Silver-functionalized g-C3N4 nanohybrids as signal-transduction tags for electrochemical immunoassay of human carbohydrate antigen 19-9

The Analyst ◽  
2016 ◽  
Vol 141 (14) ◽  
pp. 4366-4372 ◽  
Author(s):  
Ai-Li Sun ◽  
Qing-An Qi

A simple and feasible electrochemical immunosensing platform was developed for highly efficient screening of a disease-related protein (human carbohydrate antigen 19-9, CA 19-9 used in this case) using silver-functionalized g-C3N4 nanosheets (Ag/g-C3N4) as signal-transduction tags.

The Analyst ◽  
2015 ◽  
Vol 140 (23) ◽  
pp. 7948-7954 ◽  
Author(s):  
Ai-Li Sun

A new electrochemical immunosensor with signal enhancement was designed for sensitive detection of disease-related protein (human carbohydrate antigen 19-9, CA 19-9 used in this case).


2016 ◽  
Vol 8 (20) ◽  
pp. 4069-4074 ◽  
Author(s):  
Jiashi Lin ◽  
Dianping Tang

A simple and low-cost electrochemical immunosensing platform with a personal glucometer (PGM)-based signal readout device was developed for the quantitative detection of human carbohydrate antigen 125 (CA 125) using invertase for the hydrolysis of sucrose.


2021 ◽  
Author(s):  
Fangfang Ma ◽  
Gaoshun Ge ◽  
Yizhen Fang ◽  
Erru Ni ◽  
Yuanyuan Su ◽  
...  

Rapid and accurate identification of cardiac troponin I (cTnl) in biological fluids is very essential for judging acute myocardial infarction (AMI). Herein, we constructed an enzyme-free electrochemical immunosensing system for...


Blood ◽  
1997 ◽  
Vol 90 (9) ◽  
pp. 3507-3515 ◽  
Author(s):  
Jian-Feng Wang ◽  
Ramesh K. Ganju ◽  
Zhong-Ying Liu ◽  
Hava Avraham ◽  
Shalom Avraham ◽  
...  

Abstract We have recently identified a novel ligand of the vascular endothelial growth factor (VEGF) family termed VEGF-related protein (VRP), which specifically binds to the FLT4 receptor. To characterize the signaling events after VRP engagement of its cognate receptor in hematopoietic cells, a population of human erythroleukemia (HEL) cells, termed HEL-JW, expressing high levels of FLT4 receptor was isolated. Stimulation of HEL-JW cells with VRP alone and in combination with the c-kit ligand/stem cell factor increased cell growth. VRP induced tyrosine phosphorylation of various proteins, including the FLT4 receptor. Further characterization of these tyrosine phosphorylated molecules revealed that Shc, Grb2, and SOS form a complex with the activated FLT4 receptor. HEL-JW cells also expressed RAFTK, a recently identified member of the focal adhesion kinase family. RAFTK was phosphorylated and activated upon VRP treatment, and there was an enhanced association of this kinase with the adaptor protein Grb2. Furthermore, the c-Jun NH2-terminal kinase (JNK), involved in growth activation and shown to mediate RAFTK signaling in other cell types, was activated by VRP stimulation. We also observed that VRP treatment of HEL-JW cells resulted in the phosphorylation of the cytoskeletal protein paxillin. This treatment resulted in an increased association of paxillin with RAFTK, which was mediated by the C-terminal region of RAFTK. These studies indicate that VRP stimulation induced the formation of a signaling complex at its activated receptor as well as activation of RAFTK. VRP-mediated activation of RAFTK may facilitate signal transduction to the cytoskeleton and downstream to the JNK pathway in FLT4-expressing blood cells.


RSC Advances ◽  
2020 ◽  
Vol 10 (70) ◽  
pp. 42804-42809
Author(s):  
Xuelian Liu ◽  
Dongyan Yang ◽  
Fahong Yin ◽  
Jia-Qi Li ◽  
Yumei Xiao ◽  
...  

In this study, the “plug-in molecular” method was firstly used to screen new strobilurin fungicides. The results indicated this is a highly efficient screening method for active compounds with guiding significance for the synthesis of new pesticides.


2000 ◽  
Vol 20 (6) ◽  
pp. 2228-2238 ◽  
Author(s):  
Keiji Itoh ◽  
Alena Antipova ◽  
Marianne J. Ratcliffe ◽  
Sergei Sokol

ABSTRACT Signaling by the Wnt family of secreted proteins plays an important role in animal development and is often misregulated in carcinogenesis. Wnt signal transduction is controlled by the rate of degradation of β-catenin by a complex of proteins including glycogen synthase kinase 3 (GSK3), adenomatous polyposis coli, and Axin. Dishevelled is required for Wnt signal transduction, and its activation results in stabilization of β-catenin. However, the biochemical events underlying this process remain largely unclear. Here we show thatXenopus Dishevelled (Xdsh) interacts with aXenopus Axin-related protein (XARP). This interaction depends on the presence of the Dishevelled-Axin (DIX) domains in both XARP and Xdsh. Moreover, the same domains are essential for signal transduction through Xdsh. Finally, our data point to a possible mechanism for signal transduction, in which Xdsh prevents β-catenin degradation by displacing GSK3 from its complex with XARP.


PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e25602 ◽  
Author(s):  
Hamid Moha ou Maati ◽  
Rémi Peyronnet ◽  
Christelle Devader ◽  
Julie Veyssiere ◽  
Fabien Labbal ◽  
...  

1998 ◽  
Vol 95 (12) ◽  
pp. 6959-6964 ◽  
Author(s):  
J. Brockdorff ◽  
S. B. Kanner ◽  
M. Nielsen ◽  
N. Borregaard ◽  
C. Geisler ◽  
...  

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