Zobrazeno 1 - 10
of 273
pro vyhledávání: '"EIF1"'
Akademický článek
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Autor:
Thakur, Anil, Hinnebusch, Alan G.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2018 May 01. 115(18), E4159-E4168.
Externí odkaz:
https://www.jstor.org/stable/26508764
Autor:
Eiji Obayashi, Rafael E. Luna, Takashi Nagata, Pilar Martin-Marcos, Hiroyuki Hiraishi, Chingakham Ranjit Singh, Jan Peter Erzberger, Fan Zhang, Haribabu Arthanari, Jacob Morris, Riccardo Pellarin, Chelsea Moore, Ian Harmon, Evangelos Papadopoulos, Hisashi Yoshida, Mahmoud L. Nasr, Satoru Unzai, Brytteny Thompson, Eric Aube, Samantha Hustak, Florian Stengel, Eddie Dagraca, Asokan Ananbandam, Philip Gao, Takeshi Urano, Alan G. Hinnebusch, Gerhard Wagner, Katsura Asano
Publikováno v:
Cell Reports, Vol 18, Iss 11, Pp 2651-2663 (2017)
During eukaryotic translation initiation, eIF3 binds the solvent-accessible side of the 40S ribosome and recruits the gate-keeper protein eIF1 and eIF5 to the decoding center. This is largely mediated by the N-terminal domain (NTD) of eIF3c, which ca
Externí odkaz:
https://doaj.org/article/cb9ad045c97d4978ad675e2642cc8c65
Akademický článek
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Autor:
Ivanov, Ivaylo P, Saba, James A, Fan, Chen-Ming, Wang, Ji, Firth, Andrew E, Cao, Chune, Green, Rachel, Dever, Thomas E
Translation start site selection in eukaryotes is influenced by context nucleotides flanking the AUG codon and by levels of the eukaryotic translation initiation factors eIF1 and eIF5. In a search of mammalian genes, we identified five homeobox (Hox)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::169813723f6845c6f998664c2324f4c3
Autor:
Virginie Marchand, Yuri Motorin, R. Elizabeth Dreggors-Walker, Sohail Khoshnevis, Homa Ghalei
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 2022, 119 (12), pp.e2117334119. ⟨10.1073/pnas.2117334119⟩
Proceedings of the National Academy of Sciences of the United States of America, 2022, 119 (12), pp.e2117334119. ⟨10.1073/pnas.2117334119⟩
Protein synthesis by ribosomes is critically important for gene expression in all cells. The ribosomal RNAs (rRNAs) are marked by numerous chemical modifications. An abundant group of rRNA modifications, present in all domains of life, is 2’-O-meth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8eeba45839433a4c7459765cb2a642e8
https://doi.org/10.1073/pnas.2117334119
https://doi.org/10.1073/pnas.2117334119
Akademický článek
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Autor:
Alan G. Hinnebusch, Jinsheng Dong
Publikováno v:
Genetics
The eukaryotic 43S pre-initiation complex (PIC) containing Met-tRNAiMet in a ternary complex (TC) with eIF2-GTP scans the mRNA leader for an AUG codon in favorable “Kozak” context. AUG recognition triggers rearrangement of the PIC from an open co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33e2059d650ab1ce8b46419be2c42b19
https://pubmed.ncbi.nlm.nih.gov/34791232
https://pubmed.ncbi.nlm.nih.gov/34791232
Publikováno v:
Biochemical and biophysical research communications. 519(1):186-191
In the process of eukaryotic translation, the formation of preinitiation complex 43S, which consists of a 40S subunit, the eIF2-GTP-Met-tRNAi(Met) ternary complex, eIF3, eIF1, eIF1A, and eIF5, is essential for translational quality control. Of those
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe74ceacd1df7b1223895ada07faa9c4
http://hdl.handle.net/2115/76740
http://hdl.handle.net/2115/76740
Publikováno v:
Communications biology. 5(1)
During translational initiation in eukaryotes, the small ribosomal subunit forms a 48S preinitiation complex (PIC) with initiation factors. The 48S PIC binds to the 5’ end of mRNA and inspects long untranslated region (UTR) for the presence of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b59e2409611d1ec89c2b05baeb081996
https://pubmed.ncbi.nlm.nih.gov/35705698
https://pubmed.ncbi.nlm.nih.gov/35705698