Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Jane E, Jackman"'
Autor:
Elwood A. Mullins, Lauren E. Salay, Clarissa L. Durie, Jane E. Jackman, Melanie D. Ohi, Walter J. Chazin, Brandt F. Eichman
Publikováno v:
bioRxiv
The mechanism by which polymerase α–primase (polα–primase) synthesizes chimeric RNA-DNA primers of defined length and composition, necessary for replication fidelity and genome stability, is unknown. Here, we report cryo-EM structures of polα
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db20f3ea7498c2840f069236454f8cd1
https://europepmc.org/articles/PMC10055150/
https://europepmc.org/articles/PMC10055150/
Autor:
Sarah E. Strassler, Isobel E. Bowles, Aiswarya Krishnamohan, Hyejeong Kim, Emily G. Kuiper, Lindsay R. Comstock, Jane E. Jackman, Graeme L. Conn
Publikováno v:
bioRxiv
The methyltransferase Trm10 modifies a subset of tRNAs on the base N1 position of the 9th nucleotide in the tRNA core. Trm10 is conserved throughout Eukarya and Archaea, and mutations in the human gene (TRMT10A) have been linked to neurological disor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f77869d49271800f1881f022c07e6fa6
https://europepmc.org/articles/PMC9915607/
https://europepmc.org/articles/PMC9915607/
Publikováno v:
RNA. 27:683-693
The tRNAHis guanylyltransferase (Thg1) was originally discovered in Saccharomyces cerevisiae where it catalyzes 3′–5′ addition of a single nontemplated guanosine (G−1) to the 5′ end of tRNAHis. In addition to this activity, S. cerevisiae Th
Publikováno v:
Journal of Biological Chemistry. 298:102393
The SpoU-TrmD (SPOUT) methyltransferase superfamily was designated when structural similarity was identified between the transfer RNA-modifying enzymes TrmH (SpoU) and TrmD. SPOUT methyltransferases are found in all domains of life and predominantly
Autor:
Jane E. Jackman
Publikováno v:
Methods in enzymology. 658
Autor:
Nathan W. Howell, Jane E. Jackman
Publikováno v:
eLS. :1-11
Publikováno v:
FEBS Lett
tRNA(His) guanylyltransferase (Thg1) specifies eukaryotic tRNA(His) identity by catalyzing a 3’ to 5’ non-Watson Crick (WC) addition of guanosine to the 5’-end of tRNA(His). Thg1 family enzymes in Archaea and Bacteria, called Thg1-like-proteins
Publikováno v:
Methods in Enzymology ISBN: 9780128235850
The application of in vitro kinetic tools has the potential to provide important insight into the molecular mechanisms of RNA modification enzymes. Utilizing quantitative biochemical approaches can reveal information about enzyme preferences for spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c21fb35a72b3153aa86c43f04dd609fa
https://doi.org/10.1016/bs.mie.2021.07.002
https://doi.org/10.1016/bs.mie.2021.07.002
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e67465 (2013)
All nucleotide polymerases and transferases catalyze nucleotide addition in a 5' to 3' direction. In contrast, tRNA(His) guanylyltransferase (Thg1) enzymes catalyze the unusual reverse addition (3' to 5') of nucleotides to polynucleotide substrates.
Externí odkaz:
https://doaj.org/article/034bc83bcdae4e00bb676cd314863cfc
Autor:
Hannah K. Choe, Parvathi Ranganathan, Jane E. Jackman, Lotus Neidemire-Colley, Gregory K. Behbehani, Charuta Kale, Raymond D. Devine, Kris Vaddi, Min Wang, Yandi Gao, Yang Zhang, Hong Lin, Natalie E. Sell, Anora Ignaci, Robert A. Baiocchi, Maciej Pietrzak, Katiri Snyder, Nina C. Zitzer, Ramiro Garzon, Maria G. Abad
Publikováno v:
JCI Insight
Acute graft-versus-host disease (aGVHD) is a T cell–mediated immunological disorder and the leading cause of nonrelapse mortality in patients who receive allogeneic hematopoietic cell transplants. Based on recent observations that protein arginine