Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Erik W. Debler"'
Autor:
Victoria S. Frisbie, Hideharu Hashimoto, Yixuan Xie, Francisca N. De Luna Vitorino, Josue Baeza, Tam Nguyen, Zhangerjiao Yuan, Janna Kiselar, Benjamin A. Garcia, Erik W. Debler
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract In higher eukaryotes, a single DOT1 histone H3 lysine 79 (H3K79) methyltransferase processively produces H3K79me2/me3 through histone H2B mono-ubiquitin interaction, while the kinetoplastid Trypanosoma brucei di-methyltransferase DOT1A and t
Externí odkaz:
https://doaj.org/article/dee92a5dbeef4bc7a7fcd20f4ce671b2
Autor:
Hideharu Hashimoto, Daniel H. Ramirez, Ophélie Lautier, Natalie Pawlak, Günter Blobel, Benoît Palancade, Erik W. Debler
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-11 (2022)
Abstract In Saccharomyces cerevisiae, the pre-mRNA leakage 39-kDa protein (ScPml39) was reported to retain unspliced pre-mRNA prior to export through nuclear pore complexes (NPCs). Pml39 homologs outside the Saccharomycetaceae family are currently un
Externí odkaz:
https://doaj.org/article/b429700f5b9c42caaae91e3fe99c311f
Autor:
Marina Farkas, Hideharu Hashimoto, Yingtao Bi, Ramana V. Davuluri, Lois Resnick-Silverman, James J. Manfredi, Erik W. Debler, Steven B. McMahon
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
The tumor suppressor p53 is a master regulator of cellular stress response pathways, including cell cycle arrest and apoptosis. Here, the authors identify molecular mechanisms of p53 binding to high- and low-affinity p53 response elements in the geno
Externí odkaz:
https://doaj.org/article/3f1e9178c9564dfeb7beebe3db18db73
Autor:
Lucie Kafková, Chengjian Tu, Kyle L. Pazzo, Kyle P. Smith, Erik W. Debler, Kimberly S. Paul, Jun Qu, Laurie K. Read
Publikováno v:
mBio, Vol 9, Iss 6 (2018)
ABSTRACT In Trypanosoma brucei and related kinetoplastid parasites, transcription of protein coding genes is largely unregulated. Rather, mRNA binding proteins, which impact processes such as transcript stability and translation efficiency, are the p
Externí odkaz:
https://doaj.org/article/647e168636894a55bb8debea108ceecc
Autor:
James M Gibson, Heying Cui, M Yusuf Ali, Xiaoxin Zhao, Erik W Debler, Jing Zhao, Kathleen M Trybus, Sozanne R Solmaz, Chunyu Wang
Publikováno v:
eLife, Vol 11 (2022)
Nup358, a protein of the nuclear pore complex, facilitates a nuclear positioning pathway that is essential for many biological processes, including neuromuscular and brain development. Nup358 interacts with the dynein adaptor Bicaudal D2 (BicD2), whi
Externí odkaz:
https://doaj.org/article/4a68972630e44150a18ff81e5f7a70b2
Autor:
Adi N.R. Poli, Rebecca C. Blyn, Gracyn Y. Buenconsejo, Erik Tang, Channy Danh, Joel Cassel, Erik W. Debler, Danae Schulz, Joseph M. Salvino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d41d1bcd168f6a78ae64771a7804b185
https://doi.org/10.2139/ssrn.4442047
https://doi.org/10.2139/ssrn.4442047
Autor:
M Yusuf Ali, Heying Cui, James M Gibson, Xiaoxin Zhao, Erik W Debler, Jing Zhao, Kathleen M Trybus, Sozanne R Solmaz, Chunyu Wang
Publikováno v:
eLife. 11
Nup358, a protein of the nuclear pore complex, facilitates a nuclear positioning pathway that is essential for many biological processes, including neuromuscular and brain development. Nup358 interacts with the dynein adaptor Bicaudal D2 (BicD2), whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c9ca744d7032af394e658c74ecbc371
https://doi.org/10.7554/elife.74714
https://doi.org/10.7554/elife.74714
Autor:
James M. Gibson, Heying Cui, M. Yusuf Ali, Xiaoxin Zhao, Tingyao Wang, David L. Moraga, Erik W. Debler, Jing Zhao, Kathleen M. Trybus, Sozanne R. Solmaz, Chunyu Wang
Publikováno v:
Biophysical Journal. 122:411a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4174a53ed65aade667884c5dc1f1fa17
https://doi.org/10.1016/j.bpj.2022.11.2233
https://doi.org/10.1016/j.bpj.2022.11.2233
Autor:
Heying Cui, Crystal R. Noell, Kaiqi Zhang, Puja Goyal, Erik W. Debler, Sozanne R. Solmaz, Jia Ying Loh, Kyle M. Loftus, Blaine B. Russ
Publikováno v:
J Phys Chem Lett
Dynein adaptors such as Bicaudal D2 (BicD2) recognize cargo for dynein-dependent transport, and cargo-bound adaptors are required to activate dynein for processive transport, but the mechanism of action is unknown. Here we report the X-ray structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c3ef6aaf2b2dc30781a13b282d7d353
https://doi.org/10.1021/acs.jpclett.9b01865
https://doi.org/10.1021/acs.jpclett.9b01865