Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Rya Ero"'
Autor:
Kwok Jian Goh, Rya Ero, Xin-Fu Yan, Jung-Eun Park, Binu Kundukad, Jun Zheng, Siu Kwan Sze, Yong-Gui Gao
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
BPI-inducible protein A (BipA), a highly conserved paralog of the well-known translational GTPases LepA and EF-G, has been implicated in bacterial motility, cold shock, stress response, biofilm formation, and virulence. BipA binds to the aminoacyl-(A
Externí odkaz:
https://doaj.org/article/5a358b61be5a466ea3eb924fd513d6b7
Publikováno v:
PLoS ONE, Vol 16, Iss 10, p e0258112 (2021)
Calmodulin, a ubiquitous eukaryotic calcium sensor responsible for the regulation of many fundamental cellular processes, is a highly flexible protein and exhibits an unusually wide range of conformations. Furthermore, CaM is known to interact with m
Externí odkaz:
https://doaj.org/article/d65587789a5045ccaa66e990323555dd
Autor:
Wenting Bu, Zarina Levitskaya, Zhi Yang Loh, Shengyang Jin, Shibom Basu, Rya Ero, Xinfu Yan, Meitian Wang, So Fong Cam Ngan, Siu Kwan Sze, Suet-Mien Tan, Yong-Gui Gao
Publikováno v:
PLoS Biology, Vol 18, Iss 7, p e3000755 (2020)
Kindlin-1, -2, and -3 directly bind integrin β cytoplasmic tails to regulate integrin activation and signaling. Despite their functional significance and links to several diseases, structural information on full-length kindlin proteins remains unkno
Externí odkaz:
https://doaj.org/article/4024b3da40da42c589700732075dd20e
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 10, p 5356 (2021)
Bacteria have evolved an array of mechanisms enabling them to resist the inhibitory effect of antibiotics, a significant proportion of which target the ribosome. Indeed, resistance mechanisms have been identified for nearly every antibiotic that is c
Externí odkaz:
https://doaj.org/article/3464d5702bcb4e3ba1d6e9ff76d13b68
Autor:
Josefine Liljeruhm, Margus Leppik, Letian Bao, Triin Truu, Maria Calvo-Noriega, Nicola S. Freyer, Aivar Liiv, Jinfan Wang, Rubén Crespo Blanco, Rya Ero, Jaanus Remme, Anthony C. Forster
Publikováno v:
RNA. 28:796-807
Escherichia coli rRNAs are post-transcriptionally modified at 36 positions but their modification enzymes are dispensable individually for growth, bringing into question their significance. However, a major growth defect was reported for deletion of
Autor:
Josefine, Liljeruhm, Margus, Leppik, Letian, Bao, Triin, Truu, Maria, Calvo-Noriega, Nicola S, Freyer, Aivar, Liiv, Jinfan, Wang, Rubén Crespo, Blanco, Rya, Ero, Jaanus, Remme, Anthony C, Forster
Publikováno v:
RNA (New York, N.Y.). 28(6)
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 5356, p 5356 (2021)
International Journal of Molecular Sciences
International Journal of Molecular Sciences
Bacteria have evolved an array of mechanisms enabling them to resist the inhibitory effect of antibiotics, a significant proportion of which target the ribosome. Indeed, resistance mechanisms have been identified for nearly every antibiotic that is c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1feedf77c7bb77425e4e8d10f61b53ce
https://hdl.handle.net/10356/152092
https://hdl.handle.net/10356/152092
Autor:
Zarina Levitskaya, Zhi Yang Loh, Suet-Mien Tan, Wenting Bu, Xin-Fu Yan, So Fong Cam Ngan, Rya Ero, Yong-Gui Gao, Shibom Basu, Siu Kwan Sze, Meitian Wang, Shengyang Jin
Publikováno v:
PLoS Biology
PLoS Biology, Vol 18, Iss 7, p e3000755 (2020)
PLoS Biology, Vol 18, Iss 7, p e3000755 (2020)
Kindlin-1, -2, and -3 directly bind integrin β cytoplasmic tails to regulate integrin activation and signaling. Despite their functional significance and links to several diseases, structural information on full-length kindlin proteins remains unkno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99363f365faed26ca1ad5ae6d121d151
https://hdl.handle.net/10356/146721
https://hdl.handle.net/10356/146721
Publikováno v:
RNA Biology
EF-G, EF4, and BipA are members of the translation factor family of GTPases with a common ribosome binding mode and GTPase activation mechanism. However, topological variations of shared as well as unique domains ensure different roles played by thes
Members of the ATP-binding cassette F (ABC-F) proteins confer resistance to several classes of clinically important antibiotics through ribosome protection. Recent structures of two ABC-F proteins, Pseudomonas aeruginosa MsrE and Bacillus subtilis Vm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21f8b166520dc45d7945b19cf00fda7b
https://hdl.handle.net/10356/104616
https://hdl.handle.net/10356/104616