scholarly journals Melting studies of dangling-ended DNA hairpins: effects of end length, loop sequence and biotinylation of loop bases

2002 ◽  
Vol 30 (18) ◽  
pp. 4088-4093 ◽  
Author(s):  
P. V. Riccelli
Keyword(s):  
2021 ◽  
Vol 103 (6) ◽  
Author(s):  
Anurag Upadhyaya ◽  
Sanjay Kumar
Keyword(s):  

Biopolymers ◽  
1999 ◽  
Vol 50 (4) ◽  
pp. 425-442 ◽  
Author(s):  
Peter M. Vallone ◽  
Teodoro M. Paner ◽  
Jovencio Hilario ◽  
Michael J. Lane ◽  
Brian D. Faldasz ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Feng Li ◽  
Wenting Yu ◽  
Jiaojiao Zhang ◽  
Yuhang Dong ◽  
Xiaohui Ding ◽  
...  

AbstractDNA nanostructures have been demonstrated as promising carriers for gene delivery. In the carrier design, spatiotemporally programmable assembly of DNA under nanoconfinement is important but has proven highly challenging due to the complexity–scalability–error of DNA. Herein, a DNA nanotechnology-based strategy via the cascade hybridization chain reaction (HCR) of DNA hairpins in polymeric nanoframework has been developed to achieve spatiotemporally programmable assembly of DNA under nanoconfinement for precise siRNA delivery. The nanoframework is prepared via precipitation polymerization with Acrydite-DNA as cross-linker. The potential energy stored in the loops of DNA hairpins can overcome the steric effect in the nanoframework, which can help initiate cascade HCR of DNA hairpins and achieve efficient siRNA loading. The designer tethering sequence between DNA and RNA guarantees a triphosadenine triggered siRNA release specifically in cellular cytoplasm. Nanoframework provides stability and ease of functionalization, which helps address the complexity–scalability–error of DNA. It is exemplified that the phenylboronate installation on nanoframework enhanced cellular uptake and smoothed the lysosomal escape. Cellular results show that the siRNA loaded nanoframework down-regulated the levels of relevant mRNA and protein. In vivo experiments show significant therapeutic efficacy of using siPLK1 loaded nanoframework to suppress tumor growth.


2015 ◽  
Vol 13 (13) ◽  
pp. 4031-4040 ◽  
Author(s):  
David E. Thurston ◽  
Higia Vassoler ◽  
Paul J. M. Jackson ◽  
Colin H. James ◽  
Khondaker M. Rahman

Pyrrolobenzodiazepine (PBD) monomer GWL-78 reacts faster with DNA hairpins containing a hexaethylene glycol (HEG) loop compared to hairpins containing a TTT loop due to the greater structural flexibility of the HEG.


2018 ◽  
Vol 46 (2) ◽  
pp. 57-67 ◽  
Author(s):  
Moe LWIN ◽  
Su Lai Yee MON ◽  
Yukio NAGANO ◽  
Kotaro KAWABE ◽  
Hideyuki MANNEN ◽  
...  

1997 ◽  
Vol 273 (1) ◽  
pp. C257-C265 ◽  
Author(s):  
A. Ruknudin ◽  
C. Valdivia ◽  
P. Kofuji ◽  
W. J. Lederer ◽  
D. H. Schulze

cDNAs for the Na+/Ca2+ exchanger from Drosophila melanogaster (Dmel/Nck) have been cloned by homology screening using the human heart Na+/Ca2+ exchanger cDNA. The overall deduced protein structure for Dmel/Nck is similar to that of mammalian Na+/Ca2+ exchanger genes NCX1 and NCX2, having six hydrophobic regions in the amino terminus separated from six at the carboxy-terminal end by a large intracellular loop. Sequence comparison of the Drosophila exchanger cDNAs with NCX1 and NCX2 Na+/Ca2+ exchangers are approximately 46% identical at the deduced amino acid level. Consensus phosphorylation sites for both protein kinase C and protein kinase A are present on the intracellular loop region of the Dmel/Nck. Alternative splicing for the Dmel/Nck gene is suggested in the same intracellular loop region as demonstrated for NCX1. Functionally, the Drosophila Na+/ Ca2+ exchanger expressed in oocytes differs from expressed mammalian NCX1 with regard to Ca2+ transport in Ca2+/ Ca2+ exchange and the effect of monovalent-dependent Ca2+/ Ca2+ exchange. The Dmel/Nck gene maps to chromosome 3 (93A-B) using in situ hybridization to polytene chromosomes, the same position as the Na(+)-K(+)-ATPase, a related transporter. We conclude that, although extracellular Na+ concentration-dependent Ca2+ transport is subserved by both human and Drosophila Na+/Ca2+ exchangers, there are clear and important differences in the transporters, which should be useful in deducing how the Na+/Ca2+ exchanger protein function depends on its structure.


2013 ◽  
Vol 117 (50) ◽  
pp. 16105-16109 ◽  
Author(s):  
Roman Tsukanov ◽  
Toma E. Tomov ◽  
Yaron Berger ◽  
Miran Liber ◽  
Eyal Nir

Sign in / Sign up

Export Citation Format

Share Document