| 1. |
- Ackelid, Ulf, et al.
(författare)
-
Ethanol sensitivity of palladium-gate metal-oxide-semiconductor structures
- 1986
-
Ingår i: IEEE Electron Device Letters. - : Institute of Electrical and Electronics Engineers (IEEE). - 0741-3106 .- 1558-0563. ; 7:6, s. 353-355
-
Tidskriftsartikel (refereegranskat)abstract
- Hydrogen-sensitive palladium-gate MOS structures heated above 150°C show sensitivity to ethanol vapor. The effect is probably due to catalytic dehydrogenation of adsorbed ethanol molecules on the surface of the palladium gate.
|
|
| 2. |
|
|
| 3. |
- Adén, Daniel, et al.
(författare)
-
A photometric and spectroscopic study of the new dwarf spheroidal galaxy in Hercules. Metallicity, velocities and a clean list of RGB members
- 2009
-
Ingår i: Astronomy & Astrophysics. - : EDP Sciences. - 0004-6361 .- 1432-0746. ; 506:3, s. 1147-1168
-
Tidskriftsartikel (refereegranskat)abstract
- Our aim is to provide as clean and as complete a sample as possible of red giant branch stars that are members of the Hercules dSph galaxy. With this sample we explore the velocity dispersion and the metallicity of the system. Stromgren photometry and multi-fibre spectroscopy are combined to provide information about the evolutionary state of the stars (via the Stromgren c_1 index) and their radial velocities. Based on this information we have selected a clean sample of red giant branch stars, and show that foreground contamination by Milky Way dwarf stars can greatly distort the results. Our final sample consists of 28 red giant branch stars in the Hercules dSph galaxy. Based on these stars we find a mean photometric metallicity of -2.35 dex which is consistent with previous studies. We find evidence for an abundance spread. Using those stars for which we have determined radial velocities we find a systemic velocity of 45.2 km/s with a dispersion of 3.72 km/s, this is lower than values found in the literature. Furthermore we identify the horizontal branch and estimate the mean magnitude of the horizontal branch of the Hercules dSph galaxy to be V_0=21.17, which corresponds to a distance of 147 kpc. We have shown that a proper cleaning of the sample results in a smaller value for the velocity dispersion of the system. This has implications for galaxy properties derived from such velocity dispersions.
|
|
| 4. |
- Aifa, Sami, 1967-, et al.
(författare)
-
A basic peptide within the juxtamembrane region is required for EGF receptor dimerization
- 2005
-
Ingår i: Experimental Cell Research. - : Elsevier BV. - 0014-4827 .- 1090-2422. ; 302:1, s. 108-114
-
Tidskriftsartikel (refereegranskat)abstract
- The epidermal growth factor receptor (EGFR) is fundamental for normal cell growth and organ development, but has also been implicated in various pathologies, notably tumors of epithelial origin. We have previously shown that the initial 13 amino acids (P13) within the intracellular juxtamembrane region (R645-R657) are involved in the interaction with calmodulin, thus indicating an important role for this region in EGFR function. Here we show that P13 is required for proper dimerization of the receptor. We expressed either the intracellular domain of EGFR (TKJM) or the intracellular domain lacking P13 (ΔTKJM) in COS-7 cells that express endogenous EGFR. Only TKJM was immunoprecipitated with an antibody directed against the extracellular part of EGFR, and only TKJM was tyrosine phosphorylated by endogenous EGFR. Using SK-N-MC cells, which do not express endogenous EGFR, that were stably transfected with either wild-type EGFR or recombinant full-length EGFR lacking P13 demonstrated that P13 is required for appropriate receptor dimerization. Furthermore, mutant EGFR lacking P13 failed to be autophosphorylated. P13 is rich in basic amino acids and in silico modeling of the EGFR in conjunction with our results suggests a novel role for the juxtamembrane domain (JM) of EGFR in mediating intracellular dimerization and thus receptor kinase activation and function. © 2004 Elsevier Inc. All rights reserved.
|
|
| 5. |
- Aifa, Sami, et al.
(författare)
-
Interactions between the juxtamembrane domain of the EGFR and calmodulin measured by surface plasmon resonance
- 2002
-
Ingår i: Cellular Signalling. - 0898-6568 .- 1873-3913. ; 14:12, s. 1005-1013
-
Tidskriftsartikel (refereegranskat)abstract
- One early response to epidermal growth factor receptor (EGFR) activation is an increase in intracellular calcium. We have used surface plasmon resonance (SPR) to study real-time interactions between the intracellular juxtamembrane (JM) region of EGFR and calmodulin. The EGFR-JM (Met644-Phe688) was expressed as a GST fusion protein and immobilised on a sensor chip surface. Calmodulin specifically interacts with EGFR-JM in a calcium-dependent manner with a high on and high off rate. Chemical modification of EGFR-JM by using arginine-selective phenylglyoxal or deletion of the basic segment Arg645-Arg657 inhibits the interaction. Phosphorylation of EGFR-JM by protein kinase C (PKC) or glutamate substitution of Thr654 inhibits the interaction, suggesting that PKC phosphorylation electrostatically interferes with calmodulin binding to basic arginine residues. Calmodulin binding was also inhibited by suramin. Our results suggest that EGFR-JM is essential for epidermal growth factor (EGF)-mediated calcium-calmodulin signalling and for signal integration between other signalling pathways.
|
|
| 6. |
- Aifa, Sami, et al.
(författare)
-
Phosphorylation of Thr654 but not Thr669 within the juxtamembrane domain of the EGF receptor inhibits calmodulin binding
- 2006
-
Ingår i: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 347:2, s. 381-387
-
Tidskriftsartikel (refereegranskat)abstract
- Calcium-calmodulin (CaM) binding to the epidermal growth factor receptor (EGFR) has been shown to both inhibit and stimulate receptor activity. CaM binds to the intracellular juxtamembrane (JM) domain (Met645-Phe688) of EGFR. Protein kinase C (PKC) mediated phosphorylation of Thr654 occurs within this domain. CaM binding to the JM domain inhibits PKC phosphorylation and conversely PKC mediated phosphorylation of Thr654 or Glu substitution of Thr654 inhibits CaM binding. A second threonine residue (Thr669) within the JM domain is phosphorylated by the mitogen-activated protein kinase (MAPK). Previous results have shown that CaM interferes with EGFR-induced MAPK activation. If and how phosphorylation of Thr669 affects CaM-EGFR interaction is however not known.In the present study we have used surface plasmon resonance (BIAcore) to study the influence of Thr669 phosphorylation on real time interactions between the intracellular juxtamembrane (JM) domain of EGFR and CaM. The EGFR-JM was expressed as GST fusion proteins in Escherichia coli and phosphorylation was mimicked by generating Glu substitutions of either Thr654 or Thr669. Purified proteins were coupled to immobilized anti-GST antibodies at the sensor surface and increasing concentration of CaM was applied. When mutating Thr654 to Glu654 no specific CaM binding could be detected. However, neither single substitutions of Thr669 (Gly669 or Glu669) nor double mutants Gly654/Gly669 or Gly654/Glu669 influenced the binding of CaM to the EGFR-JM. This clearly shows that PKC may regulate EGF-mediated CaM signalling through phosphorylation of Thr654 whereas phosphorylation of Thr669 seems to play a CaM independent regulatory role. The role of both residues in the EGFR-calmodulin interaction was also studied in silico. Our modelling work supports a scenario where Thr654 from the JM domain interacts with Glu120 in the calmodulin molecule. Phosphorylation of Thr654 or Glu654 substitution creates a repulsive electrostatic force that would diminish CaM binding to the JM domain. These results are in line with the Biacore experiments showing a weak binding of the CaM to the JM domain with Thr654 mutated to Glu. Furthermore, these results provide a hypothesis to how CaM binding to EGFR might both positively and negatively interfere with EGFR-activity. © 2006 Elsevier Inc. All rights reserved.
|
|
| 7. |
- Aili, Daniel, 1977-, et al.
(författare)
-
Aggregation-Induced Folding of a de novo Designed Polypeptide Immobilized on Gold Nanoparticles
- 2006
-
Ingår i: Journal of the American Chemical Society. - : ACS Publications. - 0002-7863 .- 1520-5126. ; 128:7, s. 2194 -2195
-
Tidskriftsartikel (refereegranskat)abstract
- This communication reports the first steps in the construction of a novel, nanoparticle-based hybrid material for biomimetic and biosensor applications. Gold nanoparticles were modified with synthetic polypeptides to enable control of the particle aggregation state in a switchable manner, and particle aggregation was, in turn, found to induce folding of the immobilized peptides.
|
|
| 8. |
|
|
| 9. |
|
|
| 10. |
|
|
