Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Anthony P Schuller"'
Autor:
Kristin S Koutmou, Anthony P Schuller, Julie L Brunelle, Aditya Radhakrishnan, Sergej Djuranovic, Rachel Green
Publikováno v:
eLife, Vol 4 (2015)
Protein output from synonymous codons is thought to be equivalent if appropriate tRNAs are sufficiently abundant. Here we show that mRNAs encoding iterated lysine codons, AAA or AAG, differentially impact protein synthesis: insertion of iterated AAA
Externí odkaz:
https://doaj.org/article/72f2c8d9511d4ac699f475ae925f7955
Autor:
Karsten Weis, Mary Dasso, Saroj G. Regmi, Matthias Wojtynek, Meltem Tatli, Edward J. Brignole, Thomas U. Schwartz, Phat Vinh Dip, Rafael Kronenberg-Tenga, Anthony P. Schuller, Ohad Medalia, David Mankus, Abigail K. R. Lytton-Jean
Publikováno v:
Nature
Nature, 598
Nature, 598
Nuclear pore complexes (NPCs) create large conduits for cargo transport between the nucleus and cytoplasm across the nuclear envelope (NE)1,2,3. These multi-megadalton structures are composed of about thirty different nucleoporins that are distribute
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4b0ae2da9b3ce28d28b42ac700236b0
Autor:
Rachel Green, Anthony P Schuller
Publikováno v:
Nature Reviews Molecular Cell Biology. 19:526-541
During protein synthesis, ribosomes encounter many roadblocks, the outcomes of which are largely determined by substrate availability, amino acid features, and reaction kinetics. Prolonged ribosome stalling is likely to be resolved by ribosome rescue
Publikováno v:
Nucleic Acids Research
Upf1 is an SF1-family RNA helicase that is essential for the nonsense-mediated decay (NMD) process in eukaryotes. While Upf1 has been shown to interact with 80S ribosomes, the molecular details of this interaction were unknown. Using purified recombi
Autor:
Anthony P Schuller, Rachel Green
Publikováno v:
Molecular Cell. 66:578-580
In a recent issue of Nature Structural & Molecular Biology, Heuer et al. (2017) present a 3.9-A cryo-EM structure of the 40S:ABCE1 post-splitting complex. This structure provides new insights into a dual role for ABCE1 in translation recycling and re
Autor:
Jun O. Liu, Safiat Ayinde, Rachel Green, Marat Yusupov, Brandon McClary, Junyan Lu, Mélanie Meyer, Daniel Romo, Anthony P Schuller, Boris Zinshteyn, Cheng Luo, Zufeng Guo, Gulnara Yusupova, Jeremy Chris P. Reyes, Morgan Jouanneau, Simone Pellegrino, Yongjun Dang
Publikováno v:
Cell Chemical Biology
Cell Chemical Biology, 2017, 24 (5), pp.605-613.e5. ⟨10.1016/j.chembiol.2017.04.006⟩
Cell Chemical Biology, 2017, 24 (5), pp.605-613.e5. ⟨10.1016/j.chembiol.2017.04.006⟩
International audience; Protein synthesis plays an essential role in cell proliferation, differentiation, and survival. Inhibitors of eukaryotic translation have entered the clinic, establishing the translation machinery as a promising target for che
Publikováno v:
Current Opinion in Structural Biology. 21:92-100
Telomeres and their associated proteins are specialized structures at the ends of linear chromosomes that function as caps that protect the DNA from exonuclease degradation and recombination events that could lead to genomic instability. In this revi
Publikováno v:
Nature. 455:633-637
A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, a
Autor:
Sergej Djuranovic, Aditya Radhakrishnan, Rachel Green, Julie L. Brunelle, Kristin S. Koutmou, Anthony P Schuller
Publikováno v:
eLife, Vol 4 (2015)
eLife
eLife
Protein output from synonymous codons is thought to be equivalent if appropriate tRNAs are sufficiently abundant. Here we show that mRNAs encoding iterated lysine codons, AAA or AAG, differentially impact protein synthesis: insertion of iterated AAA