| 1. |
- Santangelo, James S., et al.
(författare)
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Global urban environmental change drives adaptation in white clover
- 2022
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Ingår i: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 375
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Tidskriftsartikel (refereegranskat)abstract
- Urbanization transforms environments in ways that alter biological evolution. We examined whether urban environmental change drives parallel evolution by sampling 110,019 white clover plants from 6169 populations in 160 cities globally. Plants were assayed for a Mendelian antiherbivore defense that also affects tolerance to abiotic stressors. Urban-rural gradients were associated with the evolution of clines in defense in 47% of cities throughout the world. Variation in the strength of clines was explained by environmental changes in drought stress and vegetation cover that varied among cities. Sequencing 2074 genomes from 26 cities revealed that the evolution of urban-rural dines was best explained by adaptive evolution, but the degree of parallel adaptation varied among cities. Our results demonstrate that urbanization leads to adaptation at a global scale.
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| 2. |
- Chan, K, et al.
(författare)
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eIF4A supports an oncogenic translation program in pancreatic ductal adenocarcinoma
- 2019
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Ingår i: Nature communications. - : Springer Science and Business Media LLC. - 2041-1723. ; 10:1, s. 5151-
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Tidskriftsartikel (refereegranskat)abstract
- Pancreatic ductal adenocarcinoma (PDA) is a lethal malignancy with limited treatment options. Although metabolic reprogramming is a hallmark of many cancers, including PDA, previous attempts to target metabolic changes therapeutically have been stymied by drug toxicity and tumour cell plasticity. Here, we show that PDA cells engage an eIF4F-dependent translation program that supports redox and central carbon metabolism. Inhibition of the eIF4F subunit, eIF4A, using the synthetic rocaglate CR-1-31-B (CR-31) reduced the viability of PDA organoids relative to their normal counterparts. In vivo, CR-31 suppresses tumour growth and extends survival of genetically-engineered murine models of PDA. Surprisingly, inhibition of eIF4A also induces glutamine reductive carboxylation. As a consequence, combined targeting of eIF4A and glutaminase activity more effectively inhibits PDA cell growth both in vitro and in vivo. Overall, our work demonstrates the importance of eIF4A in translational control of pancreatic tumour metabolism and as a therapeutic target against PDA.
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| 3. |
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| 4. |
- Burestedt, E., et al.
(författare)
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Optimisation and validation of an automated solid phase extraction technique coupled on-line to enzyme-based biosensor detection for the determination of phenolic compounds in surface water samples
- 1995
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Ingår i: Chromatographia. - Heidelberg : Springer Berlin/Heidelberg. - 0009-5893 .- 1612-1112. ; 41:3-4, s. 207-215
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Tidskriftsartikel (refereegranskat)abstract
- A fully integrated screening system for phenolic compounds was developed incorporating on-line solid phase extraction, fractionation and biosensor detection. Two different types of biosensors, solid graphite and carbon paste electrodes incorporating the enzyme tyrosinase, were compared and used in the screening system. Interfacing of the solid phase extraction and fractionation with the biosensor detection was given special attention since the biosensors were not compatible with the organic modifier used for desorption of phenols from the solid phase extraction step. The system was validated with conventional analytical techniques. Surface water samples from the Ebro river were spiked with 1,10, and 25μg L−1 of catechol, phenol,p-cresol, respectively. Three out of seven samples were spiked and the correct samples were identified, containing phenols equivalent to the spiked concentrations. © 1995 Friedr. Vieweg & Sohn Verlagsgesellschaft mbH.
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| 5. |
- Christenson, Andreas, et al.
(författare)
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Direct electron transfer between ligninolytic redox enzymes and electrodes
- 2004
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Ingår i: Electroanalysis. - : Wiley. - 1040-0397 .- 1521-4109. ; 16:13-14, s. 1074-1092
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Forskningsöversikt (refereegranskat)abstract
- The electrochemistry of the ligninolytic redox enzymes, which include lignin peroxidase, manganese peroxidase and laccase and possibly also cellobiose dehydrogenase, is reviewed and discussed in conjunction with their basic biochemical characteristics. It is shown that long-range electron transfer between these enzymes and electrodes can be established and their ability to degrade lignin through a direct electron transfer mechanism is discussed.
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| 6. |
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| 7. |
- Ferapontova, Elena, et al.
(författare)
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Direct electrochemistry of proteins and enzymes
- 2005
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Ingår i: Electrochemistry of nucleic acids and proteins : towards electrochemical sensors for genomic and proteomics. - 044452150X
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Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
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| 8. |
- Haghighi, Behzad, et al.
(författare)
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Prussian blue modified glassy carbon electrodes - Study on operational stability and its application as a sucrose biosensor
- 2004
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Ingår i: Talanta. - : Elsevier BV. - 1873-3573 .- 0039-9140. ; 64:1, s. 3-12
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Tidskriftsartikel (refereegranskat)abstract
- Stabilisation of electrochemically deposited Prussian blue (PB) films on glassy carbon (GC) electrodes has been investigated and an enhancement in the stability of the PB films is reported if the electrodes are treated with tetrabutyl ammonium toluene-4-sulfonate (TTS) in the electrochemical activation step following the electrodeposition. A multi-enzyme PB based biosensor for sucrose detection was made in order to demonstrate that PB films can be coupled with an oxidase system. A tri-enzyme system, comprising glucose oxidase, mutarotase and invertase, was crosslinked with glutaraldehyde and bovine albumin serum on the PB modified glassy carbon electrode. The deposited PB operated as an electrocatalyst for electrochemical reduction of hydrogen peroxide, the final product of the enzyme reaction sequence. The electrochemical response was studied using flow injection analysis for the determination of sucrose, glucose and H2O2. The optimal concentrations of the immobilisation mixture was standardised as 8 U of glucose oxidase, 8 U of mutarotase, 16 U of invertase, 0.5% glutaraldchyde (0.025 mul) and 0.5 % BSA (0.025 mg) in a final volume of 5 mul applied at the electrode surface (0.066 cm(2)). The biosensor exhibited a linear response for sucrose (4-800 muM), glucose (2-800 muM) and H2O2 (1-800 muM) and the detection limit was 4.5, 1.5 and 0.5 muM for sucrose, glucose and H2O2, respectively. The sample throughput was ca. 60 samples h(-1). An increase in the operational and storage stability of the sucrose biosensor was also noted when the PB modified electrodes were conditioned in phosphate buffer containing 0.05 M TTS during the preparation of the PB films. (C) 2004 Elsevier B.V. All rights reserved.
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| 9. |
- Ma, Su, et al.
(författare)
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Direct Electron-Transfer Anisotropy of a Site-Specifically Immobilized Cellobiose Dehydrogenase
- 2019
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Ingår i: ACS Catalysis. - : American Chemical Society (ACS). - 2155-5435. ; , s. 7607-7615
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Tidskriftsartikel (refereegranskat)abstract
- To study the direct electron transfer (DET) of the multicofactor enzyme cellobiose dehydrogenase (CDH) in regard to its orientation on an electrode surface, a recently published, maleimide-based immobilization method was used in combination with site-directed mutagenesis to establish different orientations on an electrode surface. CDH from Myriococcum thermophilum was chosen for this study because its protein structure is resolved and the factors influencing the movement of its mobile cytochrome domain (CYT) are established. Seven CDH variants with a surface-exposed cysteine residue in different spatial positions were generated for site-specific maleimide coupling. Surface plasmon resonance and cyclic voltammetry showed that all CDH variants, but not the wild-type CDH, bound covalently to gold electrodes or glassy carbon electrodes and were catalytically active. For DET, the CYT domain needs to move from the closed-state conformation, where it obtains an electron from the catalytic flavin adenine dinucleotide (FAD) cofactor to the open state where it can donate an electron to the electrode. We therefore hypothesized that the mobility of the CYT domain and its distance to the electrode is central for DET. We found that the uniform spatial orientations of CDH influenced DET as follows: an orientation of the two-domain enzyme on the side, with CYT in proximity to the electrode, resulted in high DET currents. Orientations with a bigger distance between CYT and the electrode, or orientations where CYT could not swing back to the dehydrogenase domain to form the closed enzyme conformation, reduced DET. In the latter case, calcium ions that stabilize the closed conformation of CDH fully recovered DET. The study demonstrates that a mobile CYT domain can compensate unfavorable orientations of the catalytic domain to a great extent and allows CDH as a multicofactor enzyme to transfer electrons even in awkward orientations. The mobile CYT domain reduces the anisotropy of DET, which is also essential for CDH's physiological function as an extracellular, electron-transferring enzyme.
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| 10. |
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| 11. |
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| 12. |
- Nilvebrant, N.-O., et al.
(författare)
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Limits for alkaline detoxification of dilute-acid lignocellulose hydrolysates
- 2003
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Ingår i: Applied Biochemistry and Biotechnology. - 1559-0291. ; 107:1-3, s. 615-628
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Tidskriftsartikel (refereegranskat)abstract
- In addition to fermentable sugars, dilute-acid hydrolysates of lignocellulose contain compounds that inhibit fermenting microorganisms, such as Saccharomyces cerevisiae. Previous results show that phenolic compounds and furan aldehydes, and to some extent aliphatic acids, act as inhibitors during fermentation of dilute-acid hydrolysates of spruce. Treatment of lignocellulose hydrolysates with alkali, usually in the form of overliming to pH 10.0, has been frequently employed as a detoxification method to improve fermentability. A spruce dilute-acid hydrolysate was treated with NaOH in a factorial design experiment, in which the pH was varied between 9.0 and 12.0, the temperature between 5 and 80°C, and the time between 1 and 7 h. Already at pH 9.0, >25% of the glucose was lost when the hydrolysate was treated at 80°C for 1 h. Among the monosaccharides, xylose was degraded faster under alkaline conditions than the hexoses (glucose, mannose, and galactose), which, in turn, were degraded faster than arabinose. The results suggest that alkali treatment of hydrolysates can be performed at temperatures below 30°C at any pH between 9.0 and 12.0 without problems with sugar degradation or formation of inhibiting aliphatic acids. Treatment with Ca(OH)2 instead of NaOH resulted in more substantial degradation of sugars. Under the harsher conditions of the factorial design experiment, the concentrations of furfural and 5-hydroxymethylfurfural decreased while the total phenolic content increased. The latter phenomenon was tentatively attributed to fragmentation of soluble aromatic oligomers in the hydrolysate. Separate phenolic compounds were affected in different ways by the alkaline conditions with some compounds showing an increase in concentration while others decreased. In conclusion, the conditions used for detoxification with alkali should be carefully controlled to optimize the positive effects and minimize the degradation of fermentable sugars.
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| 13. |
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| 14. |
- Ricci, F, et al.
(författare)
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Electroanalytical study of Prussian Blue modified glassy carbon paste electrodes
- 2003
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Ingår i: Electroanalysis. - : Wiley. - 1040-0397 .- 1521-4109. ; 15:14, s. 1204-1211
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Tidskriftsartikel (refereegranskat)abstract
- Two types of glassy carbon (GC) powder (i.e., Sigradur K and Sigradur G) have been mixed with mineral oil to obtain glassy carbon paste electrodes (GCPE's). The electrochemical behavior of such electrodes at different percentages of glassy carbon has been evaluated with respect to the electrochemistry of ferricyanide as revealed with cyclic voltammetry and the best paste composition was chosen. GC was then modified with Prussian Blue (PB), mixed at different percentages with unmodified GC and with a fixed amount of mineral oil in order to obtain PB modified glassy carbon paste electrodes (PB-GCPE's). PB-GCPE's with different percentages of GC modified with PB (PB-GC) were compared and the dependence on the amount of PB on their performances was evaluated by studying the parameters of cyclic voltammetry (i.e., current peak, Ep, anodic and cathodic current ratio, charge density) and the amperometric response to H2O2. Data interpretation based on the GC surface area is presented. GCPE's with a selected amount of PB-GC were then tested as H2O2 probes and all the analytical parameters together with the dependence on pH were evaluated. Some preliminary experiments with these electrodes assembled as glucose, lysine and lactate biosensors are also reported.
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| 15. |
- Ricci, F, et al.
(författare)
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Investigation of the effect of different glassy carbon materials on the performance of Prussian blue based sensors for hydrogen peroxide
- 2003
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Ingår i: Electroanalysis. - : Wiley. - 1040-0397 .- 1521-4109. ; 15:3, s. 175-182
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Tidskriftsartikel (refereegranskat)abstract
- Three different kinds of glassy carbon (GC-R, GC-K, GC-G) were equally pretreated, further modified with electrochemically deposited Prussian Blue and used as sensors for hydrogen peroxide at an applied potential of -50 mV (vs. Ag|AgCl). Their performance was evaluated with respect to the following parameters: the coverage and electrochemistry of the electrodeposited Prussian Blue, the sensitivity and the lower limit of detection for hydrogen peroxide, and the operational stability of the sensors. GC-R showed the best behavior concerning the surface coverage and the operational stability of the electrodeposited Prussian Blue. For this electrode the sensitivity for hydrogen peroxide (10 M) was 0.25 A/M cm2 and the detection limit was 0.1 M. Scanning electron microscopy was used to study the surfaces of the three electrodes before and after the electrodeposition of Prussian Blue and to search for the reason for the three different behaviors between the different glassy carbon materials. The Prussian Blue modified GC-R was also used for the construction of a glucose biosensor based on immobilizing glucose oxidase in Nafion membranes on top of electrodeposited Prussian Blue layer. The operational stability of the glucose biosensors was studied in the flow injection mode at an applied potential of -50 mV (vs. Ag|AgCl) and alternatively injecting standard solutions of hydrogen peroxide (10 M) and glucose (1 mM) for 3 h. For the GC-R based biosensor a 2.8% decrease of the initial glucose response was observed.
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| 16. |
- Torabi, F., et al.
(författare)
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Coulometric determination of NAD+ and NADH in normal and cancer cells using LDH, RVC and a polymer mediator
- 1999
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Ingår i: Talanta. - 1873-3573. ; 50:4, s. 787-797
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Tidskriftsartikel (refereegranskat)abstract
- An electrochemical method for the measurement of NAD(+) and NADH in normal and cancer tissues using flow injection analysis (FIA) is reported. Reticulated vitreous carbon (RVC) electrodes with entrapped L-lactate dehydrogenase (LDH) and a new redox polymer containing covalently bound toluidine blue O (TBO) were employed for this purpose. Both NAD(+) and NADH were estimated coulometrically based on their reaction with LDH. The latter was immobilized on controlled pore glass (CPG) by cross-linking with glutaraldehyde and packed within the RVC. The concentrations of NAD(+) and NADH in the tissues, estimated using different electron mediators such as ferricyanide (FCN), meldola blue (MB) and TBO have also been compared. The effects of flow rate, pH, applied potential (versus Ag/AgCl reference) and adsorption of the mediators have also been investigated. Based bn the measurements of NAD(+) and NADH in normal and cancer tissues it has been concluded that the NADH concentration is lower, while the NAD(+) concentration is higher in cancer tissues. Amongst the electron mediators TBO was found to be a more stable mediator for such measurements. (C) 1999 Elsevier Science B.V. All rights reserved.
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