Sensitive Detection of Small Molecule–Protein Interactions on a Metal–Insulator–Metal Label‐Free Biosensing Platform

2012 ◽  
Vol 7 (8) ◽  
pp. 1867-1874 ◽  
Author(s):  
Amir Syahir ◽  
Kotaro Kajikawa ◽  
Hisakazu Mihara
2005 ◽  
Vol 102 (9) ◽  
pp. 3208-3212 ◽  
Author(s):  
W. U. Wang ◽  
C. Chen ◽  
K.-h. Lin ◽  
Y. Fang ◽  
C. M. Lieber

Langmuir ◽  
2010 ◽  
Vol 26 (8) ◽  
pp. 6053-6057 ◽  
Author(s):  
Amir Syahir ◽  
Hisakazu Mihara ◽  
Kotaro Kajikawa

The Analyst ◽  
2018 ◽  
Vol 143 (9) ◽  
pp. 2023-2028 ◽  
Author(s):  
Chang Yeol Lee ◽  
Hyo Yong Kim ◽  
Soeun Kim ◽  
Ki Soo Park ◽  
Hyun Gyu Park

A new strategy to detect a small molecule–protein interaction was devised based on terminal protection-mediated exponential strand displacement amplification (eSDA).


RSC Advances ◽  
2015 ◽  
Vol 5 (8) ◽  
pp. 6100-6105 ◽  
Author(s):  
Xue Gong ◽  
Wenjiao Zhou ◽  
Yaqin Chai ◽  
Yun Xiang ◽  
Ruo Yuan

Protection of ssDNA from digesting by Exo I generates amplified color transition for label-free and sensitive detection of folate receptors.


2011 ◽  
Vol 54 (8) ◽  
pp. 1277-1283 ◽  
Author(s):  
DianMing Zhou ◽  
YiDan Wu ◽  
Pei Liu ◽  
HaoTian Bai ◽  
LiJuan Tang ◽  
...  

2018 ◽  
Vol 122 (11) ◽  
pp. 6255-6266 ◽  
Author(s):  
Lisa P. Hackett ◽  
Wenyue Li ◽  
Abid Ameen ◽  
Lynford L. Goddard ◽  
Gang Logan Liu

2011 ◽  
Vol 16 (10) ◽  
pp. 1170-1185 ◽  
Author(s):  
Chun-wa Chung ◽  
Jason Witherington

Bromodomains are structurally conserved protein modules present in a large number of chromatin-associated proteins and in many nuclear histone acetyltransferases. The bromodomain functions as an acetyl-lysine binding domain and has been shown to be pivotal in regulating protein–protein interactions in chromatin-mediated cellular gene transcription, cell proliferation, and viral transcriptional activation. Structural analyses of these modules in complex with acetyl-lysine peptide ligands provide insights into the molecular basis for recognition and ligand selectivity within this epigenetic reader family. However, there are significant challenges in configuring assays to identify inhibitors of these proteins. This review focuses on the progress made in developing methods to identify peptidic and small-molecule ligands using biophysical label-free and biochemical approaches. The advantage of each technique and the results reported are summarized, highlighting the potential applicably to other reader domains and the caveats in translation from simple in vitro systems to a biological context.


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