-1 by HPV-16 E7. Transient transfections were performed in NIH-3T3 cells using IFNb promoter-CAT reporter and HPV-16 E7 with increasing the amount of TSA, a typical inhibitor of HDAC. CAT ELISA was performed as described.
FIG. 4 HDAC is involved in the repression of IRF-1 by HPV-16 E7. Transient transfections were performed in NIH-3T3 cells using IFNb promoter-CAT reporter and HPV-16 E7 with increasing the amount of TSA, a typical inhibitor of HDAC. CAT ELISA was performed as described.CC-BY · From the PDF
Image 7
CC-BY · From the PDF
Image 8
CC-BY · From the PDF
FIG. 6 Schematic view on how HPV-E7 inactivates IRF-1 function. HPV-E7 is associated with HDAC through the direct interaction between Mi2 b and its carboxyl-terminal Zn finger (9). In addition, the amino-terminal domain of E7 interacts with the carboxyl-terminal transactivation domain ( TAD ) of IRF-1. IRF-1, a transcription factor, binds to IRF-1 response element ( IRFRE ) located on several IFNinducible genes, one example, an IFNb gene, and activates their gene expression. Upon HPV infection, HPV-E7 first associated with NuRD complex containing HDAC and then interacts with IRF-1. Because HDAC mediates the histone deacetylation of chromatin, such interactions could be responsible for the transcriptional repression of IRF-1 by HPV-E7 that is further implicated in the evasion of IRF-1-dependent immune response in cervical carcinogenesis.
FIG. 6 Schematic view on how HPV-E7 inactivates IRF-1 function. HPV-E7 is associated with HDAC through the direct interaction between Mi2 b and its carboxyl-terminal Zn finger (9). In addition, the amino-terminal domain of E7 interacts with the carboxyl-terminal transactivation domain ( TAD ) of IRF-1. IRF-1, a transcription factor, binds to IRF-1 response element ( IRFRE ) located on several IFNinducible genes, one example, an IFNb gene, and activates their gene expression. Upon HPV infection, HPV-E7 first associated with NuRD complex containing HDAC and then interacts with IRF-1. Because HDAC mediates the histone deacetylation of chromatin, such interactions could be responsible for the transcriptional repression of IRF-1 by HPV-E7 that is further implicated in the evasion of IRF-1-dependent immune response in cervical carcinogenesis.CC-BY · From the PDF

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 36

  1. Pfister, 1987, Adv. Cancer Res., 48, 113, 10.1016/S0065-230X(08)60691-0 · DOI
  2. zur Hausen, 1996, Biochim. Biophys. Acta, 1288, F55
  3. Mansur, 1993, Biochim. Biophys. Acta, 1155, 323
  4. Jensen-Durr, 1996, Trends Genet., 12, 270, 10.1016/0168-9525(96)81455-7 · DOI
  5. Jewers, 1992, J. Virol., 66, 1329, 10.1128/jvi.66.3.1329-1335.1992 · DOI
  6. Brokaw, 1994, Virology, 205, 603, 10.1006/viro.1994.1688 · DOI
  7. Huang, 1993, Mol. Cell. Biol., 13, 953
  8. Wu, 1993, J. Virol., 67, 2404
  9. Brehm, 1999, EMBO J., 18, 2449, 10.1093/emboj/18.9.2449 · DOI · Paper page
  10. Taniguchi, 1997, Biochim. Biophys. Acta, 1333, M9
  11. Kirchhoff, 1993, Nucleic Acids Res., 21, 2881, 10.1093/nar/21.12.2881 · DOI
  12. Ploegh, 1998, Science, 280, 248, 10.1126/science.280.5361.248 · DOI
  13. Timmers, 1989, J. Virol., 63, 1470, 10.1128/jvi.63.3.1470-1473.1989 · DOI
  14. Proffitt, 1997, FEBS Lett., 400, 141, 10.1016/S0014-5793(96)01375-0 · DOI
  15. Ronco, 1998, Genes Dev., 12, 2061, 10.1101/gad.12.13.2061 · DOI · Paper page
  16. Vojtek, 1993, Cell, 74, 205, 10.1016/0092-8674(93)90307-C · DOI
  17. Le Douarinm, 1995, Nucleic Acids Res., 23, 876, 10.1093/nar/23.5.876 · DOI
  18. Tora, 1989, Cell, 59, 477, 10.1016/0092-8674(89)90031-7 · DOI
  19. vom Baur, 1998, Genes Dev., 12, 1278, 10.1101/gad.12.9.1278 · DOI
  20. Schneider, 1996, BioTechniques, 20, 960, 10.2144/96206bm03 · DOI
  21. Um, 1998, J. Biol. Chem., 273, 20728, 10.1074/jbc.273.33.20728 · DOI
  22. Demers, 1996, J. Virol., 70, 6862, 10.1128/jvi.70.10.6862-6869.1996 · DOI
  23. Germain, 1994, Cell, 76, 287, 10.1016/0092-8674(94)90336-0 · DOI
  24. Rollins, 1991, Mol. Cell. Biol., 11, 3125
  25. Cromme, 1993, Br. J. Cancer, 67, 1372, 10.1038/bjc.1993.254 · DOI
  26. Cromme, 1994, Br. J. Cancer, 69, 1176, 10.1038/bjc.1994.231 · DOI
  27. Riethdorf, 1996, Am. J. Pathol., 149, 1469
  28. Kleine-Lowinski, 1999, Int. J. Cancer, 82, 6, 10.1002/(SICI)1097-0215(19990702)82:1<6::AID-IJC2>3.0.CO;2-3 · DOI
  29. Min, 1996, J. Immunol., 156, 3174, 10.4049/jimmunol.156.9.3174 · DOI
  30. Hobart, 1997, J. Immunol., 158, 4260, 10.4049/jimmunol.158.9.4260 · DOI
  31. Chatterjee-Kishore, 1998, J. Biol. Chem., 273, 16177, 10.1074/jbc.273.26.16177 · DOI
  32. Zhou, 1998, J. Immunol., 160, 3908, 10.4049/jimmunol.160.8.3908 · DOI
  33. Valente, 1998, J. Immunol., 161, 3719, 10.4049/jimmunol.161.7.3719 · DOI
  34. Schafer, 1998, J. Biol. Chem., 273, 2714, 10.1074/jbc.273.5.2714 · DOI
  35. Borchers, 1999, Arch. Virol., 144, 1539, 10.1007/s007050050609 · DOI
  36. Barnard, 1999, Virology, 259, 305, 10.1006/viro.1999.9771 · DOI

Cited by

See all 285

Metadata

Authors
Park, J.-S., Kim, E.-J., Kwon, H.-J., Hwang, E.-S., Namkoong, S.-E., & Um, S.-J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-03
Volume
275
Issue
10
Pages
6764-6769
ISSN
0021-9258
DOI
10.1074/jbc.275.10.6764
Cited by
285
References
3
Language
en
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review