Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Maria K Mateyak"'
Autor:
Maria K Mateyak, Justyna K Pupek, Alexandra E Garino, McCllelan C Knapp, Sarah F Colmer, Terri Goss Kinzy, Stephen Dunaway
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0190524 (2018)
In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-depe
Externí odkaz:
https://doaj.org/article/42ac79ade2dd45988516e906fcbd528e
Publikováno v:
FEBS Letters. 595:2208-2220
Previous studies have suggested that phosphorylation of translation elongation factor 1A (eEF1A) can alter its function, and large-scale phospho-proteomic analyses in Saccharomyces cerevisiae have identified 14 eEF1A residues phosphorylated under var
Autor:
Maria K. Mateyak, Yixuan Wu, Huijuan Cui, Xinfu Jiao, Ronald P. Hart, Megerditch Kiledjian, Liang Tong, Ewa Grudzien-Nogalska
Publikováno v:
Nature chemical biology
We recently demonstrated that mammalian cells harbor nicotinamide adenine dinucleotide (NAD)-capped messenger RNAs that are hydrolyzed by the DXO deNADding enzyme. Here, we report that the Nudix protein Nudt12 is a second mammalian deNADding enzyme s
Autor:
Sarah F. Colmer, Stephen Dunaway, Terri Goss Kinzy, Maria K. Mateyak, Alexandra E. Garino, Justyna K. Pupek, McCllelan C. Knapp
Publikováno v:
PLoS ONE, Vol 13, Iss 1, p e0190524 (2018)
PLoS ONE
PLoS ONE
In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-depe
Autor:
Maria K. Mateyak, Terri Goss Kinzy
Publikováno v:
Journal of Biological Chemistry. 288:24647-24655
Eukaryotic translation elongation factor 2 (eEF2) facilitates the movement of the peptidyl tRNA-mRNA complex from the A site of the ribosome to the P site during protein synthesis. ADP-ribosylation (ADPR) of eEF2 by bacterial toxins on a unique dipht
Publikováno v:
Evolution of the Protein Synthesis Machinery and Its Regulation ISBN: 9783319394671
Translation, the mechanism by which proteins are synthesized based on the information encoded in mRNA, is an essential process in all living organisms. Consisting of initiation, elongation and termination phases, many aspects of this process are cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd03a2f7c93489953020944300963853
https://doi.org/10.1007/978-3-319-39468-8_14
https://doi.org/10.1007/978-3-319-39468-8_14
Autor:
Terri Goss Kinzy, Maria K. Mateyak
Publikováno v:
Trends in Biochemical Sciences. 42:587-588
Protein synthesis requires factors that are proposed to enhance discrete steps. Eukaryotic initiation factor eIF5A was initially thought to affect initiation; however, it was later shown to facilitate translation elongation at polyproline. Recent wor
Autor:
Terri Goss Kinzy, Maria K. Mateyak
Publikováno v:
Journal of Biological Chemistry. 285:21209-21213
Eukaryotic translation elongation factor 1A (eEF1A) is one of the most abundant protein synthesis factors. eEF1A is responsible for the delivery of all aminoacyl-tRNAs to the ribosome, aside from initiator and selenocysteine tRNAs. In addition to its
Autor:
Caterina Iorio, Bryan E. Snow, Lea Harrington, Virginia A. Zakian, Jana Paderova, Maria K. Mateyak, Jeremy A. Squire, Andrew Wakeham
Publikováno v:
Molecular and Cellular Biology. 27:1017-1026
Pif1 is a 5'-to-3' DNA helicase critical to DNA replication and telomere length maintenance in the budding yeast Saccharomyces cerevisiae. ScPif1 is a negative regulator of telomeric repeat synthesis by telomerase, and recombinant ScPif1 promotes the
Autor:
Maria K. Mateyak, Virginia A. Zakian
Publikováno v:
Cell Cycle. 5:2796-2804
The evolutionarily conserved PIF1 DNA helicase family is important for the maintenance of genome stability in the yeast, Saccharomyces cerevisiae. There are two PIF1 family helicases in S. cerevisiae, Pif1p and Rrm3p that both possess 5'-->3' DNA hel