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Author |
Pilehvar, S.; Gielkens, K.; Trashin, S.A.; Dardenne, F.; Blust, R.; De Wael, K. |
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Title |
(Electro)sensing of phenicol antibiotics : a review |
Type |
A1 Journal article |
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Year  |
2016 |
Publication |
Critical reviews in food science and nutrition |
Abbreviated Journal |
Crit Rev Food Sci |
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Volume |
56 |
Issue |
14 |
Pages |
2416-2429 |
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Keywords |
A1 Journal article; Pharmacology. Therapy; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
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Abstract |
The presence of residues from frequent antibiotic use in animal feed can cause serious health risks by contaminating products for human consumption such as meat and milk. The present article gives an overview of the electrochemical methods developed for the detection of phenicol antibiotic residues (chloramphenicol, thiamphenicol, and florfenicol) in different kinds of foodstuffs. Electrochemical sensors based on different biomolecules and nanomaterials are described. The detection limit of various developed methods with their advantages and disadvantage will be highlighted. |
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Wos |
000382757200015 |
Publication Date |
2015-04-02 |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
1040-8398 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
6.077 |
Times cited |
13 |
Open Access |
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Notes |
; The authors are highly thankful for the University of Antwerp Grants (DOCPRO/ IWS). ; |
Approved |
Most recent IF: 6.077 |
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Call Number |
UA @ admin @ c:irua:125663 |
Serial |
5585 |
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Author |
De Henau, S.; Tilleman, L.; Vangheel, M.; Luyckx, E.; Trashin, S.; Pauwels, M.; Germani, F.; Vlaeminck, C.; Vanfleteren, J.R.; Bert, W.; Pesce, A.; Nardini, M.; Bolognesi, M.; De Wael, K.; Moens, L.; Dewilde, S.; Braeckman, B.P. |
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Title |
A redox signalling globin is essential for reproduction in Caenorhabditis elegans |
Type |
A1 Journal article |
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Year |
2015 |
Publication |
Nature communications |
Abbreviated Journal |
Nat Commun |
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Volume |
6 |
Issue |
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Pages |
8782 |
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Keywords |
A1 Journal article; Engineering sciences. Technology; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
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Abstract |
Moderate levels of reactive oxygen species (ROS) are now recognized as redox signalling molecules. However, thus far, only mitochondria and NADPH oxidases have been identified as cellular sources of ROS in signalling. Here we identify a globin (GLB-12) that produces superoxide, a type of ROS, which serves as an essential signal for reproduction in C. elegans. We find that GLB-12 has an important role in the regulation of multiple aspects in germline development, including germ cell apoptosis. We further describe how GLB-12 displays specific molecular, biochemical and structural properties that allow this globin to act as a superoxide generator. In addition, both an intra- and extracellular superoxide dismutase act as key partners of GLB-12 to create a transmembrane redox signal. Our results show that a globin can function as a driving factor in redox signalling, and how this signal is regulated at the subcellular level by multiple control layers. |
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Wos |
000367577100002 |
Publication Date |
2015-12-01 |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
2041-1723 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
12.124 |
Times cited |
20 |
Open Access |
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Notes |
; We thank Dr K. Matsumoto and Dr T. Mizuno for kindly providing the mek-1(ks54) sek-1(km4) double mutant, the antibody anti-PMK-1 and technical advice on antibody use; Dr D. Kim for kindly providing the pDK177 RNAi strain; Dr M. Ubbink and Dr Q. Bashir for providing CCP; Dr K. Oegema and the OD lab for sharing technical expertise; M. Couvreur for assistance in generating transgenic lines; and Dr T. Dansen for the final support. Some strains were provided by the CGC, which is funded by the NIH Office of Research Infrastructure Programs (P40 OD010440). S.D.H. and F.G. are PhD fellows of the Fund for Scientific Research (FWO). Financial support to S.D. and L.M. was provided by the University of Antwerp (BOF UA TOP 2006), to K.D.W., S.D. and S.T. by the University of Antwerp (BOF-GOA) and to S.D., L.M., B.P.B., by FWO project G.0247.09. ; |
Approved |
Most recent IF: 12.124; 2015 IF: 11.470 |
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Call Number |
UA @ admin @ c:irua:129310 |
Serial |
5809 |
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Author |
Vagin, M.Y.; Trashin, S.A.; Beloglazkina, E.K.; Majouga, A.G. |
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Title |
Direct reagentless detection of the affinity binding of recombinant His-tagged firefly luciferase with a nickel-modified gold electrode |
Type |
A1 Journal article |
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Year |
2015 |
Publication |
Mendeleev communications |
Abbreviated Journal |
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Volume |
25 |
Issue |
4 |
Pages |
290-292 |
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Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
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Abstract |
The direct reagentless electrochemical detection of recombinant firefly luciferase binding with a gold electrode modified with nickel complex of 1,16-di[4-(2,6-dihydroxycarbonyl)pyridyl]-1,16-dioxa-8,9-dithiahexadecane has been carried out. |
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Wos |
000360416600021 |
Publication Date |
2015-08-07 |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
0959-9436 |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
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Times cited |
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Open Access |
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Notes |
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Approved |
no |
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Call Number |
UA @ admin @ c:irua:127814 |
Serial |
7811 |
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Author |
Borhani, A.H.; Berghmans, H.; Trashin, S.; De Wael, K.; Fago, A.; Moens, L.; Habibi-Rezaei, M.; Dewilde, S. |
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Title |
Kinetic properties and heme pocket structure of two domains of the polymeric hemoglobin of Artemia in comparison with the native molecule |
Type |
A1 Journal article |
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Year |
2015 |
Publication |
Biochimica et biophysica acta : proteins and proteomics |
Abbreviated Journal |
Bba-Proteins Proteom |
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Volume |
1854 |
Issue |
10a |
Pages |
1307-1316 |
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Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
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Abstract |
In this project, we studied some physicochemical properties of two different globin domains of the polymeric hemoglobin of the brine shrimp Artemia salina and compared them with those of the native molecule. Two domains (AsHbC1D1 and AsHbC1D5) were cloned and expressed in BL21(DE3)pLysS strain of Escherichiacoli. The recombinant proteins as well as the native hemoglobin (AfHb) were purified from bacteria and frozen Artemia, respectively by standard chromatographic methods and assessed by SDS-PAGE. The heme environment of these proteins was studied by optical spectroscopy and ligand-binding kinetics (e.g. CO association and O2 binding affinity) were measured for the two recombinant proteins and the native hemoglobin. This indicates that the CO association rate for AsHbC1D1 is higher than that of AsHbC1D5 and AfHb, while the calculated P50 value for AsHbC1D1 is lower than that of AsHbC1D5 and AfHb. The geminate and bimolecular rebinding parameters indicate a significant difference between both domains. Moreover, EPR results showed that the heme pocket in AfHb is in a more closed conformation than the heme pocket in myoglobin. Finally, the reduction potential of − 0.13 V versus the standard hydrogen electrode was determined for AfHb by direct electrochemical measurements. It is about 0.06 V higher than the potential of the single domain AsHbC1D5. This work shows that each domain in the hemoglobin of Artemia has different characteristics of ligand binding. |
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Wos |
000362307500008 |
Publication Date |
2015-05-22 |
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Series Editor |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
1570-9639 |
ISBN |
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Additional Links |
UA library record; WoS full record |
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Impact Factor |
2.773 |
Times cited |
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Open Access |
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Notes |
; This work was supported by the general grant for visiting scholar of the Ministry of Science, Research and Technology of I. R. Iran and by the University of Antwerp. ; |
Approved |
Most recent IF: 2.773; 2015 IF: 2.747 |
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Call Number |
UA @ admin @ c:irua:125909 |
Serial |
5683 |
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Author |
Trashin, S.; De Jong, M.; Breugelmans, T.; Pilehvar, S.; De Wael, K. |
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Title |
Label-free impedance aptasensor for major peanut allergen Ara h 1 |
Type |
A1 Journal article |
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Year |
2015 |
Publication |
Electroanalysis |
Abbreviated Journal |
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Volume |
27 |
Issue |
1 |
Pages |
32-37 |
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Keywords |
A1 Journal article; Engineering sciences. Technology; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation); Applied Electrochemistry & Catalysis (ELCAT) |
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Abstract |
The peanut allergen Ara h 1 belonging to the vicilin family of seed storage proteins is known to be a suitable marker for peanut detection in foods. In the present work, we suggest an electrochemical detection of Ara h 1 using a recently selected 80-base DNA aptamer. The detection strategy relies on insulation effect of a bulky protein captured by an immobilized aptamer. The electrodes were modified by the aptamer and characterized using electrochemical impedance spectroscopy (EIS). The aptamer surface density and analytical parameters of the calibration curves for Ara h 1 were compared with the system prepared with thrombin binding aptamer (TBA) and operated in the same conditions. |
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Wos |
000347838300004 |
Publication Date |
2014-10-13 |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
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Times cited |
10 |
Open Access |
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Notes |
; ST greatly appreciates the Research Council University of Antwerp (IWS BOF UA) for funding the post-doctoral fellowship. ; |
Approved |
Most recent IF: NA |
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Call Number |
UA @ admin @ c:irua:119442 |
Serial |
5686 |
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Author |
Anaf, W.; Trashin, S.; Schalm, O.; van Dorp, D.; Janssens, K.; De Wael, K. |
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Title |
Electrochemical photodegradation study of semiconductor pigments : influence of environmental parameters |
Type |
A1 Journal article |
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Year |
2014 |
Publication |
Analytical chemistry |
Abbreviated Journal |
Anal Chem |
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Volume |
86 |
Issue |
19 |
Pages |
9742-9748 |
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Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation); Antwerp Cultural Heritage Sciences (ARCHES) |
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Abstract |
Chemical transformations in paintings often induce discolorations, disturbing the appearance of the image. For an appropriate conservation of such valuable and irreplaceable heritage objects, it is important to have a good know-how on the degradation processes of the (historical) materials: which pigments have been discolored, what are the responsible processes, and which (environmental) conditions have the highest impact on the pigment degradation and should be mitigated. Pigment degradation is already widely studied, either by analyzing historical samples or by accelerated weathering experiments on dummies. However, in historic samples several processes may have taken place, increasing the complexity of the current state, while aging experiments are time-consuming due to the often extended aging period. An alternative method is proposed for a fast monitoring of degradation processes of semiconductor pigments, using an electrochemical setup mimicking the real environment and allowing the identification of harmful environmental parameters for each pigment. Examples are given for the pigments cadmium yellow (CdS) and vermilion (α-HgS). |
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Wos |
000343017100058 |
Publication Date |
2014-08-27 |
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Series Editor |
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Series Title |
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Abbreviated Series Title |
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Series Volume |
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Series Issue |
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Edition |
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ISSN |
0003-2700; 5206-882x |
ISBN |
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Additional Links |
UA library record; WoS full record; WoS citing articles |
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Impact Factor |
6.32 |
Times cited |
18 |
Open Access |
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Notes |
; ; |
Approved |
Most recent IF: 6.32; 2014 IF: 5.636 |
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Call Number |
UA @ admin @ c:irua:118834 |
Serial |
5593 |
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