Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Tolga Cagatay"'
Autor:
Prasanna Bhat, Vasilisa Aksenova, Matthew Gazzara, Emily A. Rex, Sadaf Aslam, Christina Haddad, Shengyan Gao, Matthew Esparza, Tolga Cagatay, Kimberly Batten, Sara S. El Zahed, Alexei Arnaoutov, Hualin Zhong, Jerry W. Shay, Blanton S. Tolbert, Mary Dasso, Kristen W. Lynch, Adolfo García-Sastre, Beatriz M. A. Fontoura
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
Abstract Nuclear export of influenza A virus (IAV) mRNAs occurs through the nuclear pore complex (NPC). Using the Auxin-Induced Degron (AID) system to rapidly degrade proteins, we show that among the nucleoporins localized at the nucleoplasmic side o
Externí odkaz:
https://doaj.org/article/ef526c85c77e4e78867cbdc75323343a
Autor:
Abhilash Padavannil, Prithwijit Sarkar, Seung Joong Kim, Tolga Cagatay, Jenny Jiou, Chad A Brautigam, Diana R Tomchick, Andrej Sali, Sheena D'Arcy, Yuh Min Chook
Publikováno v:
eLife, Vol 8 (2019)
We report the crystal structure of nuclear import receptor Importin-9 bound to its cargo, the histones H2A-H2B. Importin-9 wraps around the core, globular region of H2A-H2B to form an extensive interface. The nature of this interface coupled with qua
Externí odkaz:
https://doaj.org/article/ae5e9b8718834362977feb5ecb5f7a66
Autor:
Jianhui Guo, Tolga Cagatay, Guangjin Zhou, Chih-Chiang Chan, Shelby Blythe, Kaye Suyama, Li Zheng, Kaifeng Pan, Chiping Qian, Richard Hamelin, Stephen N Thibodeau, Peter S Klein, Keith A Wharton, Wanguo Liu
Publikováno v:
PLoS ONE, Vol 4, Iss 11, p e7982 (2009)
BACKGROUND:Mutation of Wnt signal antagonists Apc or Axin activates beta-catenin signaling in many cancers including the majority of human colorectal adenocarcinomas. The phenotype of apc or axin mutation in the fruit fly Drosophila melanogaster is s
Externí odkaz:
https://doaj.org/article/8d558a3f738942fa89bc2c7afe0fa3c4
Autor:
Shengyan Gao, Matthew Esparza, Ishmael Dehghan, Vasilisa Aksenova, Ke Zhang, Kimberly Batten, Max B. Ferretti, Bridget E. Begg, Tolga Cagatay, Jerry W. Shay, Adolfo García-Sastre, Elizabeth J. Goldsmith, Zhijian J. Chen, Mary Dasso, Kristen W. Lynch, Melanie H. Cobb, Beatriz M. A. Fontoura
Publikováno v:
Proceedings of the National Academy of Sciences. 119
Nuclear speckles are non–membrane-bound organelles known as storage sites for messenger RNA (mRNA) processing and splicing factors. More recently, nuclear speckles have also been implicated in splicing and export of a subset of mRNAs, including the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa8dba4e8991398c40ada3d78f6a36d3
https://doi.org/10.1073/pnas.2206046119
https://doi.org/10.1073/pnas.2206046119
Autor:
Hiroyoshi Matsumura, Tolga Cagatay, Taro Mannen, Yuh Min Chook, Chad A. Brautigam, Abner Gonzalez, Ashley Niesman, Takuya Yoshizawa, Ayano Fujiwara
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Mutations in the RNA-binding protein FUS cause familial amyotropic lateral sclerosis (ALS). Several mutations that affect the proline-tyrosine nuclear localization signal (PY-NLS) of FUS cause severe juvenile ALS. FUS also undergoes liquid–liquid p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3f5ab30c5ae6ce343c56c343ea68904
https://doi.org/10.1038/s41598-021-83196-y
https://doi.org/10.1038/s41598-021-83196-y
Publikováno v:
Molecular Biology of the Cell
CRM1 (Exportin1/XPO1) exports hundreds of broadly functioning protein cargoes out of the cell nucleus by binding to their classical nuclear export signals (NESs). The 8- to 15-amino-acid-long NESs contain four to five hydrophobic residues and are hig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af7ca8cdbf23b3d9b41b336b450a0ae0
https://doi.org/10.1091/mbc.e18-02-0096
https://doi.org/10.1091/mbc.e18-02-0096
Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization
Autor:
Ying C. Li, Ho Yee Joyce Fung, Philip Thomas, Emile S. Pinarbasi, Tolga Cagatay, Yuh Min Chook
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-16 (2018)
Scientific Reports
Scientific Reports
ALS (Amyotrophic Lateral Sclerosis) is a neurodegenerative disease characterized by the redistribution of the RNA binding protein TDP-43 in affected neurons: from predominantly nuclear to aggregated in the cytosol. However, the determinants of TDP-43
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9efdbc95f21534dd2ec386862431db6d
https://doaj.org/article/e0bc0cffa6c242cf85832575acd6acd8
https://doaj.org/article/e0bc0cffa6c242cf85832575acd6acd8
Autor:
Tolga Cagatay, Yuh Min Chook, Jenny Jiou, Sheena D'Arcy, Prithwijit Sarkar, Andrej Sali, Chad A. Brautigam, Diana R. Tomchick, Abhilash Padavannil, Seung Joong Kim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::434408b98179a161ae8026518a9c1ee3
https://doi.org/10.7554/elife.43630.030
https://doi.org/10.7554/elife.43630.030
Autor:
Sheena D'Arcy, Seung Joong Kim, Tolga Cagatay, Yuh Min Chook, Diana R. Tomchick, Chad A. Brautigam, Andrej Sali, Abhilash Padavannil, Prithwijit Sarkar, Jenny Jiou
Publikováno v:
eLife, Vol 8 (2019)
eLife
eLife
We report the crystal structure of nuclear import receptor Importin-9 bound to its cargo, the histones H2A-H2B. Importin-9 wraps around the core, globular region of H2A-H2B to form an extensive interface. The nature of this interface coupled with qua
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82203da5b7393d0793fc6e61ea10c7dc
https://escholarship.org/uc/item/0jf662t1
https://escholarship.org/uc/item/0jf662t1
Publikováno v:
Journal of Biological Chemistry. 291:21171-21183
N-terminal tails of histones H3 and H4 are known to bind several different Importins to import the histones into the cell nucleus. However, it is not known what binding elements in the histone tails are recognized by the individual Importins. Biochem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7a0dbe992789ef45fd50baa8223400e
https://doi.org/10.1074/jbc.m116.730218
https://doi.org/10.1074/jbc.m116.730218