NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific [3-15N]uridine substitutions.

It has been reported that a 183 residue fragment, consisting of the two RNA-binding domains (RBD1- RBD2) of the Drosophila melanogster Sex-lethal (Sxl) protein, strongly binds an oligonucleotide of the target RNA sequence (5'-GUUUUUUUUC-3') that regulates alternative splicing, and forms four or five...

Whakaahuatanga katoa

I tiakina i:

Ngā taipitopito rārangi puna kōrero
I whakaputaina i:	Nucleic Acids Res
Ngā kaituhi matua:	Kim, I, Muto, Y, Inoue, M, Watanabe, S, Kitamura, A, Yokoyama, S, Hosono, K, Takaku, H, Ono, A, Kainosho, M, Sakamoto, H, Shimura, Y
Hōputu:	Artigo
Reo:	Inglês
I whakaputaina:	Oxford University Press 1997
Ngā marau:	Research Article
Urunga tuihono:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC146625/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9092663/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/25.8.1565
Ngā Tūtohu:	Tāpirihia he Tūtohu Kāore He Tūtohu, Me noho koe te mea tuatahi ki te tūtohu i tēnei pūkete!

NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific [3-15N]uridine substitutions.

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