Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Daniel E. Eyler"'
Autor:
Jeremy Monroe, Daniel E. Eyler, Lili Mitchell, Indrajit Deb, Abigail Bojanowski, Pooja Srinivas, Christine M. Dunham, Bijoyita Roy, Aaron T. Frank, Kristin S. Koutmou
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-11 (2024)
Abstract The ribosome utilizes hydrogen bonding between mRNA codons and aminoacyl-tRNAs to ensure rapid and accurate protein production. Chemical modification of mRNA nucleobases can adjust the strength and pattern of this hydrogen bonding to alter p
Externí odkaz:
https://doaj.org/article/50975c01401849b98fd36770145e907c
Autor:
Anne Preis, Andre Heuer, Clara Barrio-Garcia, Andreas Hauser, Daniel E. Eyler, Otto Berninghausen, Rachel Green, Thomas Becker, Roland Beckmann
Publikováno v:
Cell Reports, Vol 8, Iss 1, Pp 59-65 (2014)
Termination and ribosome recycling are essential processes in translation. In eukaryotes, a stop codon in the ribosomal A site is decoded by a ternary complex consisting of release factors eRF1 and guanosine triphosphate (GTP)-bound eRF3. After GTP h
Externí odkaz:
https://doaj.org/article/15fd0e18d40f49a0a9b67c4687f05f60
Publikováno v:
Nature biotechnology.
Publikováno v:
PLoS ONE, Vol 12, Iss 3, p e0174041 (2017)
Human alkyladenine DNA glycosylase (AAG) initiates base excision repair (BER) to guard against mutations by excising alkylated and deaminated purines. Counterintuitively, increased expression of AAG has been implicated in increased rates of spontaneo
Externí odkaz:
https://doaj.org/article/f2a0a7a56bae4f4bb9f2813fe3e5be79
Autor:
Meredith K. Purchal, Daniel E. Eyler, Mehmet Tardu, Monika K. Franco, Megan M. Korn, Taslima Khan, Ryan McNassor, Rachel Giles, Katherine Lev, Hari Sharma, Jeremy Monroe, Leena Mallik, Markos Koutmos, Kristin S. Koutmou
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Pseudouridine is among the most-abundant RNA modifications. We present a framework for conceptualizing how eukaryotic pseudouridine synthases select their substrates. This work reveals the structure of yeast pseudouridine synthase 7 (Pus
Autor:
Kristin S. Koutmou, Yury S. Polikanov, Daniel E. Eyler, Malgorzata Dobosz-Bartoszek, Bijoyita Roy, Monika K Franco, Joshua D. Jones, Zahra Batool, Monica Z. Wu, Michelle L. Dubuke
Publikováno v:
Proc Natl Acad Sci U S A
Chemical modifications of RNAs have long been established as key modulators of nonprotein-coding RNA structure and function in cells. There is a growing appreciation that messenger RNA (mRNA) sequences responsible for directing protein synthesis can
Publikováno v:
The Journal of Biological Chemistry
Background: eRF3 is an essential, conserved gene, whose essential function has remained obscure. Results: eRF3 increases multiple turnover peptide release rates beyond the level expected from its stimulation of single turnover krel. Conclusion: eRF3
Autor:
Daniel E. Eyler, Jianhua Ju, Jun O. Liu, Ben Shen, Shridhar Bhat, Tilman Schneider-Poetsch, William C. Merrick, Yongjun Dang, Rachel Green
Publikováno v:
Nature chemical biology
Although the protein synthesis inhibitor cycloheximide (CHX) has been known for decades, its precise mechanism of action remains incompletely understood. The glutarimide portion of CHX is seen in a family of structurally related natural products incl
Publikováno v:
Nature
Various factors associate with the ribosome to assist in initiation, elongation and termination. Textbook accounts of protein synthesis describe just two universally conserved translation elongation factors — EF-Tu/eEF1A and EF-G/eEF2. Now a study
Autor:
Daniel E. Eyler, Tilman Schneider-Poetsch, John C. Jewett, Viresh H. Rawal, Rachel Green, Yongjun Dang, Shridhar Bhat, Jun O. Liu
Mycalamide B (MycB) is a marine sponge-derived natural product with potent antitumor activity. Although it has been shown to inhibit protein synthesis, the molecular mechanism of action by MycB remains incompletely understood. We verified the inhibit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaa30791abd62b97b21d57890d6f690b
https://europepmc.org/articles/PMC3153980/
https://europepmc.org/articles/PMC3153980/