Ni–nitrilotriacetic acid-modified quantum dots as a site-specific labeling agent of histidine-tagged proteins in live cells

2008 ◽  
pp. 1910 ◽  
Author(s):  
Junwon Kim ◽  
Hye-Young Park ◽  
Jaeseung Kim ◽  
Jiyoung Ryu ◽  
Do Yoon Kwon ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Nitrilotriacetic Acid ◽  
Live Cells ◽  
Site Specific ◽  
A Site

PEG-interspersed nitrilotriacetic acid-functionalized quantum dots for site-specific labeling of prion proteins expressed on cell surfaces

Biomaterials ◽  
2010 ◽  
Vol 31 (32) ◽  
pp. 8362-8370 ◽  
Author(s):  
Min Xie ◽  
Kan Luo ◽  
Bi-Hai Huang ◽  
Shu-Lin Liu ◽  
Jun Hu ◽  
...  
Keyword(s):  
Quantum Dots ◽  
Prion Proteins ◽  
Nitrilotriacetic Acid ◽  
Cell Surfaces ◽  
Site Specific

scholarly journals Selected peptide-based fluorescent probes for biological applications

2020 ◽  
Vol 16 ◽  
pp. 2971-2982
Author(s):  
Debabrata Maity
Keyword(s):  
Fluorescent Probes ◽  
Direct Detection ◽  
Aqueous Media ◽  
Live Cells ◽  
Biological Applications ◽  
Site Specific ◽  
Specific Manner ◽  
Environmentally Sensitive ◽  
Living Organisms ◽  
A Site

To understand the molecular interactions, present in living organisms and their environments, chemists are trying to create novel chemical tools. In this regard, peptide-based fluorescence techniques have attracted immense interest. Synthetic peptide-based fluorescent probes are advantageous over protein-based sensors, since they are synthetically accessible, more stable, and can be easily modified in a site-specific manner for selective biological applications. Peptide receptors labeled with environmentally sensitive/FRET fluorophores have allowed direct detection/monitoring of biomolecules in aqueous media and in live cells. In this review, key peptide-based approaches for different biological applications are presented.

scholarly journals Time-lapse Imaging of Individual BKCa Channels in Live Cells Using Site-specific Labeling of Quantum Dots

2009 ◽  
Vol 96 (3) ◽  
pp. 35a
Author(s):  
Ji-Yeon Kim ◽  
Haedeun Kim ◽  
Sungho Chang ◽  
Chul-Seung Park
Keyword(s):  
Quantum Dots ◽  
Time Lapse ◽  
Live Cells ◽  
Bkca Channels ◽  
Site Specific ◽  
Time Lapse Imaging

scholarly journals Effects of Palmitoylation on the Movement of BKCA Channels In Live Cells using Site-Specific Labeling with Quantum Dots

2013 ◽  
Vol 104 (2) ◽  
pp. 474a
Author(s):  
Byoung-Cheol Lee ◽  
Sulgi Kim ◽  
Sehoon Won ◽  
A-Ram Lee ◽  
Chul-Seung Park
Keyword(s):  
Quantum Dots ◽  
Live Cells ◽  
Bkca Channels ◽  
Site Specific

scholarly journals Functional expression of a yeast mitochondrial intron-encoded protein requires RNA processing at a conserved dodecamer sequence at the 3' end of the gene.

1989 ◽  
Vol 9 (4) ◽  
pp. 1507-1512 ◽  
Author(s):  
H Zhu ◽  
H Conrad-Webb ◽  
X S Liao ◽  
P S Perlman ◽  
R A Butow
Keyword(s):  
Genetic Analysis ◽  
Rna Processing ◽  
Fold Increase ◽  
Functional Expression ◽  
Rrna Gene ◽  
Yeast Mitochondria ◽  
Wild Type ◽  
Site Specific ◽  
Var1 Gene ◽  
A Site

All mRNAs of yeast mitochondria are processed at their 3' ends within a conserved dodecamer sequence, 5'-AAUAAUAUUCUU-3'. A dominant nuclear suppressor, SUV3-I, was previously isolated because it suppresses a dodecamer deletion at the 3' end of the var1 gene. We have tested the effects of SUV3-1 on a mutant containing two adjacent transversions within a dodecamer at the 3' end of fit1, a gene located within the 1,143-base-pair intron of the 21S rRNA gene, whose product is a site-specific endonuclease required in crosses for the quantitative transmission of that intron to 21S alleles that lack it. The fit1 dodecamer mutations blocked both intron transmission and dodecamer cleavage, neither of which was suppressed by SUV3-1 when present in heterozygous or homozygous configurations. Unexpectedly, we found that SUV3-1 completely blocked cleavage of the wild-type fit1 dodecamer and, in SUV3-1 homozygous crosses, intron conversion. In addition, SUV3-1 resulted in at least a 40-fold increase in the amount of excised intron accumulated. Genetic analysis showed that these phenotypes resulted from the same mutation. We conclude that cleavage of a wild-type dodecamer sequence at the 3' end of the fit1 gene is essential for fit1 expression.

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