Zobrazeno 1 - 10
of 23
pro vyhledávání: '"D E, Draper"'
Autor:
Xiaobing Zuo, Anton Barty, Lixin Fan, R.A. Tuckey, John C. H. Spence, Thomas A. White, Jiashan Zhang, Charles D. Schwieters, Jason R. Stagno, Kemin Tan, Nadia A. Zatsepin, Chufeng Li, Chelsie E. Conrad, D.R. Wendel, Subrata Panja, Mark S. Hunter, Sébastien Boutet, Dominik Oberthuer, Garrett Nelson, Jesse Coe, Xinhua Ji, D. E. Draper, Marzena A. Dyba, Sergey G. Tarasov, Juraj Knoska, Adrian R. Ferré-D'Amaré, Max O. Wiedorn, Petra Fromme, Sarah A. Woodson, Yun-Xing Wang, Henry N. Chapman, Yuba R. Bhandari, Uwe Weierstall, Yuan Liu, Ping Yu, Mengning Liang, Monalisa Swain, Thomas D. Grant
Publikováno v:
Nature 541, 242-246 (2017). doi:10.1038/nature20599
Nature / Physical science 541, 242-246(2016). doi:10.1038/nature20599
Riboswitches are structural RNA elements that are generally located in the 5′ untranslated region of messenger RNA. During regulation of gene expression, ligand binding to t
Riboswitches are structural RNA elements that are generally located in the 5′ untranslated region of messenger RNA. During regulation of gene expression, ligand binding to t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81d60895173000247b56f5b29cf22195
Autor:
G L, Conn, D E, Draper
Publikováno v:
Current Opinion in Structural Biology. 8:278-285
New information concerning RNA structure is accumulating at an ever increasing rate-from short helices with mismatched bases of 5S rRNA and complex RNA aptamers. The importance of recurring structural motifs, ion binding, and the kinetics and energet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::439612ebc07a42c64275507dcf4fb656
https://doi.org/10.1016/s0959-440x(98)80059-6
https://doi.org/10.1016/s0959-440x(98)80059-6
Publikováno v:
The Journal of biological chemistry. 276(42)
Ribosomal protein S4 represses synthesis of the four ribosomal proteins (including itself) in the Escherichia coli alpha operon by binding to a nested pseudoknot structure that spans the ribosome binding site. A model for the repression mechanism pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7275864484afdad515ec132b112a0d56
https://pubmed.ncbi.nlm.nih.gov/11504736
https://pubmed.ncbi.nlm.nih.gov/11504736
Autor:
R, Shiman, D E, Draper
Publikováno v:
Journal of molecular biology. 302(1)
The effects of monovalent cations (Li(+), Na(+), K(+), Rb(+), Cs(+), and NH4(+)) on the thermal stability of RNA tertiary structure were investigated by UV melting. We show that with the RNA used here (nucleotides 1051-1108 of Escherichia coli 23 S r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0244aec77f3c99c848e78fabefcd173e
https://pubmed.ncbi.nlm.nih.gov/10964562
https://pubmed.ncbi.nlm.nih.gov/10964562
Autor:
D, GuhaThakurta, D E, Draper
Publikováno v:
Journal of molecular biology. 295(3)
The C-terminal domain of ribosomal protein L11, L11-C76, binds in the distorted minor groove of a helix within a 58 nucleotide domain of 23 S rRNA. To study the electrostatic component of RNA recognition in this protein, arginine and lysine residues
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::37400a326e77a01c754a3568635146c5
https://pubmed.ncbi.nlm.nih.gov/10623547
https://pubmed.ncbi.nlm.nih.gov/10623547
Publikováno v:
Journal of molecular biology. 292(2)
Prokaryotic protein S4 initiates assembly of the small ribosomal subunit by binding to 16 S rRNA. Residues 43-200 of S4 from Bacillus stearothermophilus (S4 Delta41) bind to both 16 S rRNA and to a mRNA pseudoknot. In order to obtain structure-based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::432ff175646e0a40bcbb0a61cfdd81ea
https://pubmed.ncbi.nlm.nih.gov/10493882
https://pubmed.ncbi.nlm.nih.gov/10493882
Autor:
V K, Misra, D E, Draper
Publikováno v:
Biopolymers. 48(2-3)
Divalent cations, like magnesium, are crucial for the structural integrity and biological activity of RNA. In this article, we present a picture of how magnesium stabilizes a particular folded form of RNA. The overall stabilization of RNA by Mg2+ is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0dad1e997395cea7b9ea3eedd7b298c4
https://pubmed.ncbi.nlm.nih.gov/10333741
https://pubmed.ncbi.nlm.nih.gov/10333741
Publikováno v:
Biochemistry. 37(34)
Comparative sequence analysis reveals a coordinated set of nucleotide exchanges between the base pair 1092/1099 and the unpaired position 1072 [(1092/1099)1072] in the L11 binding domain of 23S ribosomal RNA. This set of exchanges has occurred at lea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2fe15303b2cbab4b70ea6abec1654be3
https://pubmed.ncbi.nlm.nih.gov/9718323
https://pubmed.ncbi.nlm.nih.gov/9718323
Publikováno v:
RNA (New York, N.Y.). 3(8)
Although eukaryotes are not generally sensitive to thiostrepton, growth of the human malaria parasite Plasmodium falciparum is severely inhibited by the drug. The proposed target in P. falciparum is the ribosome of the plastid-like organelle (35 kb c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::87c3b25b4a627d565155386e44ebb4b5
https://pubmed.ncbi.nlm.nih.gov/9257641
https://pubmed.ncbi.nlm.nih.gov/9257641
Autor:
D E, Draper
Publikováno v:
Trends in biochemical sciences. 21(4)
RNAs are surprisingly adept at folding into specific shapes capable of ligand recognition and catalysis. Thermodynamic analysis of the unfolding of several different RNAs suggests that there are at least three strategies an RNA might use to achieve a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7da898988062e6a226ce4d52c8c8df04
https://pubmed.ncbi.nlm.nih.gov/8701472
https://pubmed.ncbi.nlm.nih.gov/8701472