Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Hara P. Ghosh"'
Autor:
Tomoko Maruyama, Mika Sakurai-Yageta, Hara P. Ghosh, Shinji Kikuchi, Yoshinori Murakami, Mari Masuda, Yuko N. Williams
Publikováno v:
Journal of Biological Chemistry. 280:42164-42171
The tumor suppressor in lung cancer 1 (TSLC1/IGSF4) encodes an immunoglobulin-superfamily cell adhesion molecule whose cytoplasmic domain contains a protein 4.1-binding motif (protein 4.1-BM) and a PDZ-binding motif (PDZ-BM). Loss of TSLC1 expression
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e6cee4cdff6ea338cea58884c1d622b
https://doi.org/10.1074/jbc.m507136200
https://doi.org/10.1074/jbc.m507136200
Publikováno v:
Oncogene. 23:5632-5642
The TSLC1 tumor-suppressor gene is silenced in a number of human cancer tissues and cell lines, including lung, prostate, liver, stomach, pancreatic, and breast cancers. Expression of TSLC1 in a non-small-cell lung cancer (NSCLC) cell line A549 suppr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ec55c0f61c19ce0d0e35ea6385f398a
https://doi.org/10.1038/sj.onc.1207756
https://doi.org/10.1038/sj.onc.1207756
Publikováno v:
Journal of Virology. 77:12807-12818
The glycoprotein (G) of vesicular stomatitis virus (VSV) is responsible for binding of virus to cells and for mediating virus entry following endocytosis by inducing fusion of the viral envelope with the endosomal membrane. The fusion peptide of G is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb3d520e71c3d808d76a8f3554916a5e
https://doi.org/10.1128/jvi.77.23.12807-12818.2003
https://doi.org/10.1128/jvi.77.23.12807-12818.2003
Publikováno v:
Virology. 310:319-332
The fusogenic envelope glycoprotein G of the rhabdovirus vesicular stomatitis virus (VSV) induces membrane fusion at acidic pH. At acidic pH the G protein undergoes a major structural reorganization leading to the fusogenic conformation. However, unl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09946943906a97ad7286f64e57bf7a5c
https://doi.org/10.1016/s0042-6822(03)00146-6
https://doi.org/10.1016/s0042-6822(03)00146-6
Autor:
Tadaichi Kitamura, Hiroshi Fukuhara, Masataka Onizuka, Yoshinori Murakami, Masami Kuramochi, Takao Sekiya, Minoru Isomura, Takamasa Kanbe, Mathew T. Pletcher, Takahiro Nobukuni, Roger H. Reeves, Tomoko Maruyama, Hara P. Ghosh
Publikováno v:
Nature Genetics. 27:427-430
The existence of tumor-suppressor genes was originally demonstrated by functional complementation through whole-cell and microcell fusion1,2. Transfer of chromosome 11 into a human non-small-cell lung cancer (NSCLC) cell line, A549, suppresses tumori
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af5c18b75325bfecd430f329347f9682
https://doi.org/10.1038/86934
https://doi.org/10.1038/86934
Autor:
Kakoli Ghosh, Hara P. Ghosh
Publikováno v:
Biochemistry and Cell Biology. 77:165-178
Nuclear factor-κB (NF-κB) binds to nucleotide sequences between -80 and -70 bp upstream of the transcriptional start site in the interleukin-8 (IL-8) promoter and is crucial for transcription of the IL-8 gene. We showed that exogenous nitric oxide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::afbfa18d019650297fc89dc533d7746d
https://doi.org/10.1139/o99-027
https://doi.org/10.1139/o99-027
Publikováno v:
Virology. 256:119-129
Site-directed mutagenesis of specific amino acids within a conserved amino-terminal region (H2) and a conserved carboxyl-terminal region (H10/A4) of the fusion protein G of vesicular stomatitis virus have previously identified these two segments as a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7812fd98a0f4d4aeca079561c54f1d21
https://doi.org/10.1006/viro.1999.9606
https://doi.org/10.1006/viro.1999.9606
Autor:
Hara P. Ghosh, Matthias J. Schnell, Robert Chernish, John K. Rose, Linda Buonocore, Eli Boritz
Publikováno v:
The EMBO Journal. 17:1289-1296
The cytoplasmic domains of viral glycoproteins are often involved in specific interactions with internal viral components. These interactions can concentrate glycoproteins at virus budding sites and drive efficient virus budding, or can determine vir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b74a1539dc27bb894a2362b2f55e5336
https://doi.org/10.1093/emboj/17.5.1289
https://doi.org/10.1093/emboj/17.5.1289
Publikováno v:
Journal of Virology. 71:7996-8000
Chimeric proteins in which the transmembrane anchoring sequence (TM) or both the TM and the cytoplasmic tail (CT) of vesicular stomatitis virus glycoprotein G were replaced with corresponding domains of viral or cellular integral membrane proteins we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65677a93f9ac6e7b80710c9cd6c17033
https://doi.org/10.1128/jvi.71.10.7996-8000.1997
https://doi.org/10.1128/jvi.71.10.7996-8000.1997
Publikováno v:
Journal of Virology. 68:2272-2285
We have used the glycoprotein gB of herpes simplex virus type 1 (gB-1), which buds from the inner nuclear membrane, as a model protein to study localization of membrane proteins in the nuclear envelope. To determine whether specific domains of gB-1 g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fb4d9698ad87152a03cd2a67f89f4ac
https://doi.org/10.1128/jvi.68.4.2272-2285.1994
https://doi.org/10.1128/jvi.68.4.2272-2285.1994