Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Changhyun Seong"'
Autor:
M. Catarina Silva, Suzanne Elsasser, Jessica Robert, Changhyun Seong, Monica Boselli, Randall W. King, Sang-Won Min, Timothy C. Gahman, Chialin Cheng, Stephen J. Haggarty, Li Gan, Ketki M. Hatle, Daniel Finley, Byung-Hoon Lee, Steven P. Gygi, Miguel A. Prado
Publikováno v:
The Journal of biological chemistry. 292(47)
The ubiquitin-proteasome system (UPS) is responsible for most selective protein degradation in eukaryotes and regulates numerous cellular processes, including cell cycle control and protein quality control. A component of this system, the deubiquitin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::573a162022325e86ded918bc99569689
https://pubmed.ncbi.nlm.nih.gov/28972160
https://pubmed.ncbi.nlm.nih.gov/28972160
Autor:
Eun Yong Shim, Amy Sid, Anna Malkova, Ji Hyun Oum, Sang Eun Lee, Youngho Kwon, Grzegorz Ira, Changhyun Seong, Jae-Hoon Ji, Sreejith Ramakrishnan, Patrick Sung
Publikováno v:
Molecular and Cellular Biology. 31:3924-3937
Homologous recombination repairs DNA double-strand breaks by searching for, invading, and copying information from a homologous template, typically the homologous chromosome or sister chromatid. Tight wrapping of DNA around histone octamers, however,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ac811b68505f16fbaca20255d7945b6
https://doi.org/10.1128/mcb.01269-10
https://doi.org/10.1128/mcb.01269-10
Autor:
Jennifer Blickwedehl, Raj K. Pandita, Manjula Agarwal, Patrick Sung, Thomas Melendy, Tej K. Pandita, Changhyun Seong, Naveen Bangia
Publikováno v:
Proceedings of the National Academy of Sciences. 105:16165-16170
Proteasome activator PA200 enhances proteasome-mediated cleavage after acidic residues in vitro ; however, its role within cells is not known. Here, we show that, in response to ionizing radiation, PA200 forms hybrid proteasomes with 19S caps and 20S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c5ba766e67d26245f80381ca18ab6b7
https://doi.org/10.1073/pnas.0803145105
https://doi.org/10.1073/pnas.0803145105
Autor:
Uffe Hasbro Mortensen, Changhyun Seong, Peter Chi, Patrick Sung, Lumir Krejci, Iben Plate, Idina Shi, Michael G. Sehorn, Binwei Song
Publikováno v:
Journal of Biological Chemistry. 283:12166-12174
A helical filament of Rad51 on single-strand DNA (ssDNA), called the presynaptic filament, catalyzes DNA joint formation during homologous recombination. Rad52 facilitates presynaptic filament assembly, and this recombination mediator activity is tho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b7a2f6c60af3153afd6612900ecb1df
https://doi.org/10.1074/jbc.m800763200
https://doi.org/10.1074/jbc.m800763200
Autor:
Rodney Rothstein, Michael Lisby, Uffe Hasbro Mortensen, Swee Chuang Lim Hallwyl, Iben Plate, Line Albertsen, Qi Feng, Changhyun Seong, Patrick Sung
Publikováno v:
DNA Repair. 7:57-66
Rad52 is essential for all homologous recombination and DNA double strand break repair events in Saccharomyces cerevisiae. This protein is multifunctional and contains several domains that allow it to interact with DNA as well as with different repai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02fbfb1a156b69bd05e9fa07950c3a93
https://doi.org/10.1016/j.dnarep.2007.07.016
https://doi.org/10.1016/j.dnarep.2007.07.016
Publikováno v:
Cell Death & Differentiation. 14:2068-2075
Cellular ionic homeostasis, fundamentally K(+) homeostasis, has been implicated as a critical regulator of apoptosis. The intracellular K(+) efflux on apoptotic insult and suppression of apoptosis by high concentration of extracellular K(+) or after
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6754c0ad76d34f055b869c1924eb5760
https://doi.org/10.1038/sj.cdd.4402221
https://doi.org/10.1038/sj.cdd.4402221
Autor:
Song Yub Shin, Changhyun Seong, Yun-Hee Lee, Byung Yun Cho, Jung Sup Lee, Bo-Eun Kim, Il-Seon Park
Publikováno v:
Biotechnology Letters. 27:1935-1942
For nucleosomal DNA fragmentation, one of the hallmarks of apoptosis, activated caspase, an apoptosis specific cysteine protease, is required to cleave ICAD/DFF45 that releases its complexed DNase, CAD/DFF40. The protein complex is located predominan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb404c9ca1aceb0ce7942fe44dfb1729
https://doi.org/10.1007/s10529-005-3906-z
https://doi.org/10.1007/s10529-005-3906-z
Homologous recombination represents an important means for the error-free elimination of DNA double-strand breaks and other deleterious DNA lesions from chromosomes. The Rad51 recombinase, a member of the RAD52 group of recombination proteins, cataly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d0fc28c884ce001138ef6306f01bd2f
https://europepmc.org/articles/PMC3320962/
https://europepmc.org/articles/PMC3320962/
Autor:
Zhu Zhu, Changhyun Seong, Lucy Lu, Patrick Sung, Peter Chi, Woo Hyun Chung, Hengyao Niu, Grzegorz Ira, Weixing Zhao, Dongqing Liu, Youngho Kwon, Rohit Prakash
Publikováno v:
Nature. 467(7311)
If not properly processed and repaired, DNA double-strand breaks (DSBs) can give rise to deleterious chromosome rearrangements, which could ultimately lead to the tumor phenotype1,2. DSB ends are resected in a 5′ to 3′ fashion in cells, to yield
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f2e077f90c077e46f8ec56daaf015db
https://pubmed.ncbi.nlm.nih.gov/20811460
https://pubmed.ncbi.nlm.nih.gov/20811460
Autor:
Patrick Sung, Rodney Rothstein, Changhyun Seong, Swee Chuang Lim Hallwyl, Uffe Hasbro Mortensen, Idina Shi
Publikováno v:
The Journal of biological chemistry. 284(48)
Saccharomyces cerevisiae Rad52 protein promotes homologous recombination by nucleating the Rad51 recombinase onto replication protein A-coated single-stranded DNA strands and also by directly annealing such strands. We show that the purified rad52-R7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6647c6ba6a6eaa30cccbc4a2ac41172
https://pubmed.ncbi.nlm.nih.gov/19812039
https://pubmed.ncbi.nlm.nih.gov/19812039