Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Sachiko Homma"'
Publikováno v:
BMC Research Notes, Vol 15, Iss 1, Pp 1-6 (2022)
Abstract Objective Aberrant expression in skeletal muscle of DUX4, a double homeobox transcription factor, underlies pathogenesis in facioscapulohumeral muscular dystrophy (FSHD). Although previous studies of FSHD muscle biopsies detected mRNAs encod
Externí odkaz:
https://doaj.org/article/239049193c71461b8c3ef4486e2f506e
Autor:
Isabel F. Masteika, Anvitha Sathya, Sachiko Homma, Bess M. Miller, Frederick M. Boyce, Jeffrey Boone Miller
Publikováno v:
Biology Open, Vol 11, Iss 2, Pp 1-12 (2022)
Abnormal expression in skeletal muscle of the double homeobox transcription factor DUX4 underlies pathogenesis in facioscapulohumeral muscular dystrophy (FSHD). Though multiple changes are known to be initiated by aberrant DUX4 expression, the downst
Externí odkaz:
https://doaj.org/article/f7fbab5ef8bf4bfab4d6bff8c99ab42d
Publikováno v:
Skeletal Muscle, Vol 6, Iss 1, Pp 1-16 (2016)
Abstract Background Nuclear bodies, such as nucleoli, PML bodies, and SC35 speckles, are dynamic sub-nuclear structures that regulate multiple genetic and epigenetic processes. Additional regulation is provided by RNA/DNA handling proteins, notably T
Externí odkaz:
https://doaj.org/article/c68b38002713427695fc4250f8d9c754
Autor:
Hiroaki Mitsuhashi, Satoshi Ishimaru, Sachiko Homma, Bryant Yu, Yuki Honma, Mary Lou Beermann, Jeffrey Boone Miller
Publikováno v:
Biology Open, Vol 7, Iss 4 (2018)
Aberrant expression of the full-length isoform of DUX4 (DUX4-FL) appears to underlie pathogenesis in facioscapulohumeral muscular dystrophy (FSHD). DUX4-FL is a transcription factor and ectopic expression of DUX4-FL is toxic to most cells. Previous s
Externí odkaz:
https://doaj.org/article/32978fad1fc14b22be538ef7551e5072
Autor:
Shinichi Takayama, John C. Reed, Samuel J. Dolezal, Akinori Hishiya, Sachiko Homma, Masahiro Iwasaki
Supplementary Figure 5 from BAG3 Regulates Motility and Adhesion of Epithelial Cancer Cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46357a96313538e4f1877e3947f9eace
https://doi.org/10.1158/0008-5472.22370016.v1
https://doi.org/10.1158/0008-5472.22370016.v1
Autor:
Shinichi Takayama, John C. Reed, Samuel J. Dolezal, Akinori Hishiya, Sachiko Homma, Masahiro Iwasaki
Supplementary Figure 3 from BAG3 Regulates Motility and Adhesion of Epithelial Cancer Cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11ec31482080ef293b337f92e31b88f5
https://doi.org/10.1158/0008-5472.22370022.v1
https://doi.org/10.1158/0008-5472.22370022.v1
Autor:
Shinichi Takayama, John C. Reed, Samuel J. Dolezal, Akinori Hishiya, Sachiko Homma, Masahiro Iwasaki
Supplementary Figure 1 from BAG3 Regulates Motility and Adhesion of Epithelial Cancer Cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68c8449a077c2bd6d64dffa91641f7d6
https://doi.org/10.1158/0008-5472.22370028.v1
https://doi.org/10.1158/0008-5472.22370028.v1
Autor:
Shinichi Takayama, John C. Reed, Samuel J. Dolezal, Akinori Hishiya, Sachiko Homma, Masahiro Iwasaki
Supplementary Figure 2 from BAG3 Regulates Motility and Adhesion of Epithelial Cancer Cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1af728cd956d80aedd3ab4e3b36f3534
https://doi.org/10.1158/0008-5472.22370025
https://doi.org/10.1158/0008-5472.22370025
Autor:
Shinichi Takayama, John C. Reed, Samuel J. Dolezal, Akinori Hishiya, Sachiko Homma, Masahiro Iwasaki
Supplementary Figure 4 from BAG3 Regulates Motility and Adhesion of Epithelial Cancer Cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a24a985fed9755a82bad4859226fef5
https://doi.org/10.1158/0008-5472.22370019
https://doi.org/10.1158/0008-5472.22370019
Autor:
Shinichi Takayama, John C. Reed, Samuel J. Dolezal, Akinori Hishiya, Sachiko Homma, Masahiro Iwasaki
BAG3 protein binds to and regulates Hsp70 chaperone activity. The BAG3 protein contains a WW domain and a proline-rich region with SH3-binding motifs, suggesting that it may interact with proteins relevant to signal transduction, recruiting Hsp70 to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::161a2854e83919397ea3aef646e10ff5
https://doi.org/10.1158/0008-5472.c.6496236
https://doi.org/10.1158/0008-5472.c.6496236